|
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 ... |
24-486 |
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: 1043.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 24 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDILRTPVSED 103
Cdd:TIGR01040 2 YRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 104 MLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 183
Cdd:TIGR01040 82 MLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 184 CRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 263
Cdd:TIGR01040 162 CRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 264 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 343
Cdd:TIGR01040 242 AYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 344 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALT 423
Cdd:TIGR01040 322 PDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALS 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1060139778 424 PDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFPKEMLKRIPASILAEFYPRDS 486
Cdd:TIGR01040 402 SEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKS 464
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
24-484 |
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: 857.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 24 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDILRTPVSED 103
Cdd:COG1156 6 YRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELPVSED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 104 MLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 183
Cdd:COG1156 86 MLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 184 CRQAglvKLPGKSvlddhtDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 263
Cdd:COG1156 166 ARQA---KVRGEE------EKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 264 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 343
Cdd:COG1156 237 AFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDITHPI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 344 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALT 423
Cdd:COG1156 317 PDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEEALS 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060139778 424 PDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFPKEMLKRIPASILAEFYPR 484
Cdd:COG1156 397 ETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPK 457
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
24-485 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 824.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 24 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDILRTPVSED 103
Cdd:PRK04196 4 YRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 104 MLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 183
Cdd:PRK04196 84 MLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 184 CRQAglvKLPGKSvlddhtDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 263
Cdd:PRK04196 164 ARQA---KVLGEE------ENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 264 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 343
Cdd:PRK04196 235 AFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 344 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALT 423
Cdd:PRK04196 315 PDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1060139778 424 PDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFPKEMLKRIPASILAEFYPRD 485
Cdd:PRK04196 395 ERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKY 456
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
24-485 |
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: 704.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 24 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDILRTPVSED 103
Cdd:TIGR01041 2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 104 MLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 183
Cdd:TIGR01041 82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 184 CRQAglvKLPGKSvlddhtDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 263
Cdd:TIGR01041 162 ARQA---TVRGEE------SEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 264 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 343
Cdd:TIGR01041 233 AFEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 344 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALT 423
Cdd:TIGR01041 313 PDLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1060139778 424 PDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFPKEMLKRIPASILAEFYPRD 485
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 ... |
95-385 |
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: 626.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 95 ILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGL 174
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 175 PHNEIAAQICRQAGLVKlpgksvlddHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPR 254
Cdd:cd01135 81 PHNELAAQIARQAGVVG---------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 255 LALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTM 334
Cdd:cd01135 152 MALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1060139778 335 PNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIG 385
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
24-488 |
6.55e-120 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 358.19 E-value: 6.55e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 24 YKTVSGVNGPLVILdEVKFPKFAEIVQLRLADGTvRSGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDILRTPVSED 103
Cdd:PRK02118 5 YTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGI-STGDEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 104 MLGRVFNGSGKPIDKGPpILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 183
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGP-ELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 184 CRQAglvklpgksvlddhtDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 263
Cdd:PRK02118 161 ALQA---------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 264 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITHPI 343
Cdd:PRK02118 226 ALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHPV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 344 PDLTGYITEGQIYvdrqLHNRQIYPpvnvLPSLSRLMKSAIGEgMTRKDHSDVSN---QLYACYAIGKDVQAMkavvGEE 420
Cdd:PRK02118 305 PDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GFK 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 421 aLTPDDLLYLEFLTKFEKNFISQGnyENRTVFESLDIGWQLL-RIF-PKEMLkrIPASILAEFYPRDSRH 488
Cdd:PRK02118 372 -LSNWDEKLLKFSELFESRLMDLE--VNIPLEEALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKNCLH 436
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
150-377 |
1.00e-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: 323.92 E-value: 1.00e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 150 GISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklpgksvLDDhtdnfAIVFAAMGVNMETARFFKQDFEEN 229
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA----------SAD-----VVVYALIGERGREVREFIEELLGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 230 GSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDL 309
Cdd:pfam00006 66 GALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060139778 310 ATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLS 377
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 ... |
97-379 |
1.20e-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: 320.94 E-value: 1.20e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 97 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH 176
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 177 NEIAAQICRQAGlvklpgksvlddHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLA 256
Cdd:cd19476 81 TVLAMQLARNQA------------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 257 LTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPN 336
Cdd:cd19476 149 LTIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1060139778 337 DDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 379
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 ... |
387-481 |
4.57e-62 |
|
V/A-type ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the V1/A1 complexes of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 349747 [Multi-domain] Cd Length: 95 Bit Score: 197.27 E-value: 4.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 387 GMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLEFLTKFEKNFISQGNYENRTVFESLDIGWQLLRIFP 466
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 1060139778 467 KEMLKRIPASILAEF 481
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
97-379 |
1.60e-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: 159.65 E-value: 1.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 97 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLph 176
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 177 neiaaqicrqaglvklpGKSVL----DDHTDNFAIVFAAMGvnmETAR----FFKQDFEENGsMENVCLFLNLANDPTIE 248
Cdd:cd01136 79 -----------------GKSTLlgmiARNTDADVNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 249 RIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQ 328
Cdd:cd01136 138 RVRAAYTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1060139778 329 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 379
Cdd:cd01136 215 FYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
26-380 |
1.84e-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: 155.96 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 26 TVSGVNGPLVildEVKFPKFA--EIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDILRTPVSED 103
Cdd:COG1157 22 RVTRVVGLLI---EAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 104 MLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSR--IypEEMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaa 181
Cdd:COG1157 98 LLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSG-------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 182 qicrqaglVklpGKSVL----DDHTDNFAIVFAAMGvnmETAR----FFKQDFEENGsMENVCLFLNLANDPTIERIITP 253
Cdd:COG1157 168 --------V---GKSTLlgmiARNTEADVNVIALIG---ERGRevreFIEDDLGEEG-LARSVVVVATSDEPPLMRLRAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 254 RLALTAAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQI- 329
Cdd:COG1157 233 YTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAFy 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1060139778 330 PILTmPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 380
Cdd:COG1157 307 TVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
92-383 |
8.87e-40 |
|
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: 150.23 E-value: 8.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 92 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 171
Cdd:TIGR00962 90 TGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 172 aglphneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERII 251
Cdd:TIGR00962 170 -------------RQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 252 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRNGSI 326
Cdd:TIGR00962 237 APYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSL 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1060139778 327 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSA 383
Cdd:TIGR00962 313 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-462 |
1.41e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 148.42 E-value: 1.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 62 QVLEVSGSKAVVQVFEGTSGIDAkNTLCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPiLAEDFLDIQGQPINPWSRI 141
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRC-GQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 142 YPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICrqaglvklpgksvldDHTDNFAIVFAAMGV-NMETAR 220
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC---------------ADSAADVMVLALIGErGREVRE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 221 FFKQDFEENGSMENVcLFLNLANDPTIERIITPRLALTAAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRG 300
Cdd:PRK06820 207 FLEQVLTPEARARTV-VVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 301 FPGYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 380
Cdd:PRK06820 285 FPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 381 KSAIGEGmtRKDHSDVSNQLYACYaigKDVQAMKAVvgEEALTPDDLLYLEFLTKFE--KNFISQGNYENRTVFESLDIG 458
Cdd:PRK06820 363 PQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEHL 435
|
....
gi 1060139778 459 WQLL 462
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 ... |
24-94 |
3.34e-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: 3.34e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060139778 24 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGD 94
Cdd:cd18118 2 YRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
44-411 |
7.81e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 143.74 E-value: 7.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 44 KFAEIVQLRLADGTVR-SGQVLEVSGSKAVVQVFEGTSGIDAkNTLCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPI 122
Cdd:PRK06936 43 RIGELCYLRNPDNSLSlQAEVIGFAQHQALLTPLGEMYGISS-NTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 123 LAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRqaglvklpgksvlddHT 202
Cdd:PRK06936 122 EPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIR---------------SA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 203 DNFAIVFAAMGV-NMETARFFKQDFEENGsMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSY 281
Cdd:PRK06936 187 EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRF 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 282 AEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQL 361
Cdd:PRK06936 265 ARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKL 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1060139778 362 HNRQIYPPVNVLPSLSRLMKSAIGegmtrKDHSDVSNQLYACYAIGKDVQ 411
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 ... |
95-378 |
1.08e-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: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 95 ILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAagl 174
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 175 phneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPR 254
Cdd:cd01132 78 ----------RQTGKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 255 LALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRNGSITQI 329
Cdd:cd01132 148 AGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1060139778 330 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 378
Cdd:cd01132 224 PIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
96-386 |
9.66e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 132.12 E-value: 9.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 96 LRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLP 175
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 176 HNEIAAQICRQAglvKLPGKsvlddhtdnfaiVFAAMGvnmETARFFKQDFEEN--GSMENVCLFLNLANDPTIERIITP 253
Cdd:PRK08472 170 KSTLMGMIVKGC---LAPIK------------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 254 RLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRnGSITQIPILT 333
Cdd:PRK08472 232 FCAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVL 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1060139778 334 MPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGE 386
Cdd:PRK08472 310 VEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
16-383 |
7.81e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 129.73 E-value: 7.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 16 AVSLVSAAYKTVSGVngplvildeVKFPKFAEIVQLRLADGTVRsGQVLEVSGSKAVVQVFEgtSGIDAKNTLCEFTGDI 95
Cdd:PRK06002 29 TVSEVTASHYRVRGL---------SRFVRLGDFVAIRADGGTHL-GEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 96 LRTPVSEDMLGRVFNGSGKPID-KGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGL 174
Cdd:PRK06002 97 LRIRPDPSWKGRVINALGEPIDgLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 175 phneiaaqicrqaglvklpGKSVL------DDHTDnfAIVFAAMGvnmETARFFKQDFEEN--GSMENVCLFLNLANDPT 246
Cdd:PRK06002 177 -------------------GKSTLlamlarADAFD--TVVIALVG---ERGREVREFLEDTlaDNLKKAVAVVATSDESP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 247 IERIITPRLALTAAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSI 326
Cdd:PRK06002 233 MMRRLAPLTATAIAEYFRDRGEN-VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSI 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1060139778 327 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSA 383
Cdd:PRK06002 312 TGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
94-466 |
3.07e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 128.31 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 94 DILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAG 173
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 174 LphneiaaqicrqaglvklpGKSVLDDHTDNFA----IVFAAMGV-NMETARFFKQDFEENGSMENVCLfLNLANDPTIE 248
Cdd:PRK05688 179 V-------------------GKSVLLGMMTRFTeadiIVVGLIGErGREVKEFIEHILGEEGLKRSVVV-ASPADDAPLM 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 249 RIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQ 328
Cdd:PRK05688 239 RLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 329 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIG-EGMTRKDHsdvSNQLYACYAIG 407
Cdd:PRK05688 318 FYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQS 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1060139778 408 KDVQAMKAVVgeEALTPDDLLYLEFLTKFEKnFISQGNYENRTVFESLDigwQLLRIFP 466
Cdd:PRK05688 395 RDLISVGAYV--AGGDPETDLAIARFPHLVQ-FLRQGLRENVSLAQSRE---QLAAIFA 447
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
13-380 |
4.27e-32 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 127.58 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 13 KFRAVSLVSAAYKTVSgVNGPLVILDEVKFpKFAEIVQLRLADGTV-RSGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEF 91
Cdd:PRK09099 15 ELAALPAVRRTGKVVE-VIGTLLRVSGLDV-TLGELCELRQRDGTLlQRAEVVGFSRDVALLSPFGELGGL-SRGTRVIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 92 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 171
Cdd:PRK09099 92 LGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 172 AGLphneiaaqicrqaglvklpGKSVLddhTDNFAI-------VFAAMGV-NMETARFFKQDFEENGsMENVCLFLNLAN 243
Cdd:PRK09099 172 AGV-------------------GKSTL---MGMFARgtqcdvnVIALIGErGREVREFIELILGEDG-MARSVVVCATSD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 244 DPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRN 323
Cdd:PRK09099 229 RSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GET 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1060139778 324 GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 380
Cdd:PRK09099 306 GSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
62-413 |
5.07e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 127.38 E-value: 5.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 62 QVLEVSGSKAVVQVFEGTSGIDAKNTLCEFTGDiLRTPVSEDMLGRVFNGSGKPIDkGPPILAEDFLDIQGQPINPWSRI 141
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGLHCGQQVMALRRR-HQVPVGEALLGRVIDGFGRPLD-GRELPDVCWKDYDAMPPPAMVRQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 142 YPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICrqaglvKLPGKSVlddhtdnfaIVFAAMGVNMETARF 221
Cdd:PRK07594 134 PITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC------NAPDADS---------NVLVLIGERGREVRE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 222 FkQDFEENGSMENVCLFLNLAND-PTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRG 300
Cdd:PRK07594 199 F-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETAVSGE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 301 FPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 380
Cdd:PRK07594 277 YPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF 354
|
330 340 350
....*....|....*....|....*....|...
gi 1060139778 381 KSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAM 413
Cdd:PRK07594 355 PVVTSH-----EHRQLAAILRRCLALYQEVELL 382
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
92-383 |
1.28e-31 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 127.00 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 92 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 171
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 172 aglphneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERII 251
Cdd:CHL00059 150 -------------RQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 252 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRVEGR--NGSI 326
Cdd:CHL00059 217 APYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQlgEGSM 292
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1060139778 327 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSA 383
Cdd:CHL00059 293 TALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA 349
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
27-443 |
7.76e-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: 7.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 27 VSGVNGPLV-----------ILD--EVKFPKFAEI---VQLRLADGTVRSgqvLEVSGSKAVVQvfegtsGIDAKNTlce 90
Cdd:TIGR01039 5 VVQVIGPVVdvefeqgelprIYNalKVQNRAESELtleVAQHLGDDTVRT---IAMGSTDGLVR------GLEVIDT--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 91 ftGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFS 170
Cdd:TIGR01039 73 --GAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 171 AAGLphneiaaqicrqaglvklpGKSVL-DDHTDNFAI------VFAAMGVNMETARFFKQDFEENGSMENVCLFLNLAN 243
Cdd:TIGR01039 151 GAGV-------------------GKTVLiQELINNIAKehggysVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 244 DPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRN 323
Cdd:TIGR01039 212 EPPGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKT 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 324 GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMK-SAIGEgmtrkDHSDVSNQLYA 402
Cdd:TIGR01039 290 GSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQ 364
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1060139778 403 CYAIGKDVQAMKAVVGEEALTPDDLLYLEFLTKFEKnFISQ 443
Cdd:TIGR01039 365 ILQRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
92-378 |
1.28e-29 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 121.18 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 92 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLdiqgqPINpwsRIYPEEM--------IQTGISAIDVMNSIARG 163
Cdd:PRK13343 91 TGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-----PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 164 QKIPIFSAaglphneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLAN 243
Cdd:PRK13343 163 QRELIIGD-------------RQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEAS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 244 DPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRN 323
Cdd:PRK13343 230 DPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPEL 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1060139778 324 --GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 378
Cdd:PRK13343 309 ggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
97-466 |
1.81e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 120.27 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 97 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLph 176
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGV-- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 177 neiaaqicrqaglvklpGKSVL----DDHTDNFAIVFAAMGvnmETARFFKqDFeengsMENVCLFLNLANDPTIERI-- 250
Cdd:PRK07960 187 -----------------GKSVLlgmmARYTQADVIVVGLIG---ERGREVK-DF-----IENILGAEGRARSVVIAAPad 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 251 ITPRLALTAAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNG 324
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 325 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSdvSNQLYACY 404
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQ--FKQLLSSF 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1060139778 405 AIGKDVQAmkavVGEEALTPDDLL--YLEFLTKFEKnFISQGNYENRTVFESLDigwQLLRIFP 466
Cdd:PRK07960 399 QRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFERADWEDSLQ---ALERIFP 454
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
99-415 |
6.44e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 118.65 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 99 PVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphne 178
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGV---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 179 iaaqicrqaglvklpGKSVL----DDHTDNFAIVFAAMGvnmETARFFKQDFEE----NGSMENVCLFLNLANDPTIeRI 250
Cdd:PRK08972 174 ---------------GKSVLlgmmTRGTTADVIVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM-RL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 251 ITPRLALTAAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIP 330
Cdd:PRK08972 235 KGCETATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFY 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 331 ILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHSDVS---NQLYACYAIG 407
Cdd:PRK08972 314 TVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQN 388
|
....*...
gi 1060139778 408 KDVQAMKA 415
Cdd:PRK08972 389 RDLISIGA 396
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
99-409 |
6.95e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 118.16 E-value: 6.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 99 PVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNE 178
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 179 IAAQICRQA-------GLVKLPGKSVLDdhtdnfaivfaamgvnmetarFFKQDFEENGsMENVCLFLNLANDPTIERII 251
Cdd:PRK06793 172 LLGMIAKNAkadinviSLVGERGREVKD---------------------FIRKELGEEG-MRKSVVVVATSDESHLMQLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 252 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEgrNGSITQIP 330
Cdd:PRK06793 230 AAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQ--KGSITGIY 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1060139778 331 ILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHSDVSNQLYACYAIGKD 409
Cdd:PRK06793 305 TVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
76-409 |
2.94e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 116.75 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 76 FEGTSGIdAKNTLCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAID 155
Cdd:PRK07721 72 YTEVAEI-APGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAID 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 156 VMNSIARGQKIPIFSAAGLPHNEIAAQICRQaglvklpgksvlddhTDNFAIVFAAMGV-NMETARFFKQDFEENGSMEN 234
Cdd:PRK07721 151 SLLTVGKGQRVGIFAGSGVGKSTLMGMIARN---------------TSADLNVIALIGErGREVREFIERDLGPEGLKRS 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 235 VcLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYE 314
Cdd:PRK07721 216 I-VVVATSDQPALMRIKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLE 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 315 RAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHS 394
Cdd:PRK07721 294 RTGTNA--SGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHK 366
|
330
....*....|....*...
gi 1060139778 395 DVSN---QLYACYAIGKD 409
Cdd:PRK07721 367 EAANrfrELLSTYQNSED 384
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
30-379 |
5.75e-27 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 112.78 E-value: 5.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 30 VNGPLV--ILDEVKFPKFAEIVQLRLADGTVRSGQVLEVSGSKAVVQVFEGTSGIDAKNTLcEFTGDILRTPVSEDMLGR 107
Cdd:PRK08149 13 IQGPIIeaELPDVAIGEICEIRAGWHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQVVL-KPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 108 VFNGSGKPIDK-GPPILAEDF---LDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaaqi 183
Cdd:PRK08149 92 VLDPTGKIVERfDAPPTVGPIseeRVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAG---------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 184 CRQAGLVklpgkSVLDDHTDNFAIVFAAMGvnmETARF---FKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAA 260
Cdd:PRK08149 162 CGKTSLM-----NMLIEHSEADVFVIGLIG---ERGREvteFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 261 EFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRNGSITQIPILTMPNDDIT 340
Cdd:PRK08149 234 EYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEP 310
|
330 340 350
....*....|....*....|....*....|....*....
gi 1060139778 341 HPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 379
Cdd:PRK08149 311 DPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
24-380 |
2.48e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 110.84 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 24 YKTVSGVNGPLVildEVKFPKFAEIVQLRLA----DGTVRSGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDILRTP 99
Cdd:PRK08927 18 YGRVVAVRGLLV---EVAGPIHALSVGARIVvetrGGRPVPCEVVGFRGDRALLMPFGPLEGV-RRGCRAVIANAAAAVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 100 VSEDMLGRVFNGSGKPID-KGPpiLAEDFLD--IQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLph 176
Cdd:PRK08927 94 PSRAWLGRVVNALGEPIDgKGP--LPQGPVPypLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGV-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 177 neiaaqicrqaglvklpGKSVL----DDHTDNFAIVFAAMGvnmETAR----FFKQDFEENGSMENVcLFLNLANDPTIE 248
Cdd:PRK08927 170 -----------------GKSVLlsmlARNADADVSVIGLIG---ERGRevqeFLQDDLGPEGLARSV-VVVATSDEPALM 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 249 RIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQ 328
Cdd:PRK08927 229 RRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITG 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1060139778 329 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 380
Cdd:PRK08927 308 LFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
97-380 |
7.15e-25 |
|
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: 103.84 E-value: 7.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 97 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQgQPINPWSRIYPE-EMIQTGISAIDVMNSIARGQKIPIFSAAGLp 175
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIH-REAPEFVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 176 hneiaaqicrqaglvklpGKSVL-DDHTDNFAI------VFAAMGVNMETARFFKQDFEENG-----SMENVCLFLNLAN 243
Cdd:cd01133 79 ------------------GKTVLiMELINNIAKahggysVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 244 DPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRN 323
Cdd:cd01133 141 EPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST--KK 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1060139778 324 GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 380
Cdd:cd01133 219 GSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
92-378 |
7.81e-25 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 107.07 E-value: 7.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 92 TGDILRTPVSEDMLGRVFNGSGKPID-KGPpILAEDFLD--------IQGQPINpwsriypeEMIQTGISAIDVMNSIAR 162
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDgKGP-IEATETRPverkapgvIDRKSVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 163 GQKIPIfsaaglphneiaaqIC-RQAGlvklpgKS------VLDDHTDNFAIVFAAMGVNMETARFFKQDFEENGSMENV 235
Cdd:PRK09281 162 GQRELI--------------IGdRQTG------KTaiaidtIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 236 CLFLNLANDPTIERIITPRLALTAAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLati 312
Cdd:PRK09281 222 IVVAATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL--- 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060139778 313 YERAGRV--EGRNGSITQIPIL-TMPNDdITHPIPdlTGY--ITEGQIYVDRQLHNRQIYPPVNVLPSLSR 378
Cdd:PRK09281 298 LERAAKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
54-405 |
1.11e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 106.13 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 54 ADGTVRSGQVLEVSGSKAVVQVFEGTSGI--DAKNTLCEFTGDILrtpVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQ 131
Cdd:PRK07196 47 VDETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGELL---IGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 132 GQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaaqicrqaglvklpGKSVL----DDHTDNFAI 207
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGV-------------------GKSVLlgmiTRYTQADVV 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 208 VFAAMGV-NMETARFFKQDFEENGSMENVcLFLNLANDPTIERIITPRLALTAAEFlaYQCEKH-VLVILTDMSSYAEAL 285
Cdd:PRK07196 185 VVGLIGErGREVKEFIEHSLQAAGMAKSV-VVAAPADESPLMRIKATELCHAIATY--YRDKGHdVLLLVDSLTRYAMAQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 286 REVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQ 365
Cdd:PRK07196 262 REIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAG 340
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1060139778 366 IYPPVNVLPSLSRLMKSAIGegmtrKDHSDVSNQLYACYA 405
Cdd:PRK07196 341 HYPAIDISQSISRCMSQVIG-----SQQAKAASLLKQCYA 375
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
99-378 |
8.08e-24 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 103.45 E-value: 8.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 99 PVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNE 178
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 179 IAAQICRQAglvklpgKSVLDdhtdnfaiVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALT 258
Cdd:PRK05922 173 LLSTIAKGS-------KSTIN--------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 259 AAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQI-PILTMPNd 337
Cdd:PRK05922 238 IAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYPN- 313
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1060139778 338 ditHP--IPDLTGYITEGQIYVDRQlHNRQIYPPVNVLPSLSR 378
Cdd:PRK05922 314 ---HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
92-378 |
1.48e-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: 103.58 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 92 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLD--------IQGQPINpwsriypeEMIQTGISAIDVMNSIARG 163
Cdd:COG0056 91 TGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPverpapgvIDRQPVH--------EPLQTGIKAIDAMIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 164 QKipifsaaglphnEIaaqIC--RQAglvklpGKSVLddhtdnfAI-------------VFAAMGVNMETARFFKQDFEE 228
Cdd:COG0056 163 QR------------EL---IIgdRQT------GKTAI-------AIdtiinqkgkdvicIYVAIGQKASTVAQVVETLEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 229 NGSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YM 305
Cdd:COG0056 215 HGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 306 YTDLatiYERAGRV--EGRNGSITQIPIL-TMPNddithpipDLTGY-------ITEGQIYVDRQLHNRQIYPPVNVLPS 375
Cdd:COG0056 294 HSRL---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLS 362
|
...
gi 1060139778 376 LSR 378
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 ... |
104-378 |
9.70e-20 |
|
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: 9.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 104 MLGRVFNGSGKPIDkgppILAE---DFLDiQGQPINPW---------SRIYPEEMIQTGISAIDVMNSIARGqkipifSA 171
Cdd:cd01134 10 LLGSIFDGIQRPLE----VIAEtgsIFIP-RGVNVQRWpvrqprpvkEKLPPNVPLLTGQRVLDTLFPVAKG------GT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 172 AGLPhneiAAQICrqaglvklpGKSVLDDHTDNFA----IVFAAMG--------VNMEtarFFKQDFEENGS--MENVCL 237
Cdd:cd01134 79 AAIP----GPFGC---------GKTVISQSLSKWSnsdvVIYVGCGergnemaeVLEE---FPELKDPITGEslMERTVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 238 FLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 317
Cdd:cd01134 143 IANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAG 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1060139778 318 RVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPVNVLPSLSR 378
Cdd:cd01134 222 RVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
144-378 |
3.65e-19 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 90.03 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 144 EEMIQTGISAIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPGKSVLDDHTDNFAIVFAAMGVNMETARFFK 223
Cdd:PRK07165 124 NEQLYTGIIAIDLLIPIGKGQRELIIGD-------------RQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 224 QDFEENGSMENVCLFLNLANDPtIERIITPRLALTAAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG 303
Cdd:PRK07165 191 ETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMAHAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPG 267
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1060139778 304 YMYTDLATIYERAGRVEGRNgSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 378
Cdd:PRK07165 268 DMFFAHSKLLERAGKFKNRK-TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
26-426 |
3.30e-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: 83.99 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 26 TVSGVNGPLV-----------ILD--EVKFPKFAEI---VQLRLADGTVRSgqvleVSgskavvqvFEGTSGIdAKNTLC 89
Cdd:COG0055 7 KIVQVIGPVVdvefpegelpaIYNalEVENEGGGELvleVAQHLGDNTVRC-----IA--------MDSTDGL-VRGMEV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 90 EFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFLDIQGQPiNPWSRIYPE-EMIQTGISAIDVMNSIARGQKIPI 168
Cdd:COG0055 73 IDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPA-PPFEEQSTKtEILETGIKVIDLLAPYAKGGKIGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 169 FSAAG---------LPHNeIAAQicrQAGLVklpgksvlddhtdnfaiVFAAMGvnmETARF---FKQDFEENGSMENVC 236
Cdd:COG0055 152 FGGAGvgktvlimeLIHN-IAKE---HGGVS-----------------VFAGVG---ERTREgndLYREMKESGVLDKTA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 237 LFLNLANDPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERA 316
Cdd:COG0055 208 LVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 317 GRVegRNGSITQIPILTMPNDDITHPIP-------DLTgyitegqIYVDRQLHNRQIYPPVNVLPSLSRLMKSAI-GEgm 388
Cdd:COG0055 288 TST--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE-- 356
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1060139778 389 trkDHSDVSN------QLYacyaigKDVQAMKAVVGEEALTPDD 426
Cdd:COG0055 357 ---EHYRVARevqrilQRY------KELQDIIAILGMDELSEED 391
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
45-388 |
1.01e-16 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 82.78 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 45 FAEIVQLRLADGTVRSGQV--LEVSGSKAVVQVFEGTSGIDAKNTLCefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPI 122
Cdd:PTZ00185 64 YNTIIMIQVSPTTFAAGLVfnLEKDGRIGIILMDNITEVQSGQKVMA--TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 123 LAEDFLDIQ--------GQPiNPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPG 194
Cdd:PTZ00185 142 RSRALLESEqtlgkvdaGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGD-------------RQTGKTSIAV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 195 KSVLDDHTDNFAI--------VFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQ 266
Cdd:PTZ00185 208 STIINQVRINQQIlsknavisIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 267 cEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GRNG-SITQIPILTMPNDDITHPIP 344
Cdd:PTZ00185 288 -GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKGGgSVTALPIVETLSNDVTAYIV 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1060139778 345 DLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGM 388
Cdd:PTZ00185 367 TNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
26-431 |
1.44e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 82.52 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 26 TVSGVNGPLVILDEVKFPKFAEIVQ---LRLAdgtvrsGQVLEVSGSKAVVQVFEGTSGIdAKNTLCEFTGDilrtPVSE 102
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRvgeEGLI------GEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 103 D----MLGRVFNGSGKPIDKgppiLAE---DFL------------------------------DIQGQ------------ 133
Cdd:PRK04192 75 ElgpgLLGSIFDGIQRPLDE----LAEksgDFLergvyvpaldrekkweftptvkvgdkveagDILGTvqetpsiehkim 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 134 -PINP-------------------------------------W---------SRIYPEEMIQTGISAIDVMNSIARGQK- 165
Cdd:PRK04192 151 vPPGVsgtvkeivsegdytvddtiavlededgegveltmmqkWpvrrprpykEKLPPVEPLITGQRVIDTFFPVAKGGTa 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 166 -IP-IFSAaglphneiaaqicrqaglvklpGKSVLDDHTDNFA----IVFAAMG--VN-M-ETARFFKQ--DFEENGS-M 232
Cdd:PRK04192 231 aIPgPFGS----------------------GKTVTQHQLAKWAdadiVIYVGCGerGNeMtEVLEEFPEliDPKTGRPlM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 233 ENVCLFLNLANDPTIER---IITprlALTAAEF---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMY 306
Cdd:PRK04192 289 ERTVLIANTSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 307 TDLATIYERAGRVE---GRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSrLMKSA 383
Cdd:PRK04192 362 SRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQ 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1060139778 384 IGEGMTRKDHSDVS---NQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLE 431
Cdd:PRK04192 441 VAPWWEENVDPDWRelrDEAMDLLQREAELQEIVRLVGPDALPEEDRLILE 491
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
232-377 |
2.63e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 81.99 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 232 MENVCLFLNLANDPTIERIITPRLALTAAEF---LAYQcekhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 308
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYfrdMGYD----VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 792
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1060139778 309 LATIYERAGRV-----EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLS 377
Cdd:PRK14698 793 LAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
49-443 |
1.44e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 78.93 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 49 VQLRLADGTVRSgqvleVSGSkAVVQVFEGTSGIDakntlcefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDFL 128
Cdd:CHL00060 61 VQQLLGNNRVRA-----VAMS-ATDGLMRGMEVID--------TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 129 diqgqPINpwsRIYPE--------EMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaaqicrqaglvklpGKSVL-D 199
Cdd:CHL00060 127 -----PIH---RSAPAfiqldtklSIFETGIKVVDLLAPYRRGGKIGLFGGAGV-------------------GKTVLiM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 200 DHTDNFA------IVFAAMG----------VNMETARFFKqdfEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 263
Cdd:CHL00060 180 ELINNIAkahggvSVFGGVGertregndlyMEMKESGVIN---EQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 264 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegRNGSITQIPILTMPNDDITHPI 343
Cdd:CHL00060 257 RDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITST--KEGSITSIQAVYVPADDLTDPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 344 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAI-GEgmtrkDHSDVSN------QLYacyaigKDVQAMKAV 416
Cdd:CHL00060 335 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE-----EHYETAQrvkqtlQRY------KELQDIIAI 403
|
410 420
....*....|....*....|....*..
gi 1060139778 417 VGEEALTPDDLLYLEFLTKFEkNFISQ 443
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 ... |
27-93 |
1.39e-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: 1.39e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 27 VSGVNGPLVILD--EVKFPKFAEIVQLRLAD-GTVRSGQVLEVSGSKAVVQVFEGTSGIDaKNTLCEFTG 93
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, ... |
393-463 |
2.49e-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: 56.30 E-value: 2.49e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1060139778 393 HSDVSNQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLEFLTKFEKnFISQGNYENRTVFESLDIGWQLLR 463
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, ... |
24-94 |
2.90e-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: 2.90e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1060139778 24 YKTVSGVNGPLVILDEVKFPKFAEIVQLRLADG---TVRSGQVLEVSGSKAVVQVFEGTSGIDAKnTLCEFTGD 94
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLSRG-ALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
30-117 |
2.51e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 46.94 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 30 VNGPLVILDEVKFPKFAEIVqlRLAD-GTVrsGQVLEVSGSKAVVQVFEGTSGIDAKNTLcEFTGDILRTPVSEDMLGRV 108
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVV--RVGElGLI--GEIIRLEGDKAVIQVYEETAGLKPGEPV-EGTGSSLSVELGPGLLTSI 84
|
....*....
gi 1060139778 109 FNGSGKPID 117
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 ... |
26-82 |
2.57e-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: 2.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060139778 26 TVSGVNGPLVILDEVKFPKFAEIV---QLRLAdgtvrsGQVLEVSGSKAVVQVFEGTSGI 82
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELVrvgEEGLI------GEIIRLEGDKATIQVYEETSGL 56
|
|
| |
