|
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 ... |
19-484 |
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: 975.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 19 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 98
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 99 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 178
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 179 ICRQAGLVKRLEKSdnLLEHQEDdNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 258
Cdd:TIGR01040 161 ICRQAGLVKLPTKD--VHDGHED-NFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 259 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 338
Cdd:TIGR01040 238 AEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 339 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGE 418
Cdd:TIGR01040 318 THPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233891 419 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFYSRD 484
Cdd:TIGR01040 398 EALSSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRK 463
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
19-481 |
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: 851.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 19 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 98
Cdd:COG1156 5 EYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELPVSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 99 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 178
Cdd:COG1156 85 DMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 179 ICRQAGLVKrleksdnllehqEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 258
Cdd:COG1156 165 IARQAKVRG------------EEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 259 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 338
Cdd:COG1156 233 AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 339 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGE 418
Cdd:COG1156 313 THPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233891 419 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFY 481
Cdd:COG1156 393 EALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYY 455
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
19-481 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 829.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 19 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 98
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 99 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 178
Cdd:PRK04196 83 DMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 179 ICRQAGLVKrleksdnllehqEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 258
Cdd:PRK04196 163 IARQAKVLG------------EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 259 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 338
Cdd:PRK04196 231 AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 339 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGE 418
Cdd:PRK04196 311 THPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15233891 419 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFY 481
Cdd:PRK04196 391 EALSERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYH 453
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
19-484 |
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: 713.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 19 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 98
Cdd:TIGR01041 1 EYSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 99 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 178
Cdd:TIGR01041 81 DMLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 179 ICRQAGLVkrleksdnllehQEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 258
Cdd:TIGR01041 161 IARQATVR------------GEESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 259 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 338
Cdd:TIGR01041 229 AEYLAFEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 339 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGE 418
Cdd:TIGR01041 309 THPIPDLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15233891 419 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFYSRD 484
Cdd:TIGR01041 389 EALSERDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYHPKY 454
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
91-384 |
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: 614.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 91 VLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGL 170
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 171 PHNEIAAQICRQAGLVKrleksdnllehqEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERII 250
Cdd:cd01135 81 PHNELAAQIARQAGVVG------------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 251 TPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPI 330
Cdd:cd01135 149 TPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 15233891 331 LTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIG 384
Cdd:cd01135 229 LTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
20-487 |
2.46e-127 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 377.07 E-value: 2.46e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 20 YRTVSGVAGPLVILeKVKGPKYQEIVNIRLGDGTtRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLD 99
Cdd:PRK02118 5 YTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGISTG-DEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 100 MLGRIFNGSGKPIDNGPPILPEAyLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQI 179
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 180 CRQAglvkrleksdnllehqEDDnfAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTA 259
Cdd:PRK02118 161 ALQA----------------EAD--IIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 260 EYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDIT 339
Cdd:PRK02118 223 EKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 340 HPTPDLTGYITEGQIYidrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRRDHSDVSN---QLYANYAIGKDVQAMkavv 416
Cdd:PRK02118 302 HPVPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM---- 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15233891 417 GEEaLSSEDLLYLEFLDKFERKFVAQGAydtrNI--FQSLDLAWTLL-RIF-PRELLhrIPAKTLDQFYSRDTTN 487
Cdd:PRK02118 369 GFK-LSNWDEKLLKFSELFESRLMDLEV----NIplEEALDLGWKILaQCFhPEEVG--IKEQLIDKYWPKNCLH 436
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
93-378 |
1.01e-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: 323.64 E-value: 1.01e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 93 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPH 172
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 173 NEIAAQICRQAglvkrleksdnllehQEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITP 252
Cdd:cd19476 81 TVLAMQLARNQ---------------AKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 253 RIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILT 332
Cdd:cd19476 146 YTGLTIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVS 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15233891 333 MPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRL 378
Cdd:cd19476 225 TPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
146-376 |
8.81e-107 |
|
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: 316.22 E-value: 8.81e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 146 GISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvkrleksdnllehqEDDnfAIVFAAMGVNMETAQFFKRDF 225
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA----------------SAD--VVVYALIGERGREVREFIEEL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 226 EENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMY 305
Cdd:pfam00006 63 LGSGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233891 306 TDLATIYERAGRIEGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLS 376
Cdd:pfam00006 142 SLLARLLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| 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 ... |
386-480 |
1.62e-58 |
|
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: 188.03 E-value: 1.62e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 386 GMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFP 465
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 15233891 466 RELLHRIPAKTLDQF 480
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
93-378 |
9.85e-43 |
|
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: 152.33 E-value: 9.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 93 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPH 172
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 173 NEIAAQICRQAglvkrleKSDnllehqeddnfAIVFAAMGVN-METAQFFKRDFEENGsMERVTLFLNLANDPTIERIIT 251
Cdd:cd01136 81 STLLGMIARNT-------DAD-----------VNVIALIGERgREVREFIEKDLGEEG-LKRSVLVVATSDESPLLRVRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 252 PRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRieGRKGSITQIPIL 331
Cdd:cd01136 142 AYTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15233891 332 TMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRL 378
Cdd:cd01136 219 LVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
22-404 |
2.06e-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: 2.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 22 TVSGVAGPLVileKVKGPKYQ--EIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGI--DNKyttVQFTGEVLKTPVS 97
Cdd:COG1157 22 RVTRVVGLLI---EAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGIspGAR---VVPTGRPLSVPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 98 LDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAG------Lp 171
Cdd:COG1157 96 DGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 172 hneiaAQICRQAglvkrleKSDnllehqeddnfAIVFAAMG-----VnmetaqffkRDFEEN--GS--MER-----VTlf 237
Cdd:COG1157 175 -----GMIARNT-------EAD-----------VNVIALIGergreV---------REFIEDdlGEegLARsvvvvAT-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 238 lnlANDPTIERIITPRIALTTAEYLAyECGKHVLVIltdMSS---YADALREVSAAREEVPGRRGYPGYMYTDLATIYER 314
Cdd:COG1157 221 ---SDEPPLMRLRAAYTATAIAEYFR-DQGKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLER 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 315 AGRieGRKGSITQI-PILTmPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHS 393
Cdd:COG1157 294 AGN--GGKGSITAFyTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSP-----EHR 365
|
410
....*....|....
gi 15233891 394 DVSN---QLYANYA 404
Cdd:COG1157 366 ALARrlrRLLARYE 379
|
|
| 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 ... |
19-90 |
4.15e-41 |
|
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: 141.41 E-value: 4.15e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233891 19 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGE 90
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
83-382 |
1.85e-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: 152.16 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 83 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISgsSINPS--ERTYPEEMIQTGISTIDVMNSIARGQ 160
Cdd:TIGR00962 85 STVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVE--KIAPGviERKSVHEPLQTGIKAIDAMIPIGRGQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 161 KIPLFSAaglphneiaaqicRQAGlvKRLEKSDNLLeHQEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNL 240
Cdd:TIGR00962 163 RELIIGD-------------RQTG--KTAVAIDTII-NQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAAT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 241 ANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGR 317
Cdd:TIGR00962 227 ASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAK 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15233891 318 I--EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSA 382
Cdd:TIGR00962 303 LndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
83-379 |
1.42e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 145.67 E-value: 1.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 83 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKI 162
Cdd:PRK06936 86 TEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 163 PLFSAAGLPHNEIAAQICRQAglvkrleksdnllehqedDNFAIVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLA 241
Cdd:PRK06936 166 GIFAAAGGGKSTLLASLIRSA------------------EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 242 NDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGriEGR 321
Cdd:PRK06936 227 DRPSMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSD 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15233891 322 KGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 379
Cdd:PRK06936 304 KGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVM 361
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
56-461 |
2.81e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 139.18 E-value: 2.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 56 RGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPiLPEAYLDISGSSINPSE 135
Cdd:PRK06820 62 LAEVVSIEQEMALLSPFASSDGLRCG-QWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 136 RTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICrqaglvkrleksdnllEHQEDDnfAIVFAAMGvnm 215
Cdd:PRK06820 140 RQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC----------------ADSAAD--VMVLALIG--- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 216 ETAQFFKRDFEENGSME---RVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAARE 292
Cdd:PRK06820 199 ERGREVREFLEQVLTPEaraRTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 293 EVPGRRGYPGYMYTDLATIYERAGRIEgrKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVL 372
Cdd:PRK06820 278 EPPAAGSFPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 373 PSLSRLMKSAIGEGmtRRDHSDVSNQLYANYaigKDVQAMKAVvgEEALSSEDLLYLEFLDKFE--RKFVAQGAYDTRNI 450
Cdd:PRK06820 356 ASVSRIMPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHL 428
|
410
....*....|.
gi 15233891 451 FQSLDLAWTLL 461
Cdd:PRK06820 429 ETTLEHLAQVV 439
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
91-377 |
1.49e-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: 130.37 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 91 VLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAY--LDISGSSINPSERTYpeEMIQTGISTIDVMNSIARGQKiplfsaa 168
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERrrVESKAPGIIPRQSVN--EPLQTGIKAIDSLIPIGRGQR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 169 glphnEIaaqIC--RQAGlvkrleKS----DNLLeHQEDDNFAIVFAAMGVNMET-AQFFKRdFEENGSMERVTLFLNLA 241
Cdd:cd01132 72 -----EL---IIgdRQTG------KTaiaiDTII-NQKGKKVYCIYVAIGQKRSTvAQIVKT-LEEHGAMEYTIVVAATA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 242 NDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRI 318
Cdd:cd01132 136 SDPAPLQYLAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKL 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233891 319 --EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 377
Cdd:cd01132 212 sdELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
85-442 |
7.97e-34 |
|
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: 132.92 E-value: 7.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 85 VQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPL 164
Cdd:TIGR01039 69 VIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 165 FSAAGLPHNEIAAQicrqagLVKRLEKsdnllEHqeddNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDP 244
Cdd:TIGR01039 149 FGGAGVGKTVLIQE------LINNIAK-----EH----GGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 245 TIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIegRKGS 324
Cdd:TIGR01039 214 PGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITST--KTGS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 325 ITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrrDHSDVSNQLYANY 403
Cdd:TIGR01039 292 ITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQIL 366
|
330 340 350
....*....|....*....|....*....|....*....
gi 15233891 404 AIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQ 442
Cdd:TIGR01039 367 QRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
39-385 |
8.41e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 129.42 E-value: 8.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 39 PKYQEIVNIRLGD-GTTRRGQVLEVDGEKAVVQVFEGTSG--IDNKyttVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNG 115
Cdd:PRK08472 37 PSVGDIVKIESSDnGKECLGMVVVIEKEQFGISPFSFIEGfkIGDK---VFISKEGLNIPVGRNLLGRVVDPLGRPIDGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 116 PPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQA-GLVKrleksdn 194
Cdd:PRK08472 114 GAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGClAPIK------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 195 llehqeddnfaiVFAAMGVN-METAQFFKRDFeeNGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVI 273
Cdd:PRK08472 187 ------------VVALIGERgREIPEFIEKNL--GGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK-NQGLDVLFI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 274 LTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDITHPTPDLTGYITEGQ 353
Cdd:PRK08472 252 MDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEG-KGSITAFFTVLVEGDDMSDPIADQSRSILDGH 330
|
330 340 350
....*....|....*....|....*....|..
gi 15233891 354 IYIDRQLHNRQIYPPINVLPSLSRLMKSAIGE 385
Cdd:PRK08472 331 IVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
55-377 |
6.15e-32 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 128.11 E-value: 6.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 55 RRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPS 134
Cdd:PRK13343 59 SRGFAFNLEEELVGAVLLDDTADI-LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAII 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 135 ERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAqicrqaglvkrleksDNLLeHQEDDNFAIVFAAMGVN 214
Cdd:PRK13343 138 ERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAI---------------DAII-NQKDSDVICVYVAIGQK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 215 METAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEV 294
Cdd:PRK13343 202 ASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRP 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 295 PGRRGYPGYMYTDLATIYERAGRIEGRK--GSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVL 372
Cdd:PRK13343 281 PGREAYPGDIFYLHSRLLERAAKLSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVG 360
|
....*
gi 15233891 373 PSLSR 377
Cdd:PRK13343 361 LSVSR 365
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
58-412 |
4.74e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 124.68 E-value: 4.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 58 QVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPpiLPEA-YLDISGSSINPSER 136
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGLHCG-QQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRE--LPDVcWKDYDAMPPPAMVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 137 TYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAGLvkrleksdnllehqeDDNFAIVFAAMGvnME 216
Cdd:PRK07594 133 QPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA---------------DSNVLVLIGERG--RE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 217 TAQFFKRDFEENgSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPG 296
Cdd:PRK07594 196 VREFIDFTLSEE-TRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 297 RRGYPGYMYTDLATIYERAGRieGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLS 376
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
330 340 350
....*....|....*....|....*....|....*.
gi 15233891 377 RLMKSAIGEgmtrrDHSDVSNQLYANYAIGKDVQAM 412
Cdd:PRK07594 352 RVFPVVTSH-----EHRQLAAILRRCLALYQEVELL 382
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
20-408 |
4.80e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 124.45 E-value: 4.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 20 YRTVSGVAGpLVIleKVKGPKYQ--EIVNIRLGDGTTR--RGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTP 95
Cdd:PRK07721 19 YGKVSRVIG-LMI--ESKGPESSigDVCYIHTKGGGDKaiKAEVVGFKDEHVLLMPYTEVAEIAPG-CLVEATGKPLEVK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 96 VSLDMLGRIFNGSGKPIDNGPpiLPEAYLDIS--GSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHN 173
Cdd:PRK07721 95 VGSGLIGQVLDALGEPLDGSA--LPKGLAPVStdQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 174 EIAAQICRQAglvkrleksdnllehQEDDNfaiVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITP 252
Cdd:PRK07721 173 TLMGMIARNT---------------SADLN---VIALIGErGREVREFIERDLGPEG-LKRSIVVVATSDQPALMRIKGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 253 RIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEgrKGSITQIPILT 332
Cdd:PRK07721 234 YTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSITAFYTVL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15233891 333 MPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHSDVSN---QLYANYAIGKD 408
Cdd:PRK07721 311 VDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQNSED 384
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
95-416 |
1.06e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 123.69 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 95 PVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNE 174
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 175 IAaqicrqaGLVKRLEKSDnllehqeddnfAIVFAAMGVN-METAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPR 253
Cdd:PRK05688 184 LL-------GMMTRFTEAD-----------IIVVGLIGERgREVKEFIEHILGEEG-LKRSVVVASPADDAPLMRLRAAM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 254 IALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTM 333
Cdd:PRK05688 245 YCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 334 PNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRdhSDVSNQLYANYAIGKDVQAMK 413
Cdd:PRK05688 324 EGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRR--AQRFKQLWSRYQQSRDLISVG 401
|
...
gi 15233891 414 AVV 416
Cdd:PRK05688 402 AYV 404
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
23-399 |
1.62e-30 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 122.95 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 23 VSGVAGPLVileKVKG--PKYQEIVNIRLGDGT-TRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLD 99
Cdd:PRK09099 28 VVEVIGTLL---RVSGldVTLGELCELRQRDGTlLQRAEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 100 MLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQI 179
Cdd:PRK09099 104 LLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 180 CRQAglvkrleksdnllehQEDDNFAIVFAAMGvnMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTTA 259
Cdd:PRK09099 184 ARGT---------------QCDVNVIALIGERG--REVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 260 EYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRieGRKGSITQIPILTMPNDDIT 339
Cdd:PRK09099 246 EYFR-DRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 340 HPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSaigegMTRRDHSDVSNQL 399
Cdd:PRK09099 323 DPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQ-----VVPREHVQAAGRL 377
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
58-408 |
1.52e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 120.08 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 58 QVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERT 137
Cdd:PRK06793 56 EVIAIEKENNMLLPFEQTEKVCYG-DSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFERE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 138 YPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvkrleksdnllehQEDDNFAIVFAAMGvnMET 217
Cdd:PRK06793 135 EITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNA---------------KADINVISLVGERG--REV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 218 AQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPgR 297
Cdd:PRK06793 198 KDFIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELP-I 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 298 RGYPGYMYTDLATIYERAGRIEgrKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 377
Cdd:PRK06793 275 GGKTLLMESYMKKLLERSGKTQ--KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSR 352
|
330 340 350
....*....|....*....|....*....|.
gi 15233891 378 LMKSAIGEgmtrrDHSDVSNQLYANYAIGKD 408
Cdd:PRK06793 353 IMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
47-382 |
9.40e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 118.18 E-value: 9.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 47 IRLGD-------GTTRRGQVLEVDGEKAVVQVFEgtSGIDNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDnGPPIL 119
Cdd:PRK06002 47 VRLGDfvairadGGTHLGEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPID-GLGPL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 120 PEAYLDISGSSINPS--ERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAGLVKrleksdnlle 197
Cdd:PRK06002 124 APGTRPMSIDATAPPamTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDT---------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 198 hqeddnfaIVFAAMG-----VnmetaqffkRDFEEN---GSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKH 269
Cdd:PRK06002 194 --------VVIALVGergreV---------REFLEDtlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFR-DRGEN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 270 VLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDITHPTPDLTGYI 349
Cdd:PRK06002 256 VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGT 335
|
330 340 350
....*....|....*....|....*....|...
gi 15233891 350 TEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSA 382
Cdd:PRK06002 336 LDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
57-382 |
3.66e-28 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 116.99 E-value: 3.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 57 GQVLEVDGekavVQVFEGTSgidnkyttVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSER 136
Cdd:CHL00059 51 GVVLMGDG----LMIQEGSS--------VKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 137 TYPEEMIQTGISTIDVMNSIARGQKiplfsaaglphnEIaaqIC--RQAGlvKRLEKSDNLLeHQEDDNFAIVFAAMGVN 214
Cdd:CHL00059 119 RSVYEPLQTGLIAIDSMIPIGRGQR------------EL---IIgdRQTG--KTAVATDTIL-NQKGQNVICVYVAIGQK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 215 METAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEV 294
Cdd:CHL00059 181 ASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 295 PGRRGYPG---YMYTDLatiYERAGRIEGR--KGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPI 369
Cdd:CHL00059 260 PGREAYPGdvfYLHSRL---LERAAKLSSQlgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAI 336
|
330
....*....|...
gi 15233891 370 NVLPSLSRLMKSA 382
Cdd:CHL00059 337 NVGISVSRVGSAA 349
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
43-378 |
7.90e-28 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 115.09 E-value: 7.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 43 EIVNIRLG---DGTTRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGK---PIDNGP 116
Cdd:PRK08149 29 EICEIRAGwhsNEVIARAQVVGFQRERTILSLIGNAQGL-SRQVVLKPTGKPLSVWVGEALLGAVLDPTGKiveRFDAPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 117 PILPEA-YLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGlphneiaaqiCRQAGLVKRLeksdnl 195
Cdd:PRK08149 108 TVGPISeERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAG----------CGKTSLMNML------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 196 LEHQEDDNFAIvfAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILT 275
Cdd:PRK08149 172 IEHSEADVFVI--GLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFR-DQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 276 DMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIegRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIY 355
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIY 326
|
330 340
....*....|....*....|...
gi 15233891 356 IDRQLHNRQIYPPINVLPSLSRL 378
Cdd:PRK08149 327 LSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
85-414 |
2.28e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 114.03 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 85 VQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPL 164
Cdd:PRK08972 88 VTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 165 FSAAGLPHNEIAaqicrqaGLVKRLEKSDnllehqeddnfAIVFAAMGV-NMETAQFFKRDFEENGSMERVTLFLNLAND 243
Cdd:PRK08972 168 FAGSGVGKSVLL-------GMMTRGTTAD-----------VIVVGLVGErGREVKEFIEEILGEEGRARSVVVAAPADTS 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 244 PTIeRIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKG 323
Cdd:PRK08972 230 PLM-RLKGCETATTIAEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQG 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 324 SITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHSDVS---NQLY 400
Cdd:PRK08972 308 SITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVY 382
|
330
....*....|....
gi 15233891 401 ANYAIGKDVQAMKA 414
Cdd:PRK08972 383 SLYQQNRDLISIGA 396
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
95-427 |
1.05e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 112.18 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 95 PVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNE 174
Cdd:PRK07960 111 PLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 175 IAaqicrqaGLVKRLEKSDnllehqeddnfAIVFAAMGvnmETAQFFKrDFEEN----GSMERVTLFLNLANDPTIERII 250
Cdd:PRK07960 191 LL-------GMMARYTQAD-----------VIVVGLIG---ERGREVK-DFIENilgaEGRARSVVIAAPADVSPLLRMQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 251 TPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPI 330
Cdd:PRK07960 249 GAAYATRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 331 LTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSdvSNQLYANYAIGKDVQ 410
Cdd:PRK07960 328 VLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQ--FKQLLSSFQRNRDLV 405
|
330
....*....|....*..
gi 15233891 411 AmkavVGEEALSSEDLL 427
Cdd:PRK07960 406 S----VGAYAKGSDPML 418
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
93-379 |
1.38e-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: 105.76 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 93 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAG--- 169
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGvgk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 170 ------LPHNeIAAqicRQAGLVkrleksdnllehqeddnfaiVFAAMGVNMETAQFFKRDFEENG-----SMERVTLFL 238
Cdd:cd01133 81 tvlimeLINN-IAK---AHGGYS--------------------VFAGVGERTREGNDLYHEMKESGvinldGLSKVALVY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 239 NLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRI 318
Cdd:cd01133 137 GQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233891 319 egRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 379
Cdd:cd01133 217 --KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
101-444 |
1.53e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 105.74 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 101 LGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQIC 180
Cdd:PRK07196 97 LGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMIT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 181 RqaglvkrleksdnlleHQEDDnfAIVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTTA 259
Cdd:PRK07196 177 R----------------YTQAD--VVVVGLIGErGREVKEFIEHSLQAAG-MAKSVVVAAPADESPLMRIKATELCHAIA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 260 EYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDIT 339
Cdd:PRK07196 238 TYYR-DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 340 HPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHSDVSNQL---YANYAIGKDVQAMKAVV 416
Cdd:PRK07196 316 DPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGS-----QQAKAASLLkqcYADYMAIKPLIPLGGYV 390
|
330 340
....*....|....*....|....*....
gi 15233891 417 -GEEALSSEDLLYLEFLDKFERKFVAQGA 444
Cdd:PRK07196 391 aGADPMADQAVHYYPAITQFLRQEVGHPA 419
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
84-377 |
2.31e-24 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 105.92 E-value: 2.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 84 TVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDIsgssinpsERTYP--------EEMIQTGISTIDVMNS 155
Cdd:PRK09281 87 TVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPV--------ERKAPgvidrksvHEPLQTGIKAIDAMIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 156 IARGQKiplfsaaglphnEIaaqIC--RQAGlvkrleKS----DNLLeHQEDDNFAIVFAAMGVNMET-AQFfKRDFEEN 228
Cdd:PRK09281 159 IGRGQR------------EL---IIgdRQTG------KTaiaiDTII-NQKGKDVICIYVAIGQKASTvAQV-VRKLEEH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 229 GSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMY 305
Cdd:PRK09281 216 GAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDN-GKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 306 TDLatiYERAGRI--EGRKGSITQIPIL-TMPNDdithptpdLTGY-------ITEGQIYIDRQLHNRQIYPPINVLPSL 375
Cdd:PRK09281 295 SRL---LERAAKLsdELGGGSLTALPIIeTQAGD--------VSAYiptnvisITDGQIFLESDLFNAGIRPAINVGISV 363
|
..
gi 15233891 376 SR 377
Cdd:PRK09281 364 SR 365
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
84-377 |
4.91e-24 |
|
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: 104.74 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 84 TVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDIsgssinpsERTYP--------EEMIQTGISTIDVMNS 155
Cdd:COG0056 87 TVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPV--------ERPAPgvidrqpvHEPLQTGIKAIDAMIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 156 IARGQKiplfsaaglphnEIaaqIC--RQAGlvkrleKS----DNLLeHQEDDNFAIVFAAMGVNMETAQFFKRDFEENG 229
Cdd:COG0056 159 IGRGQR------------EL---IIgdRQTG------KTaiaiDTII-NQKGKDVICIYVAIGQKASTVAQVVETLEEHG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 230 SMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMYT 306
Cdd:COG0056 217 AMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 307 DLatiYERAGRI--EGRKGSITQIPIL-TMPNddithptpDLTGY-------ITEGQIYIDRQLHNRQIYPPINVLPSLS 376
Cdd:COG0056 296 RL---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLSVS 364
|
.
gi 15233891 377 R 377
Cdd:COG0056 365 R 365
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
95-377 |
2.95e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 101.90 E-value: 2.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 95 PVSLDMLGRIFNGSGKPIDNGPPiLPEAYLD-ISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHN 173
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQ-LPKTHLKpLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 174 EIAAQICRQAglvkrleksdnllehQEDDNfaiVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPR 253
Cdd:PRK05922 172 SLLSTIAKGS---------------KSTIN---VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 254 IALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEgrKGSITQI-PILT 332
Cdd:PRK05922 234 AAMTIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILH 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 15233891 333 MPNdditHPT--PDLTGYITEGQIYIDRQlHNRQIYPPINVLPSLSR 377
Cdd:PRK05922 311 YPN----HPDifTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
12-379 |
1.47e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 96.97 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 12 GTLEIGMEYRTVSGVAGPLVileKVKGPKYQEIVNIRL----GDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVqF 87
Cdd:PRK08927 10 GDIDTLVIYGRVVAVRGLLV---EVAGPIHALSVGARIvvetRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAV-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 88 TGEVLKTPVSLDMLGRIFNGSGKPIDNGPPiLPEayldisGSSINPSERTYPE--------EMIQTGISTIDVMNSIARG 159
Cdd:PRK08927 86 ANAAAAVRPSRAWLGRVVNALGEPIDGKGP-LPQ------GPVPYPLRAPPPPahsrarvgEPLDLGVRALNTFLTCCRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 160 QKIPLFSAAGLPHNEIAAQICRQAglvkrleksdnllehqedDNFAIVFAAMGVN-METAQFFKRDFEENGsMERVTLFL 238
Cdd:PRK08927 159 QRMGIFAGSGVGKSVLLSMLARNA------------------DADVSVIGLIGERgREVQEFLQDDLGPEG-LARSVVVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 239 NLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRI 318
Cdd:PRK08927 220 ATSDEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPG 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233891 319 EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 379
Cdd:PRK08927 299 PIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
83-425 |
2.28e-21 |
|
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: 96.70 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 83 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKI 162
Cdd:COG0055 70 MEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 163 PLFSAAG---------LPHNeIAAQicrQAGLVkrleksdnllehqeddnfaiVFAamGVNMET--AQFFKRDFEENGSM 231
Cdd:COG0055 150 GLFGGAGvgktvlimeLIHN-IAKE---HGGVS--------------------VFA--GVGERTreGNDLYREMKESGVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 232 ERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATI 311
Cdd:COG0055 204 DKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGAL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 312 YEragRI-EGRKGSITQIPILTMPNDDITHPTP-------DLTgyitegqIYIDRQLHNRQIYPPINVLPSLSRLMKSAI 383
Cdd:COG0055 284 QE---RItSTKKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLI 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 15233891 384 -GEgmtrrDHSDVSN---QLYANYaigKDVQAMKAVVGEEALSSED 425
Cdd:COG0055 354 vGE-----EHYRVARevqRILQRY---KELQDIIAILGMDELSEED 391
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
22-387 |
5.90e-20 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 92.80 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 22 TVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQV--LEVDGEKAVV---QVFEGTSGidnkyTTVQFTGEVLKTPV 96
Cdd:PTZ00185 45 SIDGTIATLIPAPGNPGVAYNTIIMIQVSPTTFAAGLVfnLEKDGRIGIIlmdNITEVQSG-----QKVMATGKLLYIPV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 97 SLDMLGRIFNGSGKPIDNGPPILPEAYLD-------ISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAG 169
Cdd:PTZ00185 120 GAGVLGKVVNPLGHEVPVGLLTRSRALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 170 LPHNEIAAqicrqAGLVKRLEKSDNLLEHqedDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERI 249
Cdd:PTZ00185 200 TGKTSIAV-----STIINQVRINQQILSK---NAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 250 ITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRK--GSITQ 327
Cdd:PTZ00185 272 LAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKggGSVTA 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 328 IPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 387
Cdd:PTZ00185 351 LPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
22-446 |
6.22e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 92.92 E-value: 6.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 22 TVSGVAGPLVILEKVKGPKYQEIV---NIRLgdgttrRGQVLEVDGEKAVVQVFEGTSGI---DnkytTVQFTGEvlktP 95
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVrvgEEGL------IGEIIRIEGDKATIQVYEETSGIkpgE----PVEFTGE----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 96 VSLD----MLGRIFNG-----------SGKPIDNG---PPI--------------------------LPEAYL------- 124
Cdd:PRK04192 72 LSVElgpgLLGSIFDGiqrpldelaekSGDFLERGvyvPALdrekkweftptvkvgdkveagdilgtVQETPSiehkimv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 125 --DISG--SSINPS-------------------------------------ERTYPEEMIQTGISTIDVMNSIARGQK-- 161
Cdd:PRK04192 152 ppGVSGtvKEIVSEgdytvddtiavlededgegveltmmqkwpvrrprpykEKLPPVEPLITGQRVIDTFFPVAKGGTaa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 162 IPLFSAAG---LPHneiaaQICRQAglvkrleksdnllehqedDNFAIVFAAMG--VNmETAQFFkRDFEE-------NG 229
Cdd:PRK04192 232 IPGPFGSGktvTQH-----QLAKWA------------------DADIVIYVGCGerGN-EMTEVL-EEFPElidpktgRP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 230 SMERVTLFLNLANDPTIER---IITpriALTTAEYlaY-ECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMY 305
Cdd:PRK04192 287 LMERTVLIANTSNMPVAAReasIYT---GITIAEY--YrDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 306 TDLATIYERAGRIE---GRKGSITQIPILTMPNDDITHPtpdltgyITEGQIYI-------DRQLHNRQIYPPINVLPSL 375
Cdd:PRK04192 362 SRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEP-------VTQNTLRIvkvfwalDAELADRRHFPAINWLTSY 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15233891 376 SrLMKSAIGEGMTRRDHSDVSNqlYANYAI-----GKDVQAMKAVVGEEALSSEDLLYLE---FLDKFerkFVAQGAYD 446
Cdd:PRK04192 435 S-LYLDQVAPWWEENVDPDWRE--LRDEAMdllqrEAELQEIVRLVGPDALPEEDRLILEvarLIRED---FLQQNAFD 507
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
231-377 |
8.05e-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: 89.56 E-value: 8.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 231 MERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLAT 310
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15233891 311 IYERAGRIE-----GRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 377
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
231-464 |
2.06e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 91.62 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 231 MERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLAT 310
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 311 IYERAGRI-----EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSrLMKSAIGE 385
Cdd:PRK14698 796 FYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS-LYVDAVKD 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 386 GMTR------RDHSDVSNQLYANYAigkDVQAMKAVVGEEALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWT 459
Cdd:PRK14698 875 WWHKnvdpewKAMRDKAMELLQKEA---ELQEIVRIVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVT 951
|
....*
gi 15233891 460 LLRIF 464
Cdd:PRK14698 952 MMRVL 956
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
97-403 |
1.50e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 88.11 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 97 SLDMLGRIFNGSGKPIdngPPI----LPEAYLDISGSSINPS----ERTYPEEMIQTGISTIDVMNSIARGQKiplfsaa 168
Cdd:PRK07165 76 SKEYFGKIIDIDGNII---YPEaqnpLSKKFLPNTSSIFNLAhglmTVKTLNEQLYTGIIAIDLLIPIGKGQR------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 169 glphnEIaaqIC--RQAGlvkrleKSD---NLLEHQEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERvTLFLNLAND 243
Cdd:PRK07165 146 -----EL---IIgdRQTG------KTHialNTIINQKNTNVKCIYVAIGQKRENLSRIYETLKEHDALKN-TIIIDAPST 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 244 PTIERIITPRIALTTAEYLAYEcgKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKg 323
Cdd:PRK07165 211 SPYEQYLAPYVAMAHAENISYN--DDVLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 324 SITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRlmksaIGEGMTRRDHSDVS---NQLY 400
Cdd:PRK07165 288 TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR-----TGSSVQSKTITKVAgeiSKIY 362
|
...
gi 15233891 401 ANY 403
Cdd:PRK07165 363 RAY 365
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
88-442 |
2.18e-18 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 87.79 E-value: 2.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 88 TGEVLKTPVSLDMLGRIFNGSGKPIDN-GPpilpeayldISGSSINPSERTYPE--------EMIQTGISTIDVMNSIAR 158
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGP---------VDTRTTSPIHRSAPAfiqldtklSIFETGIKVVDLLAPYRR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 159 GQKIPLFSAAGLPHN----EIAAQICRQAGLVKrleksdnllehqeddnfaiVFAAMG--------VNMETAQFFKRDfE 226
Cdd:CHL00060 161 GGKIGLFGGAGVGKTvlimELINNIAKAHGGVS-------------------VFGGVGertregndLYMEMKESGVIN-E 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 227 ENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYT 306
Cdd:CHL00060 221 QNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLST 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 307 DLATIYERAGRIegRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAI-GE 385
Cdd:CHL00060 301 EMGSLQERITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 15233891 386 gmtrrDHSDVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQ 442
Cdd:CHL00060 379 -----EHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 429
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
23-89 |
7.45e-13 |
|
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: 63.33 E-value: 7.45e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 23 VSGVAGPLVILEKVKGPKYQEIVNIRLG---DGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTG 89
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVElveFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRG-DEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
20-90 |
6.14e-12 |
|
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: 61.17 E-value: 6.14e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15233891 20 YRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDG---TTRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGE 90
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGnneTVLKAEVIGFRGDRAILQLFESTRGLSRG-ALVEPTGR 73
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
392-462 |
1.09e-08 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 51.68 E-value: 1.09e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15233891 392 HSDVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQGAYDTRNIFQSLDLAWTLLR 462
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
26-113 |
2.30e-06 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 50.41 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15233891 26 VAGPLVILEKVKGPKYQEIVniRLGDgTTRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIF 105
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVV--RVGE-LGLIGEIIRLEGDKAVIQVYEETAGL-KPGEPVEGTGSSLSVELGPGLLTSIY 85
|
....*...
gi 15233891 106 NGSGKPID 113
Cdd:PRK14698 86 DGIQRPLE 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 ... |
22-78 |
4.41e-06 |
|
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: 44.05 E-value: 4.41e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15233891 22 TVSGVAGPLVILEKVKGPKYQEIVniRLGDgttRR--GQVLEVDGEKAVVQVFEGTSGI 78
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELV--RVGE---EGliGEIIRLEGDKATIQVYEETSGL 56
|
|
| |
