|
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 ... |
30-493 |
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: 1041.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 30 TYKTVSGVNGPLVILDEVKFPKYAEIVQLKLADGSLRSGQVLEVSGSKAVVQVFEGTSGIDAKNTHCEFTGDILRTPVSE 109
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 110 DMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 189
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 190 ICRQAGLVKLPGKSVLDSHEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEF 269
Cdd:TIGR01040 161 ICRQAGLVKLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 270 LAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 349
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 350 IPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 429
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1663746890 430 TPDDLLYLEFLSKFEKNFISQGSYENRTVFESLDIGWQLLRIFPKEMLKRIPASTLAEFYPRDS 493
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKS 464
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
27-491 |
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: 859.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 27 PRLTYKTVSGVNGPLVILDEVKFPKYAEIVQLKLADGSLRSGQVLEVSGSKAVVQVFEGTSGIDAKNTHCEFTGDILRTP 106
Cdd:COG1156 2 MKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 107 VSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEI 186
Cdd:COG1156 82 VSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 187 AAQICRQAglvKLPGKsvldshEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTA 266
Cdd:COG1156 162 AAQIARQA---KVRGE------EEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 267 AEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDI 346
Cdd:COG1156 233 AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 347 THPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGE 426
Cdd:COG1156 313 THPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663746890 427 EALTPDDLLYLEFLSKFEKNFISQGSYENRTVFESLDIGWQLLRIFPKEMLKRIPASTLAEFYPR 491
Cdd:COG1156 393 EALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPK 457
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
31-492 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 826.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 31 YKTVSGVNGPLVILDEVKFPKYAEIVQLKLADGSLRSGQVLEVSGSKAVVQVFEGTSGIDAKNTHCEFTGDILRTPVSED 110
Cdd:PRK04196 4 YRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 111 MLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 190
Cdd:PRK04196 84 MLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 191 CRQAglvKLPGKsvldshEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 270
Cdd:PRK04196 164 ARQA---KVLGE------EENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 271 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 350
Cdd:PRK04196 235 AFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 351 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALT 430
Cdd:PRK04196 315 PDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALS 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663746890 431 PDDLLYLEFLSKFEKNFISQGSYENRTVFESLDIGWQLLRIFPKEMLKRIPASTLAEFYPRD 492
Cdd:PRK04196 395 ERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKY 456
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
31-492 |
0e+00 |
|
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 200071 [Multi-domain] Cd Length: 458 Bit Score: 708.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 31 YKTVSGVNGPLVILDEVKFPKYAEIVQLKLADGSLRSGQVLEVSGSKAVVQVFEGTSGIDAKNTHCEFTGDILRTPVSED 110
Cdd:TIGR01041 2 YSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 111 MLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 190
Cdd:TIGR01041 82 MLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 191 CRQAglvKLPGKsvldshEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 270
Cdd:TIGR01041 162 ARQA---TVRGE------ESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 271 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPI 350
Cdd:TIGR01041 233 AFEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 351 PDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALT 430
Cdd:TIGR01041 313 PDLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALS 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663746890 431 PDDLLYLEFLSKFEKNFISQGSYENRTVFESLDIGWQLLRIFPKEMLKRIPASTLAEFYPRD 492
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 ... |
102-392 |
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: 630.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 102 ILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGL 181
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 182 PHNEIAAQICRQAGLVKlpgksvldsHEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPR 261
Cdd:cd01135 81 PHNELAAQIARQAGVVG---------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 262 LALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTM 341
Cdd:cd01135 152 MALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTM 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1663746890 342 PNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIG 392
Cdd:cd01135 232 PNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
31-495 |
4.55e-122 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 363.97 E-value: 4.55e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 31 YKTVSGVNGPLVILdEVKFPKYAEIVQLKLADGSlRSGQVLEVSGSKAVVQVFEGTSGIdAKNTHCEFTGDILRTPVSED 110
Cdd:PRK02118 5 YTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGI-STGDEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 111 MLGRVFNGSGKPIDKGPpILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQI 190
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGP-ELEGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 191 CRQAglvklpgksvldsheDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFL 270
Cdd:PRK02118 161 ALQA---------------EADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 271 AYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDITHPI 350
Cdd:PRK02118 226 ALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHPV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 351 PDLTGYITEGQIYvdrqLHNRQIYPpvnvLPSLSRLMKSAIGEgMTRKDHSDVSN---QLYACYAIGKDVQAMkavvGEE 427
Cdd:PRK02118 305 PDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GFK 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 428 aLTPDDLLYLEFLSKFEKNFISQGSyeNRTVFESLDIGWQLL-RIF-PKEMLkrIPASTLAEFYPRDSRH 495
Cdd:PRK02118 372 -LSNWDEKLLKFSELFESRLMDLEV--NIPLEEALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKNCLH 436
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
157-384 |
9.22e-110 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 324.31 E-value: 9.22e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 157 GISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklpgksvldsheDNFAIVFAAMGVNMETARFFKQDFEEN 236
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA---------------SADVVVYALIGERGREVREFIEELLGS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 237 GSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDL 316
Cdd:pfam00006 66 GALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1663746890 317 ATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLS 384
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 ... |
104-386 |
5.45e-108 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 322.10 E-value: 5.45e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 104 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPH 183
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 184 NEIAAQICRQAglvklpgksvldSHEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLA 263
Cdd:cd19476 81 TVLAMQLARNQ------------AKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 264 LTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPN 343
Cdd:cd19476 149 LTIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPG 227
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1663746890 344 DDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 386
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 ... |
394-488 |
1.22e-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: 1.22e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 394 GMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLEFLSKFEKNFISQGSYENRTVFESLDIGWQLLRIFP 473
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 1663746890 474 KEMLKRIPASTLAEF 488
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
104-386 |
6.17e-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: 158.49 E-value: 6.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 104 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLph 183
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 184 neiaaqicrqaglvklpGKSVLDS----HEDNFAIVFAAMGvnmETAR----FFKQDFEENGsMENVCLFLNLANDPTIE 255
Cdd:cd01136 79 -----------------GKSTLLGmiarNTDADVNVIALIG---ERGRevreFIEKDLGEEG-LKRSVLVVATSDESPLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 256 RIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNGSITQ 335
Cdd:cd01136 138 RVRAAYTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITA 214
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1663746890 336 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 386
Cdd:cd01136 215 FYTVLVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
33-387 |
2.33e-41 |
|
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: 153.26 E-value: 2.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 33 TVSGVNGPLVildEVKFPKYA--EIVQLKLADGSLRSGQVLEVSGSKAVVQVFEGTSGIdAKNTHCEFTGDILRTPVSED 110
Cdd:COG1157 22 RVTRVVGLLI---EAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 111 MLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSR--IypEEMIQTGISAIDVMNSIARGQKIPIFSAAGlphneiaa 188
Cdd:COG1157 98 LLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERarI--TEPLDTGVRAIDGLLTVGRGQRIGIFAGSG-------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 189 qicrqaglVklpGKSVL----------DshednfAIVFAAMGvnmETAR----FFKQDFEENGsMENVCLFLNLANDPTI 254
Cdd:COG1157 168 --------V---GKSTLlgmiarnteaD------VNVIALIG---ERGRevreFIEDDLGEEG-LARSVVVVATSDEPPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 255 ERIITPRLALTAAEFLAYQcEKHVLVIltdMSS---YAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRveGRNG 331
Cdd:COG1157 227 MRLRAAYTATAIAEYFRDQ-GKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKG 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1663746890 332 SITQI-PILTmPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 387
Cdd:COG1157 301 SITAFyTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM 356
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
99-390 |
1.14e-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: 149.85 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 99 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 178
Cdd:TIGR00962 90 TGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGD 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 179 aglphneiaaqicRQAGLVKLPGKSVLDSHEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERII 258
Cdd:TIGR00962 170 -------------RQTGKTAVAIDTIINQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 259 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRNGSI 333
Cdd:TIGR00962 237 APYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSL 312
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1663746890 334 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSA 390
Cdd:TIGR00962 313 TALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| ATP-synt_V_A-type_beta_N |
cd18118 |
V/A-type ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the V1/A1 ... |
30-101 |
1.35e-39 |
|
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: 137.56 E-value: 1.35e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1663746890 30 TYKTVSGVNGPLVILDEVKFPKYAEIVQLKLADGSLRSGQVLEVSGSKAVVQVFEGTSGIDAKNTHCEFTGD 101
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
69-469 |
2.89e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 144.96 E-value: 2.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 69 QVLEVSGSKAVVQVFEGTSGIDAkNTHCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPiLAEDYLDIQGQPINPWSRI 148
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGLRC-GQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLTRQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 149 YPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICrqaglvklpgksvldSHEDNFAIVFAAMGV-NMETAR 227
Cdd:PRK06820 142 PIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC---------------ADSAADVMVLALIGErGREVRE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 228 FFKQDFEENGSMENVcLFLNLANDPTIERIITPRLALTAAEFLAyQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRG 307
Cdd:PRK06820 207 FLEQVLTPEARARTV-VVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 308 FPGYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 387
Cdd:PRK06820 285 FPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 388 KSAIGEGmtRKDHSDVSNQLYACYaigKDVQAMKAVvgEEALTPDDLLYLEFLSKFE--KNFISQGSYENRTVFESLDIG 465
Cdd:PRK06820 363 PQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEHL 435
|
....
gi 1663746890 466 WQLL 469
Cdd:PRK06820 436 AQVV 439
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
88-418 |
1.45e-37 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 142.97 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 88 GIDAkNTHCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSI 167
Cdd:PRK06936 81 GISS-NTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 168 ARGQKIPIFSAAGlphneiaaqicrqaglvklPGKSVLDS----HEDNFAIVFAAMGV-NMETARFFKQDFEENGsMENV 242
Cdd:PRK06936 160 GEGQRMGIFAAAG-------------------GGKSTLLAslirSAEVDVTVLALIGErGREVREFIESDLGEEG-LRKA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 243 CLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYER 322
Cdd:PRK06936 220 VLVVATSDRPSMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMER 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 323 AGrvEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGegmtrKDHSD 402
Cdd:PRK06936 299 AG--QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVS-----KEHKT 371
|
330
....*....|....*.
gi 1663746890 403 VSNQLYACYAIGKDVQ 418
Cdd:PRK06936 372 WAGRLRELLAKYEEVE 387
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
102-385 |
2.84e-35 |
|
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: 132.68 E-value: 2.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 102 ILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAagl 181
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 182 phneiaaqicRQAGLVKLPGKSVLDSHEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPR 261
Cdd:cd01132 78 ----------RQTGKTAIAIDTIINQKGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 262 LALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRV--EGRNGSITQI 336
Cdd:cd01132 148 AGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTAL 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1663746890 337 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 385
Cdd:cd01132 224 PIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
103-393 |
3.42e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 133.66 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 103 LRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLP 182
Cdd:PRK08472 90 LNIPVGRNLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVG 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 183 HNEIAAQICRQAglvKLPGKsvldshednfaiVFAAMGvnmETARFFKQDFEEN--GSMENVCLFLNLANDPTIERIITP 260
Cdd:PRK08472 170 KSTLMGMIVKGC---LAPIK------------VVALIG---ERGREIPEFIEKNlgGDLENTVIVVATSDDSPLMRKYGA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 261 RLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRnGSITQIPILT 340
Cdd:PRK08472 232 FCAMSVAEYFKNQ-GLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVL 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1663746890 341 MPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGE 393
Cdd:PRK08472 310 VEGDDMSDPIADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
69-420 |
3.96e-33 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 130.46 E-value: 3.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 69 QVLEVSGSKAVVQVFEGTSGIdakntHCEFTGDILR----TPVSEDMLGRVFNGSGKPIDkGPPILAEDYLDIQGQPINP 144
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGL-----HCGQQVMALRrrhqVPVGEALLGRVIDGFGRPLD-GRELPDVCWKDYDAMPPPA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 145 WSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICrqaglvKLPGKSVldshednfaIVFAAMGVNME 224
Cdd:PRK07594 130 MVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLC------NAPDADS---------NVLVLIGERGR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 225 TARFFkQDFEENGSMENVCLFLNLAND-PTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP 303
Cdd:PRK07594 195 EVREF-IDFTLSEETRKRCVIVVATSDrPALERVRALFVATTIAEFFRDN-GKRVVLLADSLTRYARAAREIALAAGETA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 304 GRRGFPGYMYTDLATIYERAGRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSL 383
Cdd:PRK07594 273 VSGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATL 350
|
330 340 350
....*....|....*....|....*....|....*..
gi 1663746890 384 SRLMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAM 420
Cdd:PRK07594 351 SRVFPVVTSH-----EHRQLAAILRRCLALYQEVELL 382
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
101-473 |
8.33e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 129.85 E-value: 8.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 101 DILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAG 180
Cdd:PRK05688 99 DTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTG 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 181 LphneiaaqicrqaglvklpGKSVLDSHEDNFA----IVFAAMGV-NMETARFFKQDFEENGSMENVCLfLNLANDPTIE 255
Cdd:PRK05688 179 V-------------------GKSVLLGMMTRFTeadiIVVGLIGErGREVKEFIEHILGEEGLKRSVVV-ASPADDAPLM 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 256 RIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQ 335
Cdd:PRK05688 239 RLRAAMYCTRIAEYFRDK-GKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 336 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIG-EGMTRKDHsdvSNQLYACYAIG 414
Cdd:PRK05688 318 FYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQR---FKQLWSRYQQS 394
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1663746890 415 KDVQAMKAVVgeEALTPDDLLYLEFLSKFEKnFISQGSYENRTVFESLDigwQLLRIFP 473
Cdd:PRK05688 395 RDLISVGAYV--AGGDPETDLAIARFPHLVQ-FLRQGLRENVSLAQSRE---QLAAIFA 447
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
18-420 |
3.52e-32 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 127.96 E-value: 3.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 18 AVSRDFIAQPRL-TYKTVSGVNGPLVILDEVKFpKYAEIVQLKLADGSL-RSGQVLEVSGSKAVVQVFEGTSGIdAKNTH 95
Cdd:PRK09099 11 ALERELAALPAVrRTGKVVEVIGTLLRVSGLDV-TLGELCELRQRDGTLlQRAEVVGFSRDVALLSPFGELGGL-SRGTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 96 CEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPI 175
Cdd:PRK09099 89 VIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 176 FSAAGLphneiaaqicrqaglvklpGKSVLDShednfaiVFA---AMGVNM---------ETARFFKQDFEENGsMENVC 243
Cdd:PRK09099 169 FAPAGV-------------------GKSTLMG-------MFArgtQCDVNVialigergrEVREFIELILGEDG-MARSV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 244 LFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERA 323
Cdd:PRK09099 222 VVCATSDRSSIERAKAAYVATAIAEYFRDR-GLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 324 GRveGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSaigegMTRKDHSDV 403
Cdd:PRK09099 301 GM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQ-----VVPREHVQA 373
|
410
....*....|....*..
gi 1663746890 404 SNQLYACYAIGKDVQAM 420
Cdd:PRK09099 374 AGRLRQLLAKHREVETL 390
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
99-443 |
5.84e-31 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 125.08 E-value: 5.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 99 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSA 178
Cdd:CHL00059 70 TGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 179 aglphneiaaqicRQAGLVKLPGKSVLDSHEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERII 258
Cdd:CHL00059 150 -------------RQTGKTAVATDTILNQKGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYL 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 259 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLatiYERAGRVEGR--NGSI 333
Cdd:CHL00059 217 APYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLSSQlgEGSM 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 334 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAigegmtrkdhsdvsnqlyacyai 413
Cdd:CHL00059 293 TALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRVGSAA----------------------- 349
|
330 340 350
....*....|....*....|....*....|
gi 1663746890 414 gkDVQAMKAVVGEEALTPDDLLYLEFLSKF 443
Cdd:CHL00059 350 --QIKAMKQVAGKLKLELAQFAELEAFAQF 377
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
30-450 |
7.11e-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: 7.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 30 TYKTVSGVNGPLVildEVKFPKYA--EIVQLKLADGSLRSGQVLEVS---GSKAVVQVFEGTSGIDAKNTHCEFTGDILR 104
Cdd:TIGR01039 1 TKGKVVQVIGPVV---DVEFEQGElpRIYNALKVQNRAESELTLEVAqhlGDDTVRTIAMGSTDGLVRGLEVIDTGAPIS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 105 TPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphn 184
Cdd:TIGR01039 78 VPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGV--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 185 eiaaqicrqaglvklpGKSVLdSHE--DNFAI------VFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIER 256
Cdd:TIGR01039 155 ----------------GKTVL-IQEliNNIAKehggysVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGAR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 257 IITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAgrVEGRNGSITQI 336
Cdd:TIGR01039 218 MRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERI--TSTKTGSITSV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 337 PILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMK-SAIGEgmtrkDHSDVSNQLYACYAIGK 415
Cdd:TIGR01039 296 QAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQILQRYK 370
|
410 420 430
....*....|....*....|....*....|....*
gi 1663746890 416 DVQAMKAVVGEEALTPDDLLYLEFLSKFEKnFISQ 450
Cdd:TIGR01039 371 ELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
30-390 |
1.69e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 123.18 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 30 TYKTVSGVngplvildeVKFPKYAEIVQLKlADGSLRSGQVLEVSGSKAVVQVFEgtSGIDAKNTHCEFTGDILRTPVSE 109
Cdd:PRK06002 36 SHYRVRGL---------SRFVRLGDFVAIR-ADGGTHLGEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 110 DMLGRVFNGSGKPID-KGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaa 188
Cdd:PRK06002 104 SWKGRVINALGEPIDgLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGV------- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 189 qicrqaglvklpGKSVLDS---HEDNF-AIVFAAMGvnmETARFFKQDFEEN--GSMENVCLFLNLANDPTIERIITPRL 262
Cdd:PRK06002 177 ------------GKSTLLAmlaRADAFdTVVIALVG---ERGREVREFLEDTlaDNLKKAVAVVATSDESPMMRRLAPLT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 263 ALTAAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMP 342
Cdd:PRK06002 242 ATAIAEYFRDRGEN-VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVD 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1663746890 343 NDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSA 390
Cdd:PRK06002 321 GDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
99-385 |
3.34e-30 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 123.10 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 99 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLdiqgqPINpwsRIYPEEM--------IQTGISAIDVMNSIARG 170
Cdd:PRK13343 91 TGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-----PLE---RPAPAIIerdfvtepLQTGIKVVDALIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 171 QKIPIFSAaglphneiaaqicRQAGLVKLPGKSVLDSHEDNFAIVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLAN 250
Cdd:PRK13343 163 QRELIIGD-------------RQTGKTAIAIDAIINQKDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEAS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 251 DPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRN 330
Cdd:PRK13343 230 DPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLSPEL 308
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1663746890 331 --GSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 385
Cdd:PRK13343 309 ggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
106-422 |
3.58e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 119.42 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 106 PVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphne 185
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGV---- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 186 iaaqicrqaglvklpGKSVL------DSHEDnfAIVFAAMGvnmETARFFKQDFEE----NGSMENVCLFLNLANDPTIe 255
Cdd:PRK08972 174 ---------------GKSVLlgmmtrGTTAD--VIVVGLVG---ERGREVKEFIEEilgeEGRARSVVVAAPADTSPLM- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 256 RIITPRLALTAAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQ 335
Cdd:PRK08972 233 RLKGCETATTIAEYFRDQGLN-VLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 336 IPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHSDVS---NQLYACYA 412
Cdd:PRK08972 312 FYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQ 386
|
330
....*....|
gi 1663746890 413 IGKDVQAMKA 422
Cdd:PRK08972 387 QNRDLISIGA 396
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
106-416 |
4.86e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 118.93 E-value: 4.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 106 PVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNE 185
Cdd:PRK06793 92 PRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKST 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 186 IAAQICRQA-------GLVKLPGKSVLDshednfaivfaamgvnmetarFFKQDFEENGsMENVCLFLNLANDPTIERII 258
Cdd:PRK06793 172 LLGMIAKNAkadinviSLVGERGREVKD---------------------FIRKELGEEG-MRKSVVVVATSDESHLMQLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 259 TPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVP-GRRGFpgYMYTDLATIYERAGRVEgrNGSITQIP 337
Cdd:PRK06793 230 AAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELPiGGKTL--LMESYMKKLLERSGKTQ--KGSITGIY 304
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1663746890 338 ILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHSDVSNQLYACYAIGKD 416
Cdd:PRK06793 305 TVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
104-473 |
4.98e-29 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 119.12 E-value: 4.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 104 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLph 183
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGV-- 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 184 neiaaqicrqaglvklpGKSVLDSHEDNFA----IVFAAMGvnmETARFFKqDFeengsMENVCLFLNLANDPTIERI-- 257
Cdd:PRK07960 187 -----------------GKSVLLGMMARYTqadvIVVGLIG---ERGREVK-DF-----IENILGAEGRARSVVIAAPad 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 258 ITPRLALTAAEFLAYQCE------KHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNG 331
Cdd:PRK07960 241 VSPLLRMQGAAYATRIAEdfrdrgQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGG 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 332 SITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGMTRKDHSdvSNQLYACY 411
Cdd:PRK07960 321 SITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQ--FKQLLSSF 398
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1663746890 412 AIGKDVQAmkavVGEEALTPDDLL--YLEFLSKFEKnFISQGSYENRTVFESLDigwQLLRIFP 473
Cdd:PRK07960 399 QRNRDLVS----VGAYAKGSDPMLdkAIALWPQLEA-FLQQGIFERADWEDSLQ---ALERIFP 454
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
97-475 |
8.84e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 115.20 E-value: 8.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 97 EFTGDILRTPVSEDMLGRVFNGSGKPID-----KG-PPILAEDyldiqgQPINPWSRIYPEEMIQTGISAIDVMNSIARG 170
Cdd:PRK07721 85 EATGKPLEVKVGSGLIGQVLDALGEPLDgsalpKGlAPVSTDQ------DPPNPLKRPPIREPMEVGVRAIDSLLTVGKG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 171 QKIPIFSAAGLPHNEIAAQICRQAglvklpgksvldSHEDNfaiVFAAMGV-NMETARFFKQDFEENGSMENVcLFLNLA 249
Cdd:PRK07721 159 QRVGIFAGSGVGKSTLMGMIARNT------------SADLN---VIALIGErGREVREFIERDLGPEGLKRSI-VVVATS 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 250 NDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgr 329
Cdd:PRK07721 223 DQPALMRIKGAYTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA-- 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 330 NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEgmtrkDHSDVSN---Q 406
Cdd:PRK07721 300 SGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrE 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663746890 407 LYACYAIGKDVQAMKAVVGEEALTPDDLL--YLEFLSkfeknFISQGSYENRTVFESLDigwQLLRIFPKE 475
Cdd:PRK07721 375 LLSTYQNSEDLINIGAYKRGSSREIDEAIqfYPQIIS-----FLKQGTDEKATFEESIQ---ALLSLFGKG 437
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
27-387 |
1.22e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 111.99 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 27 PRLTYKTVSGVNGPLVildEVKFPKYAEIVQLKLADGSLRSGQVL-EV---SGSKAVVQVFEGTSGIdAKNTHCEFTGDI 102
Cdd:PRK08927 14 TLVIYGRVVAVRGLLV---EVAGPIHALSVGARIVVETRGGRPVPcEVvgfRGDRALLMPFGPLEGV-RRGCRAVIANAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 103 LRTPVSEDMLGRVFNGSGKPID-KGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGL 181
Cdd:PRK08927 90 AAVRPSRAWLGRVVNALGEPIDgKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 182 phneiaaqicrqaglvklpGKSVLDS----HEDNFAIVFAAMGvnmETAR----FFKQDFEENGSMENVcLFLNLANDPT 253
Cdd:PRK08927 170 -------------------GKSVLLSmlarNADADVSVIGLIG---ERGRevqeFLQDDLGPEGLARSV-VVVATSDEPA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 254 IERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSI 333
Cdd:PRK08927 227 LMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTI 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1663746890 334 TQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 387
Cdd:PRK08927 306 TGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
99-386 |
2.78e-26 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 110.85 E-value: 2.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 99 TGDILRTPVSEDMLGRVFNGSGKPIDK-GPPILAE---DYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIP 174
Cdd:PRK08149 76 TGKPLSVWVGEALLGAVLDPTGKIVERfDAPPTVGpisEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 175 IFSAAGLPHNEIAAQICRQA-------GLVKLPGKSVLDshednfaivfaamgvnmetarfFKQDFEENGSMENVCLFLN 247
Cdd:PRK08149 156 IFASAGCGKTSLMNMLIEHSeadvfviGLIGERGREVTE----------------------FVESLRASSRREKCVLVYA 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 248 LANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVe 327
Cdd:PRK08149 214 TSDFSSVDRCNAALVATTVAEYFRDQ-GKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT- 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1663746890 328 gRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRL 386
Cdd:PRK08149 292 -LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
99-385 |
3.92e-25 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 108.23 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 99 TGDILRTPVSEDMLGRVFNGSGKPID-KGPpILAEDYLD--------IQGQPINpwsriypeEMIQTGISAIDVMNSIAR 169
Cdd:PRK09281 91 TGRILEVPVGEALLGRVVNPLGQPIDgKGP-IEATETRPverkapgvIDRKSVH--------EPLQTGIKAIDAMIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 170 GQKIPIfsaaglphneiaaqIC-RQAGlvklpgKS------VLDSHEDNFAIVFAAMGVNMETARFFKQDFEENGSMENV 242
Cdd:PRK09281 162 GQRELI--------------IGdRQTG------KTaiaidtIINQKGKDVICIYVAIGQKASTVAQVVRKLEEHGAMEYT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 243 CLFLNLANDPTIERIITPRLALTAAEFLAYQCeKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YMYTDLati 319
Cdd:PRK09281 222 IVVAATASDPAPLQYLAPYAGCAMGEYFMDNG-KDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL--- 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663746890 320 YERAGRV--EGRNGSITQIPIL-TMPNDdITHPIPdlTGY--ITEGQIYVDRQLHNRQIYPPVNVLPSLSR 385
Cdd:PRK09281 298 LERAAKLsdELGGGSLTALPIIeTQAGD-VSAYIP--TNVisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
104-387 |
7.92e-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: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 104 RTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQgQPINPWSRIYPE-EMIQTGISAIDVMNSIARGQKIPIFSAAGLp 182
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIH-REAPEFVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 183 hneiaaqicrqaglvklpGKSVLdSHE--DNFAI------VFAAMGVNMETARFFKQDFEENG-----SMENVCLFLNLA 249
Cdd:cd01133 79 ------------------GKTVL-IMEliNNIAKahggysVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 250 NDPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVegR 329
Cdd:cd01133 140 NEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST--K 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1663746890 330 NGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLM 387
Cdd:cd01133 218 KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
36-412 |
7.50e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 103.82 E-value: 7.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 36 GVNGplVILDEVKFP-KYAEIVQLKLADGSLRSGQVLEVSGSKAVVQVFEGTSGI--DAKNTHCEFTGDILrtpVSEDML 112
Cdd:PRK07196 23 RVTG--LLLESVGCRlAIGQRCRIESVDETFIEAQVVGFDRDITYLMPFKHPGGVlgGARVFPSEQDGELL---IGDSWL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 113 GRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLphneiaaqicr 192
Cdd:PRK07196 98 GRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGV----------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 193 qaglvklpGKSVL----DSHEDNFAIVFAAMGV-NMETARFFKQDFEENGSMENVcLFLNLANDPTIERIITPRLALTAA 267
Cdd:PRK07196 167 --------GKSVLlgmiTRYTQADVVVVGLIGErGREVKEFIEHSLQAAGMAKSV-VVAAPADESPLMRIKATELCHAIA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 268 EFlaYQCEKH-VLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGrNGSITQIPILTMPNDDI 346
Cdd:PRK07196 238 TY--YRDKGHdVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1663746890 347 THPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGegmtrKDHSDVSNQLYACYA 412
Cdd:PRK07196 315 QDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIG-----SQQAKAASLLKQCYA 375
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
99-385 |
1.35e-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: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 99 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLD--------IQGQPINpwsriypeEMIQTGISAIDVMNSIARG 170
Cdd:COG0056 91 TGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPverpapgvIDRQPVH--------EPLQTGIKAIDAMIPIGRG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 171 QKipifsaaglphnEIaaqIC--RQAglvklpGKSVLdshednfAI-------------VFAAMGVNMETARFFKQDFEE 235
Cdd:COG0056 163 QR------------EL---IIgdRQT------GKTAI-------AIdtiinqkgkdvicIYVAIGQKASTVAQVVETLEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 236 NGSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG---YM 312
Cdd:COG0056 215 HGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 313 YTDLatiYERAGRV--EGRNGSITQIPIL-TMPNddithpipDLTGY-------ITEGQIYVDRQLHNRQIYPPVNVLPS 382
Cdd:COG0056 294 HSRL---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLS 362
|
...
gi 1663746890 383 LSR 385
Cdd:COG0056 363 VSR 365
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
106-385 |
2.60e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 102.29 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 106 PVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPINPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNE 185
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 186 IAAQICRQAglvklpgKSVLDshednfaiVFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALT 265
Cdd:PRK05922 173 LLSTIAKGS-------KSTIN--------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMT 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 266 AAEFLAYQCEKhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQI-PILTMPNd 344
Cdd:PRK05922 238 IAEYFRDQGHR-VLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYPN- 313
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1663746890 345 ditHP--IPDLTGYITEGQIYVDRQlHNRQIYPPVNVLPSLSR 385
Cdd:PRK05922 314 ---HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
151-385 |
2.76e-19 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 90.42 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 151 EEMIQTGISAIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPGKSVLDSHEDNFAIVFAAMGVNMETARFFK 230
Cdd:PRK07165 124 NEQLYTGIIAIDLLIPIGKGQRELIIGD-------------RQTGKTHIALNTIINQKNTNVKCIYVAIGQKRENLSRIY 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 231 QDFEENGSMENVCLFLNLANDPtIERIITPRLALTAAEFLAYqcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPG 310
Cdd:PRK07165 191 ETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMAHAENISY--NDDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPG 267
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663746890 311 YMYTDLATIYERAGRVEGRNgSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSR 385
Cdd:PRK07165 268 DMFFAHSKLLERAGKFKNRK-TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
111-385 |
5.29e-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: 87.24 E-value: 5.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 111 MLGRVFNGSGKPIDkgppILAE---DYLDiQGQPINPW---------SRIYPEEMIQTGISAIDVMNSIARGqkipifSA 178
Cdd:cd01134 10 LLGSIFDGIQRPLE----VIAEtgsIFIP-RGVNVQRWpvrqprpvkEKLPPNVPLLTGQRVLDTLFPVAKG------GT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 179 AGLPhneiAAQICrqaglvklpGKSVLDSHEDNFA----IVFAAMG--------VNMEtarFFKQDFEENGS--MENVCL 244
Cdd:cd01134 79 AAIP----GPFGC---------GKTVISQSLSKWSnsdvVIYVGCGergnemaeVLEE---FPELKDPITGEslMERTVL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 245 FLNLANDPTIERIITPRLALTAAEFLAYQcEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAG 324
Cdd:cd01134 143 IANTSNMPVAAREASIYTGITIAEYFRDM-GYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAG 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1663746890 325 RVE-----GRNGSITQIPILTMPNDDITHPIPDLTGYITegQIY--VDRQLHNRQIYPPVNVLPSLSR 385
Cdd:cd01134 222 RVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIV--QVFwgLDKKLAQRRHFPSINWLISYSK 287
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
99-433 |
5.36e-18 |
|
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: 86.30 E-value: 5.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 99 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLDIQGQPiNPWSRIYPE-EMIQTGISAIDVMNSIARGQKIPIFS 177
Cdd:COG0055 75 TGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPA-PPFEEQSTKtEILETGIKVIDLLAPYAKGGKIGLFG 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 178 AAGLphneiaaqicrqaglvklpGKSVLDS---HedNFAI------VFAAMGvnmETARF---FKQDFEENGSMENVCLF 245
Cdd:COG0055 154 GAGV-------------------GKTVLIMeliH--NIAKehggvsVFAGVG---ERTREgndLYREMKESGVLDKTALV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 246 LNLANDPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGR 325
Cdd:COG0055 210 FGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 326 VegRNGSITQIPILTMPNDDITHPIP-------DLTgyitegqIYVDRQLHNRQIYPPVNVLPSLSRLMKSAI-GEgmtr 397
Cdd:COG0055 290 T--KKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE---- 356
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1663746890 398 kDHSDVSN------QLYacyaigKDVQAMKAVVGEEALTPDD 433
Cdd:COG0055 357 -EHYRVARevqrilQRY------KELQDIIAILGMDELSEED 391
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
52-395 |
2.51e-16 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 81.63 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 52 YAEIVQLKLADGSLRSGQV--LEVSGSKAVVQVFEGTSGIDAKNTHCefTGDILRTPVSEDMLGRVFNGSGKPIDKGPPI 129
Cdd:PTZ00185 64 YNTIIMIQVSPTTFAAGLVfnLEKDGRIGIILMDNITEVQSGQKVMA--TGKLLYIPVGAGVLGKVVNPLGHEVPVGLLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 130 LAEDYLDIQ--------GQPiNPWSRIYPEEMIQTGISAIDVMNSIARGQKIPIFSAaglphneiaaqicRQAGLVKLPG 201
Cdd:PTZ00185 142 RSRALLESEqtlgkvdaGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGD-------------RQTGKTSIAV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 202 KSVLDSHEDNFAI--------VFAAMGVNMETARFFKQDFEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQ 273
Cdd:PTZ00185 208 STIINQVRINQQIlsknavisIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNR 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 274 cEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVE-GRNG-SITQIPILTMPNDDITHPIP 351
Cdd:PTZ00185 288 -GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSpGKGGgSVTALPIVETLSNDVTAYIV 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1663746890 352 DLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAIGEGM 395
Cdd:PTZ00185 367 TNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
239-384 |
3.68e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 81.61 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 239 MENVCLFLNLANDPTIERIITPRLALTAAEF---LAYQcekhVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTD 315
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYfrdMGYD----VALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASK 792
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1663746890 316 LATIYERAGRV-----EGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLS 384
Cdd:PRK14698 793 LAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS 866
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
33-438 |
1.08e-15 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 79.83 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 33 TVSGVNGPLVILDEVKFPKYAEIVqlKLADGSLRsGQVLEVSGSKAVVQVFEGTSGIdAKNTHCEFTGDilrtPVSED-- 110
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVV--RVGEEGLI-GEIIRIEGDKATIQVYEETSGI-KPGEPVEFTGE----PLSVElg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 111 --MLGRVFNG-----------SGKPIDKG---------------------------------------------PP---- 128
Cdd:PRK04192 78 pgLLGSIFDGiqrpldelaekSGDFLERGvyvpaldrekkweftptvkvgdkveagdilgtvqetpsiehkimvPPgvsg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 129 ----ILAE-DY-----------LDIQGQPINPW------------SRIYPEEMIQTGISAIDVMNSIARGQK--IP-IFS 177
Cdd:PRK04192 158 tvkeIVSEgDYtvddtiavledEDGEGVELTMMqkwpvrrprpykEKLPPVEPLITGQRVIDTFFPVAKGGTaaIPgPFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 178 AaglphneiaaqicrqaglvklpGKSVLDSHEDNFA----IVFAAMG--VN-M-ETARFFKQ--DFEENGS-MENVCLFL 246
Cdd:PRK04192 238 S----------------------GKTVTQHQLAKWAdadiVIYVGCGerGNeMtEVLEEFPEliDPKTGRPlMERTVLIA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 247 NLANDPTIER---IITprlALTAAEF---LAYqcekHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIY 320
Cdd:PRK04192 296 NTSNMPVAAReasIYT---GITIAEYyrdMGY----DVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFY 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 321 ERAGRVE---GRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSrLMKSAIGEGMTR 397
Cdd:PRK04192 369 ERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQVAPWWEE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1663746890 398 KDHSDVS---NQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLE 438
Cdd:PRK04192 448 NVDPDWRelrDEAMDLLQREAELQEIVRLVGPDALPEEDRLILE 491
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
99-450 |
1.62e-15 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 78.93 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 99 TGDILRTPVSEDMLGRVFNGSGKPIDKGPPILAEDYLdiqgqPINpwsRIYPE--------EMIQTGISAIDVMNSIARG 170
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS-----PIH---RSAPAfiqldtklSIFETGIKVVDLLAPYRRG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 171 QKIPIFSAAGLphneiaaqicrqaglvklpGKSVLdSHE--DNFA------IVFAAMG----------VNMETARFFKqd 232
Cdd:CHL00060 162 GKIGLFGGAGV-------------------GKTVL-IMEliNNIAkahggvSVFGGVGertregndlyMEMKESGVIN-- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 233 fEENGSMENVCLFLNLANDPTIERIITPRLALTAAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYM 312
Cdd:CHL00060 220 -EQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 313 YTDLATIYERAGRVegRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPVNVLPSLSRLMKSAI- 391
Cdd:CHL00060 299 STEMGSLQERITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIv 376
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1663746890 392 GEgmtrkDHSDVSN------QLYacyaigKDVQAMKAVVGEEALTPDDLLYLEFLSKFEkNFISQ 450
Cdd:CHL00060 377 GE-----EHYETAQrvkqtlQRY------KELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQ 429
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
34-100 |
6.98e-11 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 57.94 E-value: 6.98e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 34 VSGVNGPLVILD--EVKFPKYAEIVQLKLAD-GSLRSGQVLEVSGSKAVVQVFEGTSGIDaKNTHCEFTG 100
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, ... |
400-470 |
2.62e-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: 2.62e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1663746890 400 HSDVSNQLYACYAIGKDVQAMKAVVGEEALTPDDLLYLEFLSKFEKnFISQGSYENRTVFESLDIGWQLLR 470
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, ... |
31-101 |
3.71e-08 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 50.39 E-value: 3.71e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1663746890 31 YKTVSGVNGPLVILDEVKFPKYAEIVQLKLADGSL---RSGQVLEVSGSKAVVQVFEGTSGIDAKnTHCEFTGD 101
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGNNetvLKAEVIGFRGDRAILQLFESTRGLSRG-ALVEPTGR 73
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
37-124 |
3.65e-05 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 46.55 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663746890 37 VNGPLVILDEVKFPKYAEIVQLkladGSL-RSGQVLEVSGSKAVVQVFEGTSGIDAKNThCEFTGDILRTPVSEDMLGRV 115
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVVRV----GELgLIGEIIRLEGDKAVIQVYEETAGLKPGEP-VEGTGSSLSVELGPGLLTSI 84
|
....*....
gi 1663746890 116 FNGSGKPID 124
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 ... |
33-89 |
2.10e-03 |
|
V/A-type ATP synthase catalytic subunit A (alpha), N-terminal domain; The alpha (A) subunit of the V1/A1 complexes of V/A-type ATP synthases, N-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 or A1 complex contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349743 [Multi-domain] Cd Length: 67 Bit Score: 36.73 E-value: 2.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1663746890 33 TVSGVNGPLVILDEVKFPKYAEIVQLkladGSLR-SGQVLEVSGSKAVVQVFEGTSGI 89
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELVRV----GEEGlIGEIIRLEGDKATIQVYEETSGL 56
|
|
| |
