|
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 ... |
26-491 |
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: 975.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 26 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 105
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 106 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 185
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 186 ICRQAGLVKRLEKSdnLLEHQEDdNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 265
Cdd:TIGR01040 161 ICRQAGLVKLPTKD--VHDGHED-NFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 266 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 345
Cdd:TIGR01040 238 AEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 346 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGE 425
Cdd:TIGR01040 318 THPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187279 426 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFYSRD 491
Cdd:TIGR01040 398 EALSSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRK 463
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
26-488 |
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 334187279 26 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 105
Cdd:COG1156 5 EYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELPVSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 106 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 185
Cdd:COG1156 85 DMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 186 ICRQAGLVKrleksdnllehqEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 265
Cdd:COG1156 165 IARQAKVRG------------EEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 266 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 345
Cdd:COG1156 233 AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 346 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGE 425
Cdd:COG1156 313 THPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187279 426 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFY 488
Cdd:COG1156 393 EALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYY 455
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
26-488 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 829.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 26 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 105
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 106 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 185
Cdd:PRK04196 83 DMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 186 ICRQAGLVKrleksdnllehqEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 265
Cdd:PRK04196 163 IARQAKVLG------------EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 266 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 345
Cdd:PRK04196 231 AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 346 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGE 425
Cdd:PRK04196 311 THPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334187279 426 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFY 488
Cdd:PRK04196 391 EALSERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYH 453
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
26-491 |
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: 713.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 26 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 105
Cdd:TIGR01041 1 EYSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 106 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 185
Cdd:TIGR01041 81 DMLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 186 ICRQAGLVkrleksdnllehQEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 265
Cdd:TIGR01041 161 IARQATVR------------GEESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 266 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 345
Cdd:TIGR01041 229 AEYLAFEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 346 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGE 425
Cdd:TIGR01041 309 THPIPDLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187279 426 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQFYSRD 491
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 ... |
98-391 |
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: 615.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 98 VLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGL 177
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 178 PHNEIAAQICRQAGLVKrleksdnllehqEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERII 257
Cdd:cd01135 81 PHNELAAQIARQAGVVG------------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 258 TPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPI 337
Cdd:cd01135 149 TPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 334187279 338 LTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIG 391
Cdd:cd01135 229 LTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
27-494 |
3.47e-127 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 377.07 E-value: 3.47e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 27 YRTVSGVAGPLVILeKVKGPKYQEIVNIRLGDGTtRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLD 106
Cdd:PRK02118 5 YTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGISTG-DEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 107 MLGRIFNGSGKPIDNGPPILPEAyLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQI 186
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 187 CRQAglvkrleksdnllehqEDDnfAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTA 266
Cdd:PRK02118 161 ALQA----------------EAD--IIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 267 EYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDIT 346
Cdd:PRK02118 223 EKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 347 HPTPDLTGYITEGQIYidrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRRDHSDVSN---QLYANYAIGKDVQAMkavv 423
Cdd:PRK02118 302 HPVPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM---- 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334187279 424 GEEaLSSEDLLYLEFLDKFERKFVAQGAydtrNI--FQSLDLAWTLL-RIF-PRELLhrIPAKTLDQFYSRDTTN 494
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 ... |
100-385 |
9.52e-109 |
|
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: 324.02 E-value: 9.52e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 100 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPH 179
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 180 NEIAAQICRQAglvkrleksdnllehQEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITP 259
Cdd:cd19476 81 TVLAMQLARNQ---------------AKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 260 RIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILT 339
Cdd:cd19476 146 YTGLTIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVS 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 334187279 340 MPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRL 385
Cdd:cd19476 225 TPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
153-383 |
9.02e-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: 316.61 E-value: 9.02e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 153 GISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvkrleksdnllehqEDDnfAIVFAAMGVNMETAQFFKRDF 232
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA----------------SAD--VVVYALIGERGREVREFIEEL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 233 EENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMY 312
Cdd:pfam00006 63 LGSGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187279 313 TDLATIYERAGRIEGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLS 383
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 ... |
393-487 |
2.32e-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: 187.64 E-value: 2.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 393 GMTRRDHSDVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFP 472
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 334187279 473 RELLHRIPAKTLDQF 487
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
100-385 |
1.05e-42 |
|
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: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 100 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPH 179
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 180 NEIAAQICRQAglvkrleKSDnllehqeddnfAIVFAAMGVN-METAQFFKRDFEENGsMERVTLFLNLANDPTIERIIT 258
Cdd:cd01136 81 STLLGMIARNT-------DAD-----------VNVIALIGERgREVREFIEKDLGEEG-LKRSVLVVATSDESPLLRVRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 259 PRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRieGRKGSITQIPIL 338
Cdd:cd01136 142 AYTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 334187279 339 TMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRL 385
Cdd:cd01136 219 LVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
29-411 |
2.07e-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: 2.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 29 TVSGVAGPLVileKVKGPKYQ--EIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGI--DNKyttVQFTGEVLKTPVS 104
Cdd:COG1157 22 RVTRVVGLLI---EAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGIspGAR---VVPTGRPLSVPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 105 LDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAG------Lp 178
Cdd:COG1157 96 DGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 179 hneiaAQICRQAglvkrleKSDnllehqeddnfAIVFAAMG-----VnmetaqffkRDFEEN--GS--MER-----VTlf 244
Cdd:COG1157 175 -----GMIARNT-------EAD-----------VNVIALIGergreV---------REFIEDdlGEegLARsvvvvAT-- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 245 lnlANDPTIERIITPRIALTTAEYLAyECGKHVLVIltdMSS---YADALREVSAAREEVPGRRGYPGYMYTDLATIYER 321
Cdd:COG1157 221 ---SDEPPLMRLRAAYTATAIAEYFR-DQGKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLER 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 322 AGRieGRKGSITQI-PILTmPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHS 400
Cdd:COG1157 294 AGN--GGKGSITAFyTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSP-----EHR 365
|
410
....*....|....
gi 334187279 401 DVSN---QLYANYA 411
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 ... |
26-97 |
4.44e-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: 4.44e-41
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187279 26 EYRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGE 97
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
90-389 |
2.31e-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: 151.77 E-value: 2.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 90 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISgsSINPS--ERTYPEEMIQTGISTIDVMNSIARGQ 167
Cdd:TIGR00962 85 STVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVE--KIAPGviERKSVHEPLQTGIKAIDAMIPIGRGQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 168 KIPLFSAaglphneiaaqicRQAGlvKRLEKSDNLLeHQEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNL 247
Cdd:TIGR00962 163 RELIIGD-------------RQTG--KTAVAIDTII-NQKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAAT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 248 ANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGR 324
Cdd:TIGR00962 227 ASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAK 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334187279 325 I--EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSA 389
Cdd:TIGR00962 303 LndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
90-386 |
1.60e-38 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 145.67 E-value: 1.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 90 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKI 169
Cdd:PRK06936 86 TEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 170 PLFSAAGLPHNEIAAQICRQAglvkrleksdnllehqedDNFAIVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLA 248
Cdd:PRK06936 166 GIFAAAGGGKSTLLASLIRSA------------------EVDVTVLALIGErGREVREFIESDLGEEG-LRKAVLVVATS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 249 NDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGriEGR 328
Cdd:PRK06936 227 DRPSMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSD 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 334187279 329 KGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 386
Cdd:PRK06936 304 KGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVM 361
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
63-468 |
2.88e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 139.56 E-value: 2.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 63 RGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPiLPEAYLDISGSSINPSE 142
Cdd:PRK06820 62 LAEVVSIEQEMALLSPFASSDGLRCG-QWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 143 RTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICrqaglvkrleksdnllEHQEDDnfAIVFAAMGvnm 222
Cdd:PRK06820 140 RQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLC----------------ADSAAD--VMVLALIG--- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 223 ETAQFFKRDFEENGSME---RVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAARE 299
Cdd:PRK06820 199 ERGREVREFLEQVLTPEaraRTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 300 EVPGRRGYPGYMYTDLATIYERAGRIEgrKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVL 379
Cdd:PRK06820 278 EPPAAGSFPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIA 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 380 PSLSRLMKSAIGEGmtRRDHSDVSNQLYANYaigKDVQAMKAVvgEEALSSEDLLYLEFLDKFE--RKFVAQGAYDTRNI 457
Cdd:PRK06820 356 ASVSRIMPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHL 428
|
410
....*....|.
gi 334187279 458 FQSLDLAWTLL 468
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 ... |
98-384 |
1.59e-34 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 130.76 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 98 VLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAY--LDISGSSINPSERTYpeEMIQTGISTIDVMNSIARGQKiplfsaa 175
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERrrVESKAPGIIPRQSVN--EPLQTGIKAIDSLIPIGRGQR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 176 glphnEIaaqIC--RQAGlvkrleKS----DNLLeHQEDDNFAIVFAAMGVNMET-AQFFKRdFEENGSMERVTLFLNLA 248
Cdd:cd01132 72 -----EL---IIgdRQTG------KTaiaiDTII-NQKGKKVYCIYVAIGQKRSTvAQIVKT-LEEHGAMEYTIVVAATA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 249 NDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRI 325
Cdd:cd01132 136 SDPAPLQYLAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKL 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187279 326 --EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 384
Cdd:cd01132 212 sdELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
92-449 |
7.44e-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: 7.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 92 VQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPL 171
Cdd:TIGR01039 69 VIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 172 FSAAGLPHNEIAAQicrqagLVKRLEKsdnllEHqeddNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDP 251
Cdd:TIGR01039 149 FGGAGVGKTVLIQE------LINNIAK-----EH----GGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 252 TIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIegRKGS 331
Cdd:TIGR01039 214 PGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITST--KTGS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 332 ITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrrDHSDVSNQLYANY 410
Cdd:TIGR01039 292 ITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQIL 366
|
330 340 350
....*....|....*....|....*....|....*....
gi 334187279 411 AIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQ 449
Cdd:TIGR01039 367 QRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
46-392 |
1.12e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 129.03 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 46 PKYQEIVNIRLGD-GTTRRGQVLEVDGEKAVVQVFEGTSG--IDNKyttVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNG 122
Cdd:PRK08472 37 PSVGDIVKIESSDnGKECLGMVVVIEKEQFGISPFSFIEGfkIGDK---VFISKEGLNIPVGRNLLGRVVDPLGRPIDGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 123 PPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQA-GLVKrleksdn 201
Cdd:PRK08472 114 GAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGClAPIK------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 202 llehqeddnfaiVFAAMGVN-METAQFFKRDFeeNGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVI 280
Cdd:PRK08472 187 ------------VVALIGERgREIPEFIEKNL--GGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK-NQGLDVLFI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 281 LTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDITHPTPDLTGYITEGQ 360
Cdd:PRK08472 252 MDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEG-KGSITAFFTVLVEGDDMSDPIADQSRSILDGH 330
|
330 340 350
....*....|....*....|....*....|..
gi 334187279 361 IYIDRQLHNRQIYPPINVLPSLSRLMKSAIGE 392
Cdd:PRK08472 331 IVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
1-384 |
4.63e-32 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 128.49 E-value: 4.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 1 MERIKSKMGAAENNLEMEgtlEIGmeyrTVSGVAGPLVILEKVKGPKYQEIVniRLGDGttRRGQVLEVDGEKAVVQVFE 80
Cdd:PRK13343 9 LARIRQRIARYEPQPDAR---EIG----RVESVGDGIAFVSGLPDAALDELL--RFEGG--SRGFAFNLEEELVGAVLLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 81 GTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVM 160
Cdd:PRK13343 78 DTADI-LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 161 NSIARGQKIPLFSAAGLPHNEIAAqicrqaglvkrleksDNLLeHQEDDNFAIVFAAMGVNMETAQFFKRDFEENGSMER 240
Cdd:PRK13343 157 IPIGRGQRELIIGDRQTGKTAIAI---------------DAII-NQKDSDVICVYVAIGQKASAVARVIETLREHGALEY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 241 VTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYE 320
Cdd:PRK13343 221 TTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLE 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334187279 321 RAGRIEGRK--GSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 384
Cdd:PRK13343 300 RAAKLSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
65-419 |
4.92e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 124.68 E-value: 4.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 65 QVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPpiLPEA-YLDISGSSINPSER 143
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGLHCG-QQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRE--LPDVcWKDYDAMPPPAMVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 144 TYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAGLvkrleksdnllehqeDDNFAIVFAAMGvnME 223
Cdd:PRK07594 133 QPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDA---------------DSNVLVLIGERG--RE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 224 TAQFFKRDFEENgSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPG 303
Cdd:PRK07594 196 VREFIDFTLSEE-TRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 304 RRGYPGYMYTDLATIYERAGRieGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLS 383
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
330 340 350
....*....|....*....|....*....|....*.
gi 334187279 384 RLMKSAIGEgmtrrDHSDVSNQLYANYAIGKDVQAM 419
Cdd:PRK07594 352 RVFPVVTSH-----EHRQLAAILRRCLALYQEVELL 382
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
27-415 |
6.05e-31 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 124.45 E-value: 6.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 27 YRTVSGVAGpLVIleKVKGPKYQ--EIVNIRLGDGTTR--RGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTP 102
Cdd:PRK07721 19 YGKVSRVIG-LMI--ESKGPESSigDVCYIHTKGGGDKaiKAEVVGFKDEHVLLMPYTEVAEIAPG-CLVEATGKPLEVK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 103 VSLDMLGRIFNGSGKPIDNGPpiLPEAYLDIS--GSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHN 180
Cdd:PRK07721 95 VGSGLIGQVLDALGEPLDGSA--LPKGLAPVStdQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 181 EIAAQICRQAglvkrleksdnllehQEDDNfaiVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITP 259
Cdd:PRK07721 173 TLMGMIARNT---------------SADLN---VIALIGErGREVREFIERDLGPEG-LKRSIVVVATSDQPALMRIKGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 260 RIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEgrKGSITQIPILT 339
Cdd:PRK07721 234 YTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSITAFYTVL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187279 340 MPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHSDVSN---QLYANYAIGKD 415
Cdd:PRK07721 311 VDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQNSED 384
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
102-423 |
1.08e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 123.69 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 102 PVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNE 181
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 182 IAaqicrqaGLVKRLEKSDnllehqeddnfAIVFAAMGVN-METAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPR 260
Cdd:PRK05688 184 LL-------GMMTRFTEAD-----------IIVVGLIGERgREVKEFIEHILGEEG-LKRSVVVASPADDAPLMRLRAAM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 261 IALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTM 340
Cdd:PRK05688 245 YCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 341 PNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRdhSDVSNQLYANYAIGKDVQAMK 420
Cdd:PRK05688 324 EGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRR--AQRFKQLWSRYQQSRDLISVG 401
|
...
gi 334187279 421 AVV 423
Cdd:PRK05688 402 AYV 404
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
30-406 |
1.72e-30 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 122.95 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 30 VSGVAGPLVileKVKG--PKYQEIVNIRLGDGT-TRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLD 106
Cdd:PRK09099 28 VVEVIGTLL---RVSGldVTLGELCELRQRDGTlLQRAEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 107 MLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQI 186
Cdd:PRK09099 104 LLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 187 CRQAglvkrleksdnllehQEDDNFAIVFAAMGvnMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTTA 266
Cdd:PRK09099 184 ARGT---------------QCDVNVIALIGERG--REVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAIA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 267 EYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRieGRKGSITQIPILTMPNDDIT 346
Cdd:PRK09099 246 EYFR-DRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGS 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 347 HPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSaigegMTRRDHSDVSNQL 406
Cdd:PRK09099 323 DPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQ-----VVPREHVQAAGRL 377
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
65-415 |
2.80e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 119.70 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 65 QVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERT 144
Cdd:PRK06793 56 EVIAIEKENNMLLPFEQTEKVCYG-DSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFERE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 145 YPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvkrleksdnllehQEDDNFAIVFAAMGvnMET 224
Cdd:PRK06793 135 EITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNA---------------KADINVISLVGERG--REV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 225 AQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPgR 304
Cdd:PRK06793 198 KDFIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELP-I 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 305 RGYPGYMYTDLATIYERAGRIEgrKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 384
Cdd:PRK06793 275 GGKTLLMESYMKKLLERSGKTQ--KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSR 352
|
330 340 350
....*....|....*....|....*....|.
gi 334187279 385 LMKSAIGEgmtrrDHSDVSNQLYANYAIGKD 415
Cdd:PRK06793 353 IMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
54-389 |
9.32e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 118.18 E-value: 9.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 54 IRLGD-------GTTRRGQVLEVDGEKAVVQVFEgtSGIDNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDnGPPIL 126
Cdd:PRK06002 47 VRLGDfvairadGGTHLGEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPID-GLGPL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 127 PEAYLDISGSSINPS--ERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAGLVKrleksdnlle 204
Cdd:PRK06002 124 APGTRPMSIDATAPPamTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDT---------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 205 hqeddnfaIVFAAMG-----VnmetaqffkRDFEEN---GSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKH 276
Cdd:PRK06002 194 --------VVIALVGergreV---------REFLEDtlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFR-DRGEN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 277 VLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDITHPTPDLTGYI 356
Cdd:PRK06002 256 VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGT 335
|
330 340 350
....*....|....*....|....*....|...
gi 334187279 357 TEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSA 389
Cdd:PRK06002 336 LDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
64-389 |
3.84e-28 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 116.99 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 64 GQVLEVDGekavVQVFEGTSgidnkyttVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSER 143
Cdd:CHL00059 51 GVVLMGDG----LMIQEGSS--------VKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 144 TYPEEMIQTGISTIDVMNSIARGQKiplfsaaglphnEIaaqIC--RQAGlvKRLEKSDNLLeHQEDDNFAIVFAAMGVN 221
Cdd:CHL00059 119 RSVYEPLQTGLIAIDSMIPIGRGQR------------EL---IIgdRQTG--KTAVATDTIL-NQKGQNVICVYVAIGQK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 222 METAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEV 301
Cdd:CHL00059 181 ASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 302 PGRRGYPG---YMYTDLatiYERAGRIEGR--KGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPI 376
Cdd:CHL00059 260 PGREAYPGdvfYLHSRL---LERAAKLSSQlgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAI 336
|
330
....*....|...
gi 334187279 377 NVLPSLSRLMKSA 389
Cdd:CHL00059 337 NVGISVSRVGSAA 349
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
50-385 |
8.41e-28 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 115.09 E-value: 8.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 50 EIVNIRLG---DGTTRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGK---PIDNGP 123
Cdd:PRK08149 29 EICEIRAGwhsNEVIARAQVVGFQRERTILSLIGNAQGL-SRQVVLKPTGKPLSVWVGEALLGAVLDPTGKiveRFDAPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 124 PILPEA-YLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGlphneiaaqiCRQAGLVKRLeksdnl 202
Cdd:PRK08149 108 TVGPISeERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAG----------CGKTSLMNML------ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 203 LEHQEDDNFAIvfAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILT 282
Cdd:PRK08149 172 IEHSEADVFVI--GLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFR-DQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 283 DMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIegRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIY 362
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIY 326
|
330 340
....*....|....*....|...
gi 334187279 363 IDRQLHNRQIYPPINVLPSLSRL 385
Cdd:PRK08149 327 LSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
102-421 |
2.50e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 114.03 E-value: 2.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 102 PVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNE 181
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 182 IAaqicrqaGLVKRLEKSDnllehqeddnfAIVFAAMGV-NMETAQFFKRDFEENGSMERVTLFLNLANDPTIeRIITPR 260
Cdd:PRK08972 178 LL-------GMMTRGTTAD-----------VIVVGLVGErGREVKEFIEEILGEEGRARSVVVAAPADTSPLM-RLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 261 IALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTM 340
Cdd:PRK08972 239 TATTIAEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 341 PNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHSDVS---NQLYANYAIGKDVQ 417
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQVYSLYQQNRDLI 392
|
....
gi 334187279 418 AMKA 421
Cdd:PRK08972 393 SIGA 396
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
102-434 |
1.07e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 112.18 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 102 PVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNE 181
Cdd:PRK07960 111 PLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 182 IAaqicrqaGLVKRLEKSDnllehqeddnfAIVFAAMGvnmETAQFFKrDFEEN----GSMERVTLFLNLANDPTIERII 257
Cdd:PRK07960 191 LL-------GMMARYTQAD-----------VIVVGLIG---ERGREVK-DFIENilgaEGRARSVVIAAPADVSPLLRMQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 258 TPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPI 337
Cdd:PRK07960 249 GAAYATRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 338 LTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHSdvSNQLYANYAIGKDVQ 417
Cdd:PRK07960 328 VLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYARVRQ--FKQLLSSFQRNRDLV 405
|
330
....*....|....*..
gi 334187279 418 AmkavVGEEALSSEDLL 434
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 ... |
100-386 |
1.20e-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: 106.15 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 100 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAG--- 176
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGvgk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 177 ------LPHNeIAAqicRQAGLVkrleksdnllehqeddnfaiVFAAMGVNMETAQFFKRDFEENG-----SMERVTLFL 245
Cdd:cd01133 81 tvlimeLINN-IAK---AHGGYS--------------------VFAGVGERTREGNDLYHEMKESGvinldGLSKVALVY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 246 NLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRI 325
Cdd:cd01133 137 GQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187279 326 egRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 386
Cdd:cd01133 217 --KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
108-451 |
1.61e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 105.74 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 108 LGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQIC 187
Cdd:PRK07196 97 LGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMIT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 188 RqaglvkrleksdnlleHQEDDnfAIVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTTA 266
Cdd:PRK07196 177 R----------------YTQAD--VVVVGLIGErGREVKEFIEHSLQAAG-MAKSVVVAAPADESPLMRIKATELCHAIA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 267 EYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDIT 346
Cdd:PRK07196 238 TYYR-DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQ 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 347 HPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHSDVSNQL---YANYAIGKDVQAMKAVV 423
Cdd:PRK07196 316 DPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGS-----QQAKAASLLkqcYADYMAIKPLIPLGGYV 390
|
330 340
....*....|....*....|....*....
gi 334187279 424 -GEEALSSEDLLYLEFLDKFERKFVAQGA 451
Cdd:PRK07196 391 aGADPMADQAVHYYPAITQFLRQEVGHPA 419
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
91-384 |
2.51e-24 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 105.92 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 91 TVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDIsgssinpsERTYP--------EEMIQTGISTIDVMNS 162
Cdd:PRK09281 87 TVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPV--------ERKAPgvidrksvHEPLQTGIKAIDAMIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 163 IARGQKiplfsaaglphnEIaaqIC--RQAGlvkrleKS----DNLLeHQEDDNFAIVFAAMGVNMET-AQFfKRDFEEN 235
Cdd:PRK09281 159 IGRGQR------------EL---IIgdRQTG------KTaiaiDTII-NQKGKDVICIYVAIGQKASTvAQV-VRKLEEH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 236 GSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMY 312
Cdd:PRK09281 216 GAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDN-GKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLH 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 313 TDLatiYERAGRI--EGRKGSITQIPIL-TMPNDdithptpdLTGY-------ITEGQIYIDRQLHNRQIYPPINVLPSL 382
Cdd:PRK09281 295 SRL---LERAAKLsdELGGGSLTALPIIeTQAGD--------VSAYiptnvisITDGQIFLESDLFNAGIRPAINVGISV 363
|
..
gi 334187279 383 SR 384
Cdd:PRK09281 364 SR 365
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
91-384 |
5.23e-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: 5.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 91 TVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDIsgssinpsERTYP--------EEMIQTGISTIDVMNS 162
Cdd:COG0056 87 TVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPV--------ERPAPgvidrqpvHEPLQTGIKAIDAMIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 163 IARGQKiplfsaaglphnEIaaqIC--RQAGlvkrleKS----DNLLeHQEDDNFAIVFAAMGVNMETAQFFKRDFEENG 236
Cdd:COG0056 159 IGRGQR------------EL---IIgdRQTG------KTaiaiDTII-NQKGKDVICIYVAIGQKASTVAQVVETLEEHG 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 237 SMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMYT 313
Cdd:COG0056 217 AMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 314 DLatiYERAGRI--EGRKGSITQIPIL-TMPNddithptpDLTGY-------ITEGQIYIDRQLHNRQIYPPINVLPSLS 383
Cdd:COG0056 296 RL---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLSVS 364
|
.
gi 334187279 384 R 384
Cdd:COG0056 365 R 365
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
102-384 |
2.76e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 101.90 E-value: 2.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 102 PVSLDMLGRIFNGSGKPIDNGPPiLPEAYLD-ISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHN 180
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQ-LPKTHLKpLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 181 EIAAQICRQAglvkrleksdnllehQEDDNfaiVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPR 260
Cdd:PRK05922 172 SLLSTIAKGS---------------KSTIN---VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 261 IALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEgrKGSITQI-PILT 339
Cdd:PRK05922 234 AAMTIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILH 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 334187279 340 MPNdditHPT--PDLTGYITEGQIYIDRQlHNRQIYPPINVLPSLSR 384
Cdd:PRK05922 311 YPN----HPDifTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
19-386 |
1.44e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 96.97 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 19 GTLEIGMEYRTVSGVAGPLVileKVKGPKYQEIVNIRL----GDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVqF 94
Cdd:PRK08927 10 GDIDTLVIYGRVVAVRGLLV---EVAGPIHALSVGARIvvetRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAV-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 95 TGEVLKTPVSLDMLGRIFNGSGKPIDNGPPiLPEayldisGSSINPSERTYPE--------EMIQTGISTIDVMNSIARG 166
Cdd:PRK08927 86 ANAAAAVRPSRAWLGRVVNALGEPIDGKGP-LPQ------GPVPYPLRAPPPPahsrarvgEPLDLGVRALNTFLTCCRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 167 QKIPLFSAAGLPHNEIAAQICRQAglvkrleksdnllehqedDNFAIVFAAMGVN-METAQFFKRDFEENGsMERVTLFL 245
Cdd:PRK08927 159 QRMGIFAGSGVGKSVLLSMLARNA------------------DADVSVIGLIGERgREVQEFLQDDLGPEG-LARSVVVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 246 NLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRI 325
Cdd:PRK08927 220 ATSDEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPG 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187279 326 EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 386
Cdd:PRK08927 299 PIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
90-432 |
2.23e-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: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 90 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKI 169
Cdd:COG0055 70 MEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 170 PLFSAAG---------LPHNeIAAQicrQAGLVkrleksdnllehqeddnfaiVFAamGVNMET--AQFFKRDFEENGSM 238
Cdd:COG0055 150 GLFGGAGvgktvlimeLIHN-IAKE---HGGVS--------------------VFA--GVGERTreGNDLYREMKESGVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 239 ERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATI 318
Cdd:COG0055 204 DKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGAL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 319 YEragRI-EGRKGSITQIPILTMPNDDITHPTP-------DLTgyitegqIYIDRQLHNRQIYPPINVLPSLSRLMKSAI 390
Cdd:COG0055 284 QE---RItSTKKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLI 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 334187279 391 -GEgmtrrDHSDVSN---QLYANYaigKDVQAMKAVVGEEALSSED 432
Cdd:COG0055 354 vGE-----EHYRVARevqRILQRY---KELQDIIAILGMDELSEED 391
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
29-394 |
6.20e-20 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 92.80 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 29 TVSGVAGPLVILEKVKGPKYQEIVNIRLGDGTTRRGQV--LEVDGEKAVV---QVFEGTSGidnkyTTVQFTGEVLKTPV 103
Cdd:PTZ00185 45 SIDGTIATLIPAPGNPGVAYNTIIMIQVSPTTFAAGLVfnLEKDGRIGIIlmdNITEVQSG-----QKVMATGKLLYIPV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 104 SLDMLGRIFNGSGKPIDNGPPILPEAYLD-------ISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAG 176
Cdd:PTZ00185 120 GAGVLGKVVNPLGHEVPVGLLTRSRALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 177 LPHNEIAAqicrqAGLVKRLEKSDNLLEHqedDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERI 256
Cdd:PTZ00185 200 TGKTSIAV-----STIINQVRINQQILSK---NAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 257 ITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRK--GSITQ 334
Cdd:PTZ00185 272 LAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKggGSVTA 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 335 IPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 394
Cdd:PTZ00185 351 LPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
29-453 |
7.30e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 92.54 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 29 TVSGVAGPLVILEKVKGPKYQEIV---NIRLgdgttrRGQVLEVDGEKAVVQVFEGTSGI---DnkytTVQFTGEvlktP 102
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVrvgEEGL------IGEIIRIEGDKATIQVYEETSGIkpgE----PVEFTGE----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 103 VSLD----MLGRIFNG-----------SGKPIDNG---PPI--------------------------LPEAYL------- 131
Cdd:PRK04192 72 LSVElgpgLLGSIFDGiqrpldelaekSGDFLERGvyvPALdrekkweftptvkvgdkveagdilgtVQETPSiehkimv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 132 --DISG--SSINPS-------------------------------------ERTYPEEMIQTGISTIDVMNSIARGQK-- 168
Cdd:PRK04192 152 ppGVSGtvKEIVSEgdytvddtiavlededgegveltmmqkwpvrrprpykEKLPPVEPLITGQRVIDTFFPVAKGGTaa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 169 IPLFSAAG---LPHneiaaQICRQAglvkrleksdnllehqedDNFAIVFAAMG--VNmETAQFFkRDFEE-------NG 236
Cdd:PRK04192 232 IPGPFGSGktvTQH-----QLAKWA------------------DADIVIYVGCGerGN-EMTEVL-EEFPElidpktgRP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 237 SMERVTLFLNLANDPTIER---IITpriALTTAEYlaY-ECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMY 312
Cdd:PRK04192 287 LMERTVLIANTSNMPVAAReasIYT---GITIAEY--YrDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 313 TDLATIYERAGRIE---GRKGSITQIPILTMPNDDITHPtpdltgyITEGQIYI-------DRQLHNRQIYPPINVLPSL 382
Cdd:PRK04192 362 SRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEP-------VTQNTLRIvkvfwalDAELADRRHFPAINWLTSY 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334187279 383 SrLMKSAIGEGMTRRDHSDVSNqlYANYAI-----GKDVQAMKAVVGEEALSSEDLLYLE---FLDKFerkFVAQGAYD 453
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 ... |
238-384 |
7.81e-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: 7.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 238 MERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLAT 317
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334187279 318 IYERAGRIE-----GRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 384
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
238-471 |
2.32e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 91.62 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 238 MERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLAT 317
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 318 IYERAGRI-----EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSrLMKSAIGE 392
Cdd:PRK14698 796 FYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYS-LYVDAVKD 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 393 GMTR------RDHSDVSNQLYANYAigkDVQAMKAVVGEEALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWT 466
Cdd:PRK14698 875 WWHKnvdpewKAMRDKAMELLQKEA---ELQEIVRIVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQVT 951
|
....*
gi 334187279 467 LLRIF 471
Cdd:PRK14698 952 MMRVL 956
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
85-410 |
1.91e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 88.11 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 85 IDNKYTTVQFTGEVLKTP------VSLDMLGRIFNGSGKPIdngPPI----LPEAYLDISGSSINPS----ERTYPEEMI 150
Cdd:PRK07165 51 INNEKGKIKINDELIELNntnkvkTSKEYFGKIIDIDGNII---YPEaqnpLSKKFLPNTSSIFNLAhglmTVKTLNEQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 151 QTGISTIDVMNSIARGQKiplfsaaglphnEIaaqIC--RQAGlvkrleKSD---NLLEHQEDDNFAIVFAAMGVNMETA 225
Cdd:PRK07165 128 YTGIIAIDLLIPIGKGQR------------EL---IIgdRQTG------KTHialNTIINQKNTNVKCIYVAIGQKRENL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 226 QFFKRDFEENGSMERvTLFLNLANDPTIERIITPRIALTTAEYLAYEcgKHVLVILTDMSSYADALREVSAAREEVPGRR 305
Cdd:PRK07165 187 SRIYETLKEHDALKN-TIIIDAPSTSPYEQYLAPYVAMAHAENISYN--DDVLIVFDDLTKHANIYREIALLTNKPVGKE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 306 GYPGYMYTDLATIYERAGRIEGRKgSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRl 385
Cdd:PRK07165 264 AFPGDMFFAHSKLLERAGKFKNRK-TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR- 341
|
330 340
....*....|....*....|....*...
gi 334187279 386 mksaIGEGMTRRDHSDVS---NQLYANY 410
Cdd:PRK07165 342 ----TGSSVQSKTITKVAgeiSKIYRAY 365
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
95-449 |
2.34e-18 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 87.79 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 95 TGEVLKTPVSLDMLGRIFNGSGKPIDN-GPpilpeayldISGSSINPSERTYPE--------EMIQTGISTIDVMNSIAR 165
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGP---------VDTRTTSPIHRSAPAfiqldtklSIFETGIKVVDLLAPYRR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 166 GQKIPLFSAAGLPHN----EIAAQICRQAGLVKrleksdnllehqeddnfaiVFAAMG--------VNMETAQFFKRDfE 233
Cdd:CHL00060 161 GGKIGLFGGAGVGKTvlimELINNIAKAHGGVS-------------------VFGGVGertregndLYMEMKESGVIN-E 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 234 ENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYT 313
Cdd:CHL00060 221 QNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLST 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 314 DLATIYERAGRIegRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAI-GE 392
Cdd:CHL00060 301 EMGSLQERITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIvGE 378
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 334187279 393 gmtrrDHSDVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQ 449
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 ... |
30-96 |
7.06e-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: 63.72 E-value: 7.06e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 30 VSGVAGPLVILEKVKGPKYQEIVNIRLG---DGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTG 96
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, ... |
27-97 |
5.93e-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: 5.93e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334187279 27 YRTVSGVAGPLVILEKVKGPKYQEIVNIRLGDG---TTRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGE 97
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, ... |
399-469 |
1.16e-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: 1.16e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334187279 399 HSDVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQGAYDTRNIFQSLDLAWTLLR 469
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
33-120 |
2.36e-06 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 50.41 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334187279 33 VAGPLVILEKVKGPKYQEIVniRLGDgTTRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIF 112
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVV--RVGE-LGLIGEIIRLEGDKAVIQVYEETAGL-KPGEPVEGTGSSLSVELGPGLLTSIY 85
|
....*...
gi 334187279 113 NGSGKPID 120
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 ... |
29-85 |
4.57e-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: 4.57e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 334187279 29 TVSGVAGPLVILEKVKGPKYQEIVniRLGDgttRR--GQVLEVDGEKAVVQVFEGTSGI 85
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELV--RVGE---EGliGEIIRLEGDKATIQVYEETSGL 56
|
|
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