|
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 ... |
20-487 |
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: 976.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 20 EYRTVSGVAGPLVILDKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 99
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 100 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 179
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 180 ICRQAGLVKRLEKTeslLGDVEEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 259
Cdd:TIGR01040 161 ICRQAGLVKLPTKD---VHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 260 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 339
Cdd:TIGR01040 238 AEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 340 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHADVSNQLYANYAIGKDVQAMKAVVGE 419
Cdd:TIGR01040 318 THPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526887681 420 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQYYSRDAA 487
Cdd:TIGR01040 398 EALSSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
20-487 |
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: 853.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 20 EYRTVSGVAGPLVILDKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 99
Cdd:COG1156 5 EYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLELPVSE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 100 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 179
Cdd:COG1156 85 DMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 180 ICRQAglvkrlekteSLLGdvEEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 259
Cdd:COG1156 165 IARQA----------KVRG--EEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 260 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 339
Cdd:COG1156 233 AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 340 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHADVSNQLYANYAIGKDVQAMKAVVGE 419
Cdd:COG1156 313 THPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGE 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526887681 420 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQYYSRDAA 487
Cdd:COG1156 393 EALSETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRA 460
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
20-482 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 831.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 20 EYRTVSGVAGPLVILDKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 99
Cdd:PRK04196 3 EYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPVSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 100 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 179
Cdd:PRK04196 83 DMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 180 ICRQAglvkrlekteSLLGdvEEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 259
Cdd:PRK04196 163 IARQA----------KVLG--EEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 260 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 339
Cdd:PRK04196 231 AEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 340 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHADVSNQLYANYAIGKDVQAMKAVVGE 419
Cdd:PRK04196 311 THPIPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGE 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526887681 420 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQYY 482
Cdd:PRK04196 391 EALSERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYH 453
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
20-487 |
0e+00 |
|
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity with eukaryotic and prokaryotic V-type (H+)-ATPases. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 200071 [Multi-domain] Cd Length: 458 Bit Score: 714.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 20 EYRTVSGVAGPLVILDKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGEVLKTPVSL 99
Cdd:TIGR01041 1 EYSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 100 DMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ 179
Cdd:TIGR01041 81 DMLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 180 ICRQAglvkrlekteSLLGdvEEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTT 259
Cdd:TIGR01041 161 IARQA----------TVRG--EESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 260 AEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDI 339
Cdd:TIGR01041 229 AEYLAFEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 340 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRDHADVSNQLYANYAIGKDVQAMKAVVGE 419
Cdd:TIGR01041 309 THPIPDLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526887681 420 EALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFPRELLHRIPAKTLDQYYSRDAA 487
Cdd:TIGR01041 389 EALSERDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYHPKYRK 456
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
92-385 |
0e+00 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 614.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 92 VLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGL 171
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 172 PHNEIAAQICRQAGLVKrlektesllgdvEEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERII 251
Cdd:cd01135 81 PHNELAAQIARQAGVVG------------SEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 252 TPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPI 331
Cdd:cd01135 149 TPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPI 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2526887681 332 LTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIG 385
Cdd:cd01135 229 LTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
21-484 |
2.69e-127 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 377.07 E-value: 2.69e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 21 YRTVSGVAGPLVILdKVKGPKYQEIVNIRLGDGTtRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLD 100
Cdd:PRK02118 5 YTKITDITGNVITV-EAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGISTG-DEVVFLGRPMQVTYSES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 101 MLGRIFNGSGKPIDNGPPILPEAyLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQI 180
Cdd:PRK02118 82 LLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 181 CRQAglvkrlektesllgdvEEDnfAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTA 260
Cdd:PRK02118 161 ALQA----------------EAD--IIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 261 EYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDIT 340
Cdd:PRK02118 223 EKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 341 HPTPDLTGYITEGQIYidrqLHNRQIYPpinvLPSLSRLMKSAIGEgMTRRDHADVSN---QLYANYAIGKDVQAMkavv 417
Cdd:PRK02118 302 HPVPDNTGYITEGQFY----LRRGRIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM---- 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526887681 418 GEEaLSSEDLLYLEFLDKFERKFVAQGAydtrNI--FQSLDLAWTLL-RIF-PRELLhrIPAKTLDQYYSR 484
Cdd:PRK02118 369 GFK-LSNWDEKLLKFSELFESRLMDLEV----NIplEEALDLGWKILaQCFhPEEVG--IKEQLIDKYWPK 432
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
94-379 |
3.02e-108 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 322.48 E-value: 3.02e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 94 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPH 173
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 174 NEIAAQICRQAGlvkrlektesllgdvEEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITP 253
Cdd:cd19476 81 TVLAMQLARNQA---------------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 254 RIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILT 333
Cdd:cd19476 146 YTGLTIAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVS 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2526887681 334 MPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRL 379
Cdd:cd19476 225 TPGDDLTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
147-377 |
4.53e-106 |
|
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: 314.68 E-value: 4.53e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 147 GISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvkrlektesllgdveeDNFAIVFAAMGVNMETAQFFKRDF 226
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQA------------------SADVVVYALIGERGREVREFIEEL 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 227 EENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMY 306
Cdd:pfam00006 63 LGSGALKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVF 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526887681 307 TDLATIYERAGRIEGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLS 377
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 ... |
387-481 |
4.33e-59 |
|
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: 189.57 E-value: 4.33e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 387 GMTRRDHADVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLAWTLLRIFP 466
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 2526887681 467 RELLHRIPAKTLDQY 481
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
94-379 |
7.05e-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: 152.71 E-value: 7.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 94 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPH 173
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 174 NEIAAQICRQAGlvkrlektesllGDVeednfaIVFAAMGVN-METAQFFKRDFEENGsMERVTLFLNLANDPTIERIIT 252
Cdd:cd01136 81 STLLGMIARNTD------------ADV------NVIALIGERgREVREFIEKDLGEEG-LKRSVLVVATSDESPLLRVRA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 253 PRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRieGRKGSITQIPIL 332
Cdd:cd01136 142 AYTATAIAEYFRDQ-GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTV 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2526887681 333 TMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRL 379
Cdd:cd01136 219 LVEGDDFNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
23-405 |
1.37e-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: 153.65 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 23 TVSGVAGPLVildKVKGPKYQ--EIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGI--DNKyttVQFTGEVLKTPVS 98
Cdd:COG1157 22 RVTRVVGLLI---EAVGPDASigELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGIspGAR---VVPTGRPLSVPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 99 LDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLphneiaa 178
Cdd:COG1157 96 DGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGV------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 179 qicrqaGlvkrleKTeSLLG--------DVeednfaIVFAAMG-----VnmetaqffkRDFEEN--GS--MER-----VT 236
Cdd:COG1157 169 ------G------KS-TLLGmiarnteaDV------NVIALIGergreV---------REFIEDdlGEegLARsvvvvAT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 237 lflnlANDPTIERIITPRIALTTAEYLAyECGKHVLVIltdMSS---YADALREVSAAREEVPGRRGYPGYMYTDLATIY 313
Cdd:COG1157 221 -----SDEPPLMRLRAAYTATAIAEYFR-DQGKNVLLL---MDSltrFAMAQREIGLAAGEPPATRGYPPSVFALLPRLL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 314 ERAGRieGRKGSITQI-PILTmPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrD 392
Cdd:COG1157 292 ERAGN--GGKGSITAFyTVLV-EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPDIVSP-----E 363
|
410
....*....|....*.
gi 2526887681 393 HADVSN---QLYANYA 405
Cdd:COG1157 364 HRALARrlrRLLARYE 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 ... |
20-91 |
1.06e-40 |
|
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: 140.26 E-value: 1.06e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526887681 20 EYRTVSGVAGPLVILDKVKGPKYQEIVNIRLGDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVQFTGE 91
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKVRFTGE 72
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
84-380 |
8.42e-39 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 146.44 E-value: 8.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 84 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKI 163
Cdd:PRK06936 86 TEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRM 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 164 PLFSAAGLPHNEIAAQICRQAGLvkrlektesllgDVeednfaIVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLA 242
Cdd:PRK06936 166 GIFAAAGGGKSTLLASLIRSAEV------------DV------TVLALIGErGREVREFIESDLGEEG-LRKAVLVVATS 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 243 NDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGriEGR 322
Cdd:PRK06936 227 DRPSMERAKAGFVATSIAEYFRDQ-GKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSD 303
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2526887681 323 KGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 380
Cdd:PRK06936 304 KGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVM 361
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
84-383 |
1.45e-38 |
|
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: 146.76 E-value: 1.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 84 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISgsSINPS--ERTYPEEMIQTGISTIDVMNSIARGQ 161
Cdd:TIGR00962 85 STVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPVE--KIAPGviERKSVHEPLQTGIKAIDAMIPIGRGQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 162 KIPLFSAaglphneiaaqicRQAGlvkrleKT----ESLLGDVEEDNFAIvFAAMGVNMETAQFFKRDFEENGSMERVTL 237
Cdd:TIGR00962 163 RELIIGD-------------RQTG------KTavaiDTIINQKDSDVYCI-YVAIGQKASTVAQVVRKLEEHGAMAYTIV 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 238 FLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMYTDLatiYE 314
Cdd:TIGR00962 223 VAATASDSASLQYLAPYTGCTMGEYFRDN-GKHALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LE 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526887681 315 RAGRI--EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSA 383
Cdd:TIGR00962 299 RAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGIRPAINVGLSVSRVGGAA 369
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
57-462 |
1.51e-36 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 139.95 E-value: 1.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 57 RGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPiLPEAYLDISGSSINPSE 136
Cdd:PRK06820 62 LAEVVSIEQEMALLSPFASSDGLRCG-QWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGPP-LTGQWRELDCPPPSPLT 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 137 RTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvkrlekteslLGDVeednfaIVFAAMGV-N 215
Cdd:PRK06820 140 RQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCADS------------AADV------MVLALIGErG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 216 METAQFFKRDFEENgSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEV 295
Cdd:PRK06820 202 REVREFLEQVLTPE-ARARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 296 PGRRGYPGYMYTDLATIYERAGRIEgrKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPS 375
Cdd:PRK06820 280 PAAGSFPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAAS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 376 LSRLMKSAIGEGmtRRDHADVSNQLYANYaigKDVQAMKAVvgEEALSSEDLLYLEFLDKFE--RKFVAQGAYDTRNIFQ 453
Cdd:PRK06820 358 VSRIMPQIVSAG--QLAMAQKLRRMLACY---QEIELLVRV--GEYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLET 430
|
....*....
gi 2526887681 454 SLDLAWTLL 462
Cdd:PRK06820 431 TLEHLAQVV 439
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
86-443 |
9.84e-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: 132.54 E-value: 9.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 86 VQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPL 165
Cdd:TIGR01039 69 VIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 166 FSAAGLPHNEIAAQicrqagLVKRLEKTESLLGdveednfaiVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDP 245
Cdd:TIGR01039 149 FGGAGVGKTVLIQE------LINNIAKEHGGYS---------VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 246 TIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIegRKGS 325
Cdd:TIGR01039 214 PGARMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITST--KTGS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 326 ITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMK-SAIGEgmtrrDHADVSNQLYANY 404
Cdd:TIGR01039 292 ITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVGE-----EHYDVARGVQQIL 366
|
330 340 350
....*....|....*....|....*....|....*....
gi 2526887681 405 AIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQ 443
Cdd:TIGR01039 367 QRYKELQDIIAILGMDELSEEDKLTVERARRIQR-FLSQ 404
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
40-386 |
3.73e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 130.58 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 40 PKYQEIVNIRLGD-GTTRRGQVLEVDGEKAVVQVFEGTSG--IDNKyttVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNG 116
Cdd:PRK08472 37 PSVGDIVKIESSDnGKECLGMVVVIEKEQFGISPFSFIEGfkIGDK---VFISKEGLNIPVGRNLLGRVVDPLGRPIDGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 117 PPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvKRLEKTESL 196
Cdd:PRK08472 114 GAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGC---LAPIKVVAL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 197 LGDVeednfaivfaamgvNMETAQFFKRDFeeNGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILT 276
Cdd:PRK08472 191 IGER--------------GREIPEFIEKNL--GGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK-NQGLDVLFIMD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 277 DMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDITHPTPDLTGYITEGQIY 356
Cdd:PRK08472 254 SVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEG-KGSITAFFTVLVEGDDMSDPIADQSRSILDGHIV 332
|
330 340 350
....*....|....*....|....*....|
gi 2526887681 357 IDRQLHNRQIYPPINVLPSLSRLMKSAIGE 386
Cdd:PRK08472 333 LSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
92-378 |
4.07e-33 |
|
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: 126.52 E-value: 4.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 92 VLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAY--LDISGSSINPSERTYpeEMIQTGISTIDVMNSIARGQKiplfsaa 169
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERrrVESKAPGIIPRQSVN--EPLQTGIKAIDSLIPIGRGQR------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 170 glphnEIaaqIC--RQAGlvkrleKTESLLGDV---EEDNFAIVFAAMGVNMET-AQFFKRdFEENGSMERVTLFLNLAN 243
Cdd:cd01132 72 -----EL---IIgdRQTG------KTAIAIDTIinqKGKKVYCIYVAIGQKRSTvAQIVKT-LEEHGAMEYTIVVAATAS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 244 DPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPG---YMYTDLatiYERAGRI- 319
Cdd:cd01132 137 DPAPLQYLAPYAGCAMGEYFRDN-GKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLs 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 320 -EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 378
Cdd:cd01132 213 dELGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
59-411 |
2.61e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 122.37 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 59 QVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPpiLPEA-YLDISGSSINPSER 137
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGLHCG-QQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRE--LPDVcWKDYDAMPPPAMVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 138 TYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAGlvkrlektesllGDVeedNFAIVFAAMGvnME 217
Cdd:PRK07594 133 QPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPD------------ADS---NVLVLIGERG--RE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 218 TAQFFKRDFEENgSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPG 297
Cdd:PRK07594 196 VREFIDFTLSEE-TRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 298 RRGYPGYMYTDLATIYERAGRieGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLS 377
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
330 340 350
....*....|....*....|....*....|....
gi 2526887681 378 RLMKSAIGEgmtrrDHADVSNQLYANYAIGKDVQ 411
Cdd:PRK07594 352 RVFPVVTSH-----EHRQLAAILRRCLALYQEVE 380
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
21-409 |
2.64e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 122.52 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 21 YRTVSGVAGpLVIldKVKGPKYQ--EIVNIRLGDGTTR--RGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTP 96
Cdd:PRK07721 19 YGKVSRVIG-LMI--ESKGPESSigDVCYIHTKGGGDKaiKAEVVGFKDEHVLLMPYTEVAEIAPG-CLVEATGKPLEVK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 97 VSLDMLGRIFNGSGKPIDNGPpiLPEAYLDIS--GSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHN 174
Cdd:PRK07721 95 VGSGLIGQVLDALGEPLDGSA--LPKGLAPVStdQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 175 EIAAQICRQAGlvkrlektesllGDVEednfaiVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITP 253
Cdd:PRK07721 173 TLMGMIARNTS------------ADLN------VIALIGErGREVREFIERDLGPEG-LKRSIVVVATSDQPALMRIKGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 254 RIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEgrKGSITQIPILT 333
Cdd:PRK07721 234 YTATAIAEYFRDQ-GLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSITAFYTVL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526887681 334 MPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHADVSN---QLYANYAIGKD 409
Cdd:PRK07721 311 VDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNHIVSP-----EHKEAANrfrELLSTYQNSED 384
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
96-417 |
2.81e-30 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 122.53 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 96 PVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNE 175
Cdd:PRK05688 104 PMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 176 IAaqicrqaGLVKRLekTESllgDVeednfaIVFAAMGVN-METAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPR 254
Cdd:PRK05688 184 LL-------GMMTRF--TEA---DI------IVVGLIGERgREVKEFIEHILGEEG-LKRSVVVASPADDAPLMRLRAAM 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 255 IALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTM 334
Cdd:PRK05688 245 YCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVLS 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 335 PNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRdhADVSNQLYANYAIGKDVQAMK 414
Cdd:PRK05688 324 EGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRR--AQRFKQLWSRYQQSRDLISVG 401
|
...
gi 2526887681 415 AVV 417
Cdd:PRK05688 402 AYV 404
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
24-400 |
1.04e-29 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 120.64 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 24 VSGVAGPLVildKVKG--PKYQEIVNIRLGDGT-TRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLD 100
Cdd:PRK09099 28 VVEVIGTLL---RVSGldVTLGELCELRQRDGTlLQRAEVVGFSRDVALLSPFGELGGL-SRGTRVIGLGRPLSVPVGPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 101 MLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQI 180
Cdd:PRK09099 104 LLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMF 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 181 CRQAGLvkrlektesllgDVEednfaiVFAAMGV-NMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTT 259
Cdd:PRK09099 184 ARGTQC------------DVN------VIALIGErGREVREFIELILGEDG-MARSVVVCATSDRSSIERAKAAYVATAI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 260 AEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRieGRKGSITQIPILTMPNDDI 339
Cdd:PRK09099 245 AEYFR-DRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESG 321
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526887681 340 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSaigegMTRRDHADVSNQL 400
Cdd:PRK09099 322 SDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQ-----VVPREHVQAAGRL 377
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
56-378 |
1.50e-29 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 121.18 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 56 RRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPS 135
Cdd:PRK13343 59 SRGFAFNLEEELVGAVLLDDTADI-LAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAII 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 136 ERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQ-ICRQAGlvkrlektesllgdveeDNFAIVFAAMGV 214
Cdd:PRK13343 138 ERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDaIINQKD-----------------SDVICVYVAIGQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 215 NMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREE 294
Cdd:PRK13343 201 KASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRDQ-GQDALIVYDDLSKHAAAYRELSLLLRR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 295 VPGRRGYPGYMYTDLATIYERAGRIEGRK--GSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINV 372
Cdd:PRK13343 280 PPGREAYPGDIFYLHSRLLERAAKLSPELggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDV 359
|
....*.
gi 2526887681 373 LPSLSR 378
Cdd:PRK13343 360 GLSVSR 365
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
59-409 |
2.45e-29 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 119.70 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 59 QVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERT 138
Cdd:PRK06793 56 EVIAIEKENNMLLPFEQTEKVCYG-DSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFERE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 139 YPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvKRLEKTESLLGDVeednfaivfaamgvNMET 218
Cdd:PRK06793 135 EITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNA---KADINVISLVGER--------------GREV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 219 AQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPgR 298
Cdd:PRK06793 198 KDFIRKELGEEG-MRKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQ-GNNVLLMMDSVTRFADARRSVDIAVKELP-I 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 299 RGYPGYMYTDLATIYERAGRIEgrKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 378
Cdd:PRK06793 275 GGKTLLMESYMKKLLERSGKTQ--KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSR 352
|
330 340 350
....*....|....*....|....*....|.
gi 2526887681 379 LMKSAIGEgmtrrDHADVSNQLYANYAIGKD 409
Cdd:PRK06793 353 IMEEIVSP-----NHWQLANEMRKILSIYKE 378
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
48-383 |
2.03e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 117.02 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 48 IRLGD-------GTTRRGQVLEVDGEKAVVQVFEgtSGIDNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDnGPPIL 120
Cdd:PRK06002 47 VRLGDfvairadGGTHLGEVVRVDPDGVTVKPFE--PRIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPID-GLGPL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 121 PEAYLDISGSSINPS--ERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAGLVKrlektesllg 198
Cdd:PRK06002 124 APGTRPMSIDATAPPamTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDT---------- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 199 dveednfaIVFAAMG-----VnmetaqffkRDFEEN---GSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKH 270
Cdd:PRK06002 194 --------VVIALVGergreV---------REFLEDtlaDNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFR-DRGEN 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 271 VLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQIPILTMPNDDITHPTPDLTGYI 350
Cdd:PRK06002 256 VLLIVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGT 335
|
330 340 350
....*....|....*....|....*....|...
gi 2526887681 351 TEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSA 383
Cdd:PRK06002 336 LDGHIVLDRAIAEQGRYPAVDPLASISRLARHA 368
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
96-415 |
1.66e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 114.41 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 96 PVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNE 175
Cdd:PRK08972 98 PVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSV 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 176 IAAQICRQA-------GLVKRL-----EKTESLLGDvEEDNFAIVFAAMgvnmetaqffkrdfeengsmervtlflnlAN 243
Cdd:PRK08972 178 LLGMMTRGTtadvivvGLVGERgrevkEFIEEILGE-EGRARSVVVAAP-----------------------------AD 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 244 DPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRK 323
Cdd:PRK08972 228 TSPLMRLKGCETATTIAEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 324 GSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHADVS---NQL 400
Cdd:PRK08972 307 GSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMrrvKQV 381
|
330
....*....|....*
gi 2526887681 401 YANYAIGKDVQAMKA 415
Cdd:PRK08972 382 YSLYQQNRDLISIGA 396
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
58-383 |
8.04e-27 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 113.13 E-value: 8.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 58 GQVLEVDGekavVQVFEGTSgidnkyttVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSER 137
Cdd:CHL00059 51 GVVLMGDG----LMIQEGSS--------VKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 138 TYPEEMIQTGISTIDVMNSIARGQKiplfsaaglphnEIaaqIC--RQAGlvKRLEKTESLLGDVEEdNFAIVFAAMGVN 215
Cdd:CHL00059 119 RSVYEPLQTGLIAIDSMIPIGRGQR------------EL---IIgdRQTG--KTAVATDTILNQKGQ-NVICVYVAIGQK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 216 METAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEV 295
Cdd:CHL00059 181 ASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 296 PGRRGYPG---YMYTDLatiYERAGRIEGR--KGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPI 370
Cdd:CHL00059 260 PGREAYPGdvfYLHSRL---LERAAKLSSQlgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAI 336
|
330
....*....|...
gi 2526887681 371 NVLPSLSRLMKSA 383
Cdd:CHL00059 337 NVGISVSRVGSAA 349
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
96-428 |
5.98e-26 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 110.26 E-value: 5.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 96 PVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNE 175
Cdd:PRK07960 111 PLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 176 IAAQICR--QAglvkrlektesllgDVeednfaIVFAAMGvnmETAQFFKrDFEEN----GSMERVTLFLNLANDPTIER 249
Cdd:PRK07960 191 LLGMMARytQA--------------DV------IVVGLIG---ERGREVK-DFIENilgaEGRARSVVIAAPADVSPLLR 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 250 IITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRKGSITQI 329
Cdd:PRK07960 247 MQGAAYATRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAF 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 330 PILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRRdhADVSNQLYANYAIGKD 409
Cdd:PRK07960 326 YTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR--VRQFKQLLSSFQRNRD 403
|
330
....*....|....*....
gi 2526887681 410 VQAmkavVGEEALSSEDLL 428
Cdd:PRK07960 404 LVS----VGAYAKGSDPML 418
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
44-379 |
6.87e-26 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 109.70 E-value: 6.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 44 EIVNIRLG---DGTTRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDN-GPPI 119
Cdd:PRK08149 29 EICEIRAGwhsNEVIARAQVVGFQRERTILSLIGNAQGL-SRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVERfDAPP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 120 LPEA---YLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQICRQAglvkrlektesl 196
Cdd:PRK08149 108 TVGPiseERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHS------------ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 197 lgdvEEDNFAIvfAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILT 276
Cdd:PRK08149 176 ----EADVFVI--GLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFR-DQGKRVVLFID 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 277 DMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIegRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIY 356
Cdd:PRK08149 249 SMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIY 326
|
330 340
....*....|....*....|...
gi 2526887681 357 IDRQLHNRQIYPPINVLPSLSRL 379
Cdd:PRK08149 327 LSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
94-380 |
1.81e-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: 105.38 E-value: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 94 KTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAG--- 170
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGvgk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 171 ------LPHNeiaaqICRQAGLVKrlektesllgdveednfaiVFAAMGVNMETAQFFKRDFEENG-----SMERVTLFL 239
Cdd:cd01133 81 tvlimeLINN-----IAKAHGGYS-------------------VFAGVGERTREGNDLYHEMKESGvinldGLSKVALVY 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 240 NLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRI 319
Cdd:cd01133 137 GQMNEPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526887681 320 egRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 380
Cdd:cd01133 217 --KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRIL 275
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
102-445 |
1.33e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 105.74 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 102 LGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHNEIAAQIC 181
Cdd:PRK07196 97 LGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMIT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 182 R--QAGLVkrlektesLLGDVEEDnfaivfaamgvNMETAQFFKRDFEENGsMERVTLFLNLANDPTIERIITPRIALTT 259
Cdd:PRK07196 177 RytQADVV--------VVGLIGER-----------GREVKEFIEHSLQAAG-MAKSVVVAAPADESPLMRIKATELCHAI 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 260 AEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGrKGSITQIPILTMPNDDI 339
Cdd:PRK07196 237 ATYYR-DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQ 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 340 THPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEgmtrrDHADVSNQL---YANYAIGKDVQAMKAV 416
Cdd:PRK07196 315 QDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMSQVIGS-----QQAKAASLLkqcYADYMAIKPLIPLGGY 389
|
330 340 350
....*....|....*....|....*....|
gi 2526887681 417 V-GEEALSSEDLLYLEFLDKFERKFVAQGA 445
Cdd:PRK07196 390 VaGADPMADQAVHYYPAITQFLRQEVGHPA 419
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
85-378 |
1.84e-23 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 103.22 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 85 TVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDIsgssinpsERTYP--------EEMIQTGISTIDVMNS 156
Cdd:PRK09281 87 TVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPV--------ERKAPgvidrksvHEPLQTGIKAIDAMIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 157 IARGQKiplfsaaglphnEIaaqIC--RQAGlvkrleKTesllgdveednfAI---------------VFAAMGVNMET- 218
Cdd:PRK09281 159 IGRGQR------------EL---IIgdRQTG------KT------------AIaidtiinqkgkdvicIYVAIGQKASTv 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 219 AQFfKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGR 298
Cdd:PRK09281 206 AQV-VRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFMDN-GKDALIVYDDLSKQAVAYRQLSLLLRRPPGR 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 299 RGYPG---YMYTDLatiYERAGRI--EGRKGSITQIPIL-TMPNDdithptpdLTGY-------ITEGQIYIDRQLHNRQ 365
Cdd:PRK09281 284 EAYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIeTQAGD--------VSAYiptnvisITDGQIFLESDLFNAG 352
|
330
....*....|...
gi 2526887681 366 IYPPINVLPSLSR 378
Cdd:PRK09281 353 IRPAINVGISVSR 365
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
96-378 |
1.93e-23 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 102.29 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 96 PVSLDMLGRIFNGSGKPIDNGPPiLPEAYLD-ISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAGLPHN 174
Cdd:PRK05922 93 HLSDHLLGRVLDGFGNPLDGKEQ-LPKTHLKpLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 175 EIAAQICrqaglvkrlekteslLGDVEEDNfaiVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERIITPR 254
Cdd:PRK05922 172 SLLSTIA---------------KGSKSTIN---VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGR 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 255 IALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEgrKGSITQI-PILT 333
Cdd:PRK05922 234 AAMTIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILH 310
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2526887681 334 MPNdditHPT--PDLTGYITEGQIYIDRQlHNRQIYPPINVLPSLSR 378
Cdd:PRK05922 311 YPN----HPDifTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR 352
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
85-378 |
4.54e-23 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 102.04 E-value: 4.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 85 TVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDIsgssinpsERTYP--------EEMIQTGISTIDVMNS 156
Cdd:COG0056 87 TVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPV--------ERPAPgvidrqpvHEPLQTGIKAIDAMIP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 157 IARGQKiplfsaaglphnEIaaqIC--RQAGlvkrleKTesllgdveednfAI---------------VFAAMGVNMETA 219
Cdd:COG0056 159 IGRGQR------------EL---IIgdRQTG------KT------------AIaidtiinqkgkdvicIYVAIGQKASTV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 220 QFFKRDFEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRR 299
Cdd:COG0056 206 AQVVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYFMDQ-GKDVLIVYDDLSKHAVAYRELSLLLRRPPGRE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 300 GYPG---YMYTDLatiYERAGRI--EGRKGSITQIPIL-TMPNddithptpDLTGY-------ITEGQIYIDRQLHNRQI 366
Cdd:COG0056 285 AYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGI 353
|
330
....*....|..
gi 2526887681 367 YPPINVLPSLSR 378
Cdd:COG0056 354 RPAINVGLSVSR 365
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
84-426 |
1.40e-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: 97.08 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 84 TTVQFTGEVLKTPVSLDMLGRIFNGSGKPIDNGPPILPEAYLDISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKI 163
Cdd:COG0055 70 MEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKI 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 164 PLFSAAG---------LPHNeIAAQicrQAGLVkrlektesllgdveednfaiVFAamGVNMET--AQFFKRDFEENGSM 232
Cdd:COG0055 150 GLFGGAGvgktvlimeLIHN-IAKE---HGGVS--------------------VFA--GVGERTreGNDLYREMKESGVL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 233 ERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATI 312
Cdd:COG0055 204 DKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGAL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 313 YEragRI-EGRKGSITQIPILTMPNDDITHPTP-------DLTgyitegqIYIDRQLHNRQIYPPINVLPSLSRLMKSAI 384
Cdd:COG0055 284 QE---RItSTKKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLI 353
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2526887681 385 -GEgmtrrDHADVSN---QLYANYaigKDVQAMKAVVGEEALSSED 426
Cdd:COG0055 354 vGE-----EHYRVARevqRILQRY---KELQDIIAILGMDELSEED 391
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
13-380 |
3.01e-21 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 95.82 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 13 GTLEIGMEYRTVSGVAGPLVildKVKGPKYQEIVNIRL----GDGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKYTTVqF 88
Cdd:PRK08927 10 GDIDTLVIYGRVVAVRGLLV---EVAGPIHALSVGARIvvetRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAV-I 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 89 TGEVLKTPVSLDMLGRIFNGSGKPIDNGPPiLPEayldisGSSINPSERTYPE--------EMIQTGISTIDVMNSIARG 160
Cdd:PRK08927 86 ANAAAAVRPSRAWLGRVVNALGEPIDGKGP-LPQ------GPVPYPLRAPPPPahsrarvgEPLDLGVRALNTFLTCCRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 161 QKIPLFSAAGLPHNEIAAQICRQAglvkrlektesllgdveeDNFAIVFAAMGV-NMETAQFFKRDFEENGsMERVTLFL 239
Cdd:PRK08927 159 QRMGIFAGSGVGKSVLLSMLARNA------------------DADVSVIGLIGErGREVQEFLQDDLGPEG-LARSVVVV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 240 NLANDPTIERIITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRI 319
Cdd:PRK08927 220 ATSDEPALMRRQAAYLTLAIAEYFRDQ-GKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPG 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526887681 320 EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM 380
Cdd:PRK08927 299 PIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
23-388 |
3.34e-20 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 93.57 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 23 TVSGVAGPLVILDKVKGPKYQEIVNIRLGDGTTRRGQV--LEVDGEKAVV---QVFEGTSGidnkyTTVQFTGEVLKTPV 97
Cdd:PTZ00185 45 SIDGTIATLIPAPGNPGVAYNTIIMIQVSPTTFAAGLVfnLEKDGRIGIIlmdNITEVQSG-----QKVMATGKLLYIPV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 98 SLDMLGRIFNGSGKPIDNGPPILPEAYLD-------ISGSSINPSERTYPEEMIQTGISTIDVMNSIARGQKIPLFSAAG 170
Cdd:PTZ00185 120 GAGVLGKVVNPLGHEVPVGLLTRSRALLEseqtlgkVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQ 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 171 LPHNEIAAqicrqAGLVKRLEKTESLLgdvEEDNFAIVFAAMGVNMETAQFFKRDFEENGSMERVTLFLNLANDPTIERI 250
Cdd:PTZ00185 200 TGKTSIAV-----STIINQVRINQQIL---SKNAVISIYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQY 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 251 ITPRIALTTAEYLAYEcGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRIEGRK--GSITQ 328
Cdd:PTZ00185 272 LAPYSGVTMGEYFMNR-GRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKggGSVTA 350
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 329 IPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAIGEGM 388
Cdd:PTZ00185 351 LPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRVGSSAQNVAM 410
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
23-447 |
6.16e-20 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 92.92 E-value: 6.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 23 TVSGVAGPLVILDKVKGPKYQEIV---NIRLgdgttrRGQVLEVDGEKAVVQVFEGTSGI---DnkytTVQFTGEvlktP 96
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVrvgEEGL------IGEIIRIEGDKATIQVYEETSGIkpgE----PVEFTGE----P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 97 VSLD----MLGRIFNG-----------SGKPIDNG---PPI--------------------------LPEAYL------- 125
Cdd:PRK04192 72 LSVElgpgLLGSIFDGiqrpldelaekSGDFLERGvyvPALdrekkweftptvkvgdkveagdilgtVQETPSiehkimv 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 126 --DISG--SSINPS-------------------------------------ERTYPEEMIQTGISTIDVMNSIARGQK-- 162
Cdd:PRK04192 152 ppGVSGtvKEIVSEgdytvddtiavlededgegveltmmqkwpvrrprpykEKLPPVEPLITGQRVIDTFFPVAKGGTaa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 163 IPLFSAAG---LPHneiaaQICRQAglvkrlektesllgDVEednfAIVFAAMG--VNmETAQFFkRDFEE-------NG 230
Cdd:PRK04192 232 IPGPFGSGktvTQH-----QLAKWA--------------DAD----IVIYVGCGerGN-EMTEVL-EEFPElidpktgRP 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 231 SMERVTLFLNLANDPTIER---IITpriALTTAEYlaY-ECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMY 306
Cdd:PRK04192 287 LMERTVLIANTSNMPVAAReasIYT---GITIAEY--YrDMGYDVLLMADSTSRWAEALREISGRLEEMPGEEGYPAYLA 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 307 TDLATIYERAGRIE---GRKGSITQIPILTMPNDDITHPtpdltgyITEGQIYI-------DRQLHNRQIYPPINVLPSL 376
Cdd:PRK04192 362 SRLAEFYERAGRVKtlgGEEGSVTIIGAVSPPGGDFSEP-------VTQNTLRIvkvfwalDAELADRRHFPAINWLTSY 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526887681 377 SrLMKSAIGEGMTRRDHADVSNqlYANYAI-----GKDVQAMKAVVGEEALSSEDLLYLE---FLDKFerkFVAQGAYD 447
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 ... |
232-378 |
1.03e-19 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 89.17 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 232 MERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLAT 311
Cdd:cd01134 137 MERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARLAE 215
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2526887681 312 IYERAGRIE-----GRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSR 378
Cdd:cd01134 216 FYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
232-465 |
2.49e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 91.62 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 232 MERVTLFLNLANDPTIERIITPRIALTTAEYLAyECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLAT 311
Cdd:PRK14698 717 MERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 312 IYERAGRI-----EGRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLM------ 380
Cdd:PRK14698 796 FYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVdavkdw 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 381 --KSAIGEGMTRRDHADVSNQLYAnyaigkDVQAMKAVVGEEALSSEDLLYLEFLDKFERKFVAQGAYDTRNIFQSLDLA 458
Cdd:PRK14698 876 whKNVDPEWKAMRDKAMELLQKEA------ELQEIVRIVGPDALPERERAILLVARMLREDYLQQDAFDEVDTYCPPEKQ 949
|
....*..
gi 2526887681 459 WTLLRIF 465
Cdd:PRK14698 950 VTMMRVL 956
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
89-443 |
2.85e-18 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 87.40 E-value: 2.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 89 TGEVLKTPVSLDMLGRIFNGSGKPIDN-GPpilpeayldISGSSINPSERTYPE--------EMIQTGISTIDVMNSIAR 159
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNlGP---------VDTRTTSPIHRSAPAfiqldtklSIFETGIKVVDLLAPYRR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 160 GQKIPLFSAAGLPHN----EIAAQICRQAGLVkrlekteSLLGDVEE------DnfaiVFAAM---GV-Nmetaqffkrd 225
Cdd:CHL00060 161 GGKIGLFGGAGVGKTvlimELINNIAKAHGGV-------SVFGGVGErtregnD----LYMEMkesGViN---------- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 226 fEENGSMERVTLFLNLANDPTIERIITPRIALTTAEYLAYECGKHVLVILTDMSSYADALREVSAAREEVPGRRGYPGYM 305
Cdd:CHL00060 220 -EQNIAESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 306 YTDLATIYERAGRIegRKGSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRLMKSAI- 384
Cdd:CHL00060 299 STEMGSLQERITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIv 376
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526887681 385 GEgmtrrDHADVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQ 443
Cdd:CHL00060 377 GE-----EHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIER-FLSQ 429
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
79-404 |
6.43e-18 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 86.18 E-value: 6.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 79 IDNKYTTVQFTGEVLKTP------VSLDMLGRIFNGSGKPIdngPPI----LPEAYLDISGSSINPS----ERTYPEEMI 144
Cdd:PRK07165 51 INNEKGKIKINDELIELNntnkvkTSKEYFGKIIDIDGNII---YPEaqnpLSKKFLPNTSSIFNLAhglmTVKTLNEQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 145 QTGISTIDVMNSIARGQKiplfsaaglphnEIaaqIC--RQAGlvkrleKTESLLGDV---EEDNFAIVFAAMGVNMETA 219
Cdd:PRK07165 128 YTGIIAIDLLIPIGKGQR------------EL---IIgdRQTG------KTHIALNTIinqKNTNVKCIYVAIGQKRENL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 220 QFFKRDFEENGSMERvTLFLNLANDPTIERIITPRIALTTAEYLAYEcgKHVLVILTDMSSYADALREVSAAREEVPGRR 299
Cdd:PRK07165 187 SRIYETLKEHDALKN-TIIIDAPSTSPYEQYLAPYVAMAHAENISYN--DDVLIVFDDLTKHANIYREIALLTNKPVGKE 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 300 GYPGYMYTDLATIYERAGRIEGRKgSITQIPILTMPNDDITHPTPDLTGYITEGQIYIDRQLHNRQIYPPINVLPSLSRl 379
Cdd:PRK07165 264 AFPGDMFFAHSKLLERAGKFKNRK-TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR- 341
|
330 340
....*....|....*....|....*...
gi 2526887681 380 mksaIGEGMTRRDHADVS---NQLYANY 404
Cdd:PRK07165 342 ----TGSSVQSKTITKVAgeiSKIYRAY 365
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
24-90 |
2.39e-12 |
|
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: 62.18 E-value: 2.39e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 24 VSGVAGPLVILDKVKGPKYQEIVNIRLG---DGTTRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTG 90
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, ... |
21-91 |
2.04e-11 |
|
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: 59.63 E-value: 2.04e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526887681 21 YRTVSGVAGPLVILDKVKGPKYQEIVNIRLGDG---TTRRGQVLEVDGEKAVVQVFEGTSGIDNKyTTVQFTGE 91
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, ... |
393-463 |
1.03e-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: 1.03e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2526887681 393 HADVSNQLYANYAIGKDVQAMKAVVGEEALSSEDLLYLEFLDKFERkFVAQGAYDTRNIFQSLDLAWTLLR 463
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEE-FLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
27-114 |
6.29e-07 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 52.33 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526887681 27 VAGPLVILDKVKGPKYQEIVniRLGDgTTRRGQVLEVDGEKAVVQVFEGTSGIdNKYTTVQFTGEVLKTPVSLDMLGRIF 106
Cdd:PRK14698 10 VTGPLVIADGMKGAKMYEVV--RVGE-LGLIGEIIRLEGDKAVIQVYEETAGL-KPGEPVEGTGSSLSVELGPGLLTSIY 85
|
....*...
gi 2526887681 107 NGSGKPID 114
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 ... |
23-79 |
1.91e-05 |
|
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: 42.51 E-value: 1.91e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2526887681 23 TVSGVAGPLVILDKVKGPKYQEIVniRLGDgttRR--GQVLEVDGEKAVVQVFEGTSGI 79
Cdd:cd18119 3 KIYRVSGPVVVAEGMSGAAMYELV--RVGE---EGliGEIIRLEGDKATIQVYEETSGL 56
|
|
| |
