|
Name |
Accession |
Description |
Interval |
E-value |
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
3-469 |
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: 919.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 3 LLKKEYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDVARL 82
Cdd:COG1156 1 MMKKEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLKNTKVRFLGEPLEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 83 GVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANE 162
Cdd:COG1156 81 PVSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 163 IAAQIARQATVRpdlsgegEKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVA 242
Cdd:COG1156 161 LAAQIARQAKVR-------GEEEKFAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 243 EYLAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDDRT 322
Cdd:COG1156 234 EYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDIT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 323 HPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGED 402
Cdd:COG1156 314 HPIPDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499486693 403 ALTENDRRYLQFADAFERFFINQGQQ-NRSIEESLQIAWALLSMLPQGELKRISKDHIGKYYGQKLEE 469
Cdd:COG1156 394 ALSETDKKYLKFADAFERRFVNQGFDeNRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRAK 461
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-469 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 910.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 5 KKEYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDVARLGV 84
Cdd:PRK04196 1 LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLKDTKVRFTGEPLKLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 85 SKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIA 164
Cdd:PRK04196 81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 165 AQIARQATVRpdlsgegEKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEY 244
Cdd:PRK04196 161 AQIARQAKVL-------GEEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 245 LAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDDRTHP 324
Cdd:PRK04196 234 LAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 325 IPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDAL 404
Cdd:PRK04196 314 IPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEAL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499486693 405 TENDRRYLQFADAFERFFINQG-QQNRSIEESLQIAWALLSMLPQGELKRISKDHIGKYYGQKLEE 469
Cdd:PRK04196 394 SERDRKYLKFADAFEREFVNQGfDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRGK 459
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
7-463 |
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: 750.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 7 EYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDVARLGVSK 86
Cdd:TIGR01041 1 EYSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTKVRFTGETLKLPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 87 EMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQ 166
Cdd:TIGR01041 81 DMLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 167 IARQATVRpdlsgegEKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLA 246
Cdd:TIGR01041 161 IARQATVR-------GEESEFAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 247 FEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDDRTHPIP 326
Cdd:TIGR01041 234 FEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 327 DLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDALTE 406
Cdd:TIGR01041 314 DLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 499486693 407 NDRRYLQFADAFERFFINQG-QQNRSIEESLQIAWALLSMLPQGELKRISKDHIGKYY 463
Cdd:TIGR01041 394 RDRKYLKFADLFERKFVRQGfNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYH 451
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
7-466 |
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: 625.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 7 EYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDVARLGVSK 86
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDAKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 87 EMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQ 166
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 167 IARQATV--RPDLSGEGEKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEY 244
Cdd:TIGR01040 161 ICRQAGLvkLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 245 LAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDDRTHP 324
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 325 IPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDAL 404
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499486693 405 TENDRRYLQFADAFERFFINQGQ-QNRSIEESLQIAWALLSMLPQGELKRISKDHIGKYYGQK 466
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPyENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRK 463
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
79-367 |
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: 568.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 79 VARLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGL 158
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 159 PANEIAAQIARQATVRPDlsgegekEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMA 238
Cdd:cd01135 81 PHNELAAQIARQAGVVGS-------EENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 239 LTVAEYLAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPD 318
Cdd:cd01135 154 LTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMPN 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 499486693 319 DDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVG 367
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
4-466 |
1.01e-125 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 372.83 E-value: 1.01e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 4 LKKEYTGITYISGPLLFVEnAKDLAYG--AIVDIKDGTgrvRGGQVIEVSEEYAVIQVFEETTGLDlATTSVSLVEDVAR 81
Cdd:PRK02118 1 MQKIYTKITDITGNVITVE-AEGVGYGelATVERKDGS---SLAQVIRLDGDKVTLQVFGGTRGIS-TGDEVVFLGRPMQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 82 LGVSKEMLGRRFNGIGKPIDGLPPITpEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPAN 161
Cdd:PRK02118 76 VTYSESLLGRRFNGSGKPIDGGPELE-GEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 162 EIAAQIARQATVrpDLsgegekeepfaVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTV 241
Cdd:PRK02118 155 ALLARIALQAEA--DI-----------IILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 242 AEYLAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGkKGSVTQIPILSMPDDDR 321
Cdd:PRK02118 222 AEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 322 THPIPDLTGYITEGQIQLsrelhRKGiypPIDPLPSLSRLMNNGVGKgKTREDHKQVSD---QLYSAYANGVDIRKLvai 398
Cdd:PRK02118 301 THPVPDNTGYITEGQFYL-----RRG---RIDPFGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM--- 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 499486693 399 iGEDaLTENDRRYLQFADAFERFFINQgQQNRSIEESLQIAWALLSMLPQGELKRISKDHIGKYYGQK 466
Cdd:PRK02118 369 -GFK-LSNWDEKLLKFSELFESRLMDL-EVNIPLEEALDLGWKILAQCFHPEEVGIKEQLIDKYWPKN 433
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
81-361 |
1.03e-114 |
|
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: 338.66 E-value: 1.03e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 81 RLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPA 160
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 161 NEIAAQIARQATvrpdlsgegeKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALT 240
Cdd:cd19476 81 TVLAMQLARNQA----------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 241 VAEYLAFEhDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDD 320
Cdd:cd19476 151 IAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGDD 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499486693 321 RTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRL 361
Cdd:cd19476 230 LTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
134-359 |
2.08e-111 |
|
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: 327.78 E-value: 2.08e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 134 GISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQATVRpdlsgegekeepfAVVFAAMGITQRELSYFIQEFERTGA 213
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD-------------VVVYALIGERGREVREFIEELLGSGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 214 LSRSVLFLNKADDPTIERILTPRMALTVAEYLAFEhDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLAT 293
Cdd:pfam00006 68 LKRTVVVVATSDEPPLARYRAPYTALTIAEYFRDQ-GKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499486693 294 IYERAGVVEGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLS 359
Cdd:pfam00006 147 LLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 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 ... |
369-462 |
2.38e-55 |
|
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: 179.55 E-value: 2.38e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 369 GKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDALTENDRRYLQFADAFERFFINQGQQ-NRSIEESLQIAWALLSMLP 447
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYeNRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 499486693 448 QGELKRISKDHIGKY 462
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
81-361 |
4.37e-55 |
|
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: 184.69 E-value: 4.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 81 RLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPA 160
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 161 NEIAAQIARQATVrpDLsgegekeepfaVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALT 240
Cdd:cd01136 81 STLLGMIARNTDA--DV-----------NVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 241 VAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVveGKKGSVTQIPILSMPDDD 320
Cdd:cd01136 148 IAEYFR-DQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVLVEGDD 224
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 499486693 321 RTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRL 361
Cdd:cd01136 225 FNDPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
30-437 |
4.94e-53 |
|
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: 184.46 E-value: 4.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 30 GAIVDIKDGTGRVRGGQVIEVSEEYAVIQVFEETTGLdLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPITPE 109
Cdd:COG1157 41 GELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGI-SPGARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 110 KRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSG------LpaneiaAQIAR--QATVrpdlsgeg 181
Cdd:COG1157 120 ERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstlL------GMIARntEADV-------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 182 ekeepfaVVFAAMGITQRELSYFIqefERT---GALSRSVLFLNKADDPTIERILTPRMALTVAEYlaF-EHDYHVLVIL 257
Cdd:COG1157 186 -------NVIALIGERGREVREFI---EDDlgeEGLARSVVVVATSDEPPLMRLRAAYTATAIAEY--FrDQGKNVLLLM 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 258 TDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVveGKKGSVTQI-PILsMPDDDRTHPIPDLTGYITEGQ 336
Cdd:COG1157 254 DSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAFyTVL-VEGDDMNDPIADAVRGILDGH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 337 IQLSRELHRKGIYPPIDPLPSLSRLMNNGVGkgktrEDHKQVSD---QLYSAYAngvDIRKLVAI----IGEDAltENDR 409
Cdd:COG1157 331 IVLSRKLAERGHYPAIDVLASISRVMPDIVS-----PEHRALARrlrRLLARYE---ENEDLIRIgayqPGSDP--ELDE 400
|
410 420
....*....|....*....|....*....
gi 499486693 410 RyLQFADAFERfFINQGQQNR-SIEESLQ 437
Cdd:COG1157 401 A-IALIPAIEA-FLRQGMDERvSFEESLA 427
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
45-401 |
1.73e-47 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 169.55 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 45 GQVIEVSEEYAVIQVFEETTGLDlATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVAR 124
Cdd:PRK06936 61 AEVIGFAQHQALLTPLGEMYGIS-SNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSR 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 125 RKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQATVRpdlsgegekeepfAVVFAAMGITQRELSYF 204
Cdd:PRK06936 140 RLIETPLSLGVRVIDGLLTCGEGQRMGIFAAAGGGKSTLLASLIRSAEVD-------------VTVLALIGERGREVREF 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 205 IQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYP 284
Cdd:PRK06936 207 IESDLGEEGLRKAVLVVATSDRPSMERAKAGFVATSIAEYFR-DQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYP 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 285 GYMYTDLATIYERAGvvEGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNN 364
Cdd:PRK06936 286 PSVFAALPRLMERAG--QSDKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ 363
|
330 340 350
....*....|....*....|....*....|....*..
gi 499486693 365 GVGKgktreDHKQVSDQLYSAYANGVDIRKLVAiIGE 401
Cdd:PRK06936 364 IVSK-----EHKTWAGRLRELLAKYEEVELLLQ-IGE 394
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
30-393 |
2.30e-45 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 163.70 E-value: 2.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 30 GAIVDIKDGTGRVRG-GQVIEVSEEYAVIQVFEETTGLDLATtSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPITP 108
Cdd:PRK08472 40 GDIVKIESSDNGKEClGMVVVIEKEQFGISPFSFIEGFKIGD-KVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGAIDY 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 109 EKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQAtvrpdlsgegekEEPFA 188
Cdd:PRK08472 119 ERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVKGC------------LAPIK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 189 VVfAAMGITQRELSYFIqEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAFE-HDyhVLVILTDMTNYCEAL 267
Cdd:PRK08472 187 VV-ALIGERGREIPEFI-EKNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQgLD--VLFIMDSVTRFAMAQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 268 REIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGkKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKG 347
Cdd:PRK08472 263 REIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEG-KGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSRELTDFG 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 499486693 348 IYPPIDPLPSLSRLMNNGVGKgktreDHKQVSDQLYSAYA----NGVDIR 393
Cdd:PRK08472 342 IYPPINILNSASRVMNDIISP-----EHKLAARKFKRLYSllkeNEVLIR 386
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
30-361 |
1.15e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 159.78 E-value: 1.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 30 GAIVDIKDGTGRVRGgQVIEVSEEYAVIQVFEEttGLDLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPITP- 108
Cdd:PRK06002 50 GDFVAIRADGGTHLG-EVVRVDPDGVTVKPFEP--RIEIGLGDAVFRKGPLRIRPDPSWKGRVINALGEPIDGLGPLAPg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 109 EKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQATvrpdlsgegekeepF- 187
Cdd:PRK06002 127 TRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADA--------------Fd 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 188 AVVFAAMGITQRELSYFIQEFERtGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAFEHDyHVLVILTDMTNYCEAL 267
Cdd:PRK06002 193 TVVIALVGERGREVREFLEDTLA-DNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGE-NVLLIVDSVTRFAHAA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 268 REIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKG 347
Cdd:PRK06002 271 REVALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQG 350
|
330
....*....|....
gi 499486693 348 IYPPIDPLPSLSRL 361
Cdd:PRK06002 351 RYPAVDPLASISRL 364
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
46-444 |
5.10e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 157.67 E-value: 5.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 46 QVIEVSEEYAVIQVFEETTGLdlatTSVSLVEDVA---RLGVSKEMLGRRFNGIGKPIDGLPPITPEKRlPITGLPLNPV 122
Cdd:PRK06820 64 EVVSIEQEMALLSPFASSDGL----RCGQWVTPLGhmhQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 123 ARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIAR--QATVrpdlsgegekeepfaVVFAAMGITQRE 200
Cdd:PRK06820 139 TRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCAdsAADV---------------MVLALIGERGRE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 201 LSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGR 280
Cdd:PRK06820 204 VREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 281 RGYPGYMYTDLATIYERAGVVEgkKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSR 360
Cdd:PRK06820 283 GSFPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSR 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 361 LMNNGVGKGktredHKQVSDQLYSAYANGVDIRKLVAI----IGEDALT-ENDRRYlqfaDAFERFFINQGQQNRSIEES 435
Cdd:PRK06820 361 IMPQIVSAG-----QLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQAdEALQRY----PAICAFLQQDHSETAHLETT 431
|
....*....
gi 499486693 436 LQIAWALLS 444
Cdd:PRK06820 432 LEHLAQVVG 440
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
82-398 |
1.14e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 156.78 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 82 LGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPAN 161
Cdd:PRK08972 97 LPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKS 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 162 EIAAQIARQATVRpdlsgegekeepfAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTV 241
Cdd:PRK08972 177 VLLGMMTRGTTAD-------------VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTI 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 242 AEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDDR 321
Cdd:PRK08972 244 AEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLTEGDDL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 322 THPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMnngvgKGKTREDHKQVS---DQLYSAYANGVDirkLVAI 398
Cdd:PRK08972 323 QDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-----PMVISEEHLEAMrrvKQVYSLYQQNRD---LISI 394
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
26-422 |
1.44e-42 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 156.47 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 26 DLAYGAIVDIKDGTGRV-RGGQVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDVArLGVSKEMLGRRFNGIGKPIDGLP 104
Cdd:PRK09099 42 DVTLGELCELRQRDGTLlQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLS-VPVGPALLGRVIDGLGEPIDGGG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 105 PITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQAtvRPDLSgegeke 184
Cdd:PRK09099 121 PLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARGT--QCDVN------ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 185 epfavVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYC 264
Cdd:PRK09099 193 -----VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFR-DRGLRVLLMMDSLTRFA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 265 EALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVveGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELH 344
Cdd:PRK09099 267 RAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITALYTVLAEDESGSDPIAEEVRGILDGHMILSREIA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 345 RKGIYPPIDPLPSLSRLMNNGVGKgktreDHKQVSDQLYSAYANGVDIRKLVAI----IGEDALTEndrRYLQFADAFER 420
Cdd:PRK09099 345 ARNQYPAIDVLGSLSRVMPQVVPR-----EHVQAAGRLRQLLAKHREVETLLQVgeyrAGSDPVAD---EAIAKIDAIRD 416
|
..
gi 499486693 421 FF 422
Cdd:PRK09099 417 FL 418
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
76-443 |
1.27e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 148.73 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 76 VEDVARLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSG 155
Cdd:PRK05688 97 LADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 156 SGLPANEIAAQIARQATVrpDLsgegekeepfaVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTP 235
Cdd:PRK05688 177 TGVGKSVLLGMMTRFTEA--DI-----------IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDAPLMRLRAA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 236 RMALTVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILS 315
Cdd:PRK05688 244 MYCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGSITAFYTVL 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 316 MPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVGKGKTREdhKQVSDQLYSAYANGVDIRKL 395
Cdd:PRK05688 323 SEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDPEHLRR--AQRFKQLWSRYQQSRDLISV 400
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 499486693 396 VAII-GEDALTENdrrylqfadAFERF-----FINQG-QQNRSIEESLQIAWALL 443
Cdd:PRK05688 401 GAYVaGGDPETDL---------AIARFphlvqFLRQGlRENVSLAQSREQLAAIF 446
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
27-362 |
4.61e-39 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 146.66 E-value: 4.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 27 LAYGAIVDIKDGTGRVRGGQVIEVSEEYAVIQVFEETTGLDLATTSVsLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPI 106
Cdd:PRK08927 38 LSVGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAV-IANAAAAVRPSRAWLGRVVNALGEPIDGKGPL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 107 TP-EKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQATVRpdlsgegekee 185
Cdd:PRK08927 117 PQgPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNADAD----------- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 186 pfAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYCE 265
Cdd:PRK08927 186 --VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR-DQGKDVLCLMDSVTRFAM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 266 ALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHR 345
Cdd:PRK08927 263 AQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGILDGHIVMERAIAE 342
|
330
....*....|....*..
gi 499486693 346 KGIYPPIDPLPSLSRLM 362
Cdd:PRK08927 343 RGRYPAINVLKSVSRTM 359
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
81-392 |
2.09e-38 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 145.31 E-value: 2.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 81 RLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPA 160
Cdd:PRK07960 109 QLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGK 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 161 NEIAAQIAR--QATVrpdlsgegekeepfaVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMA 238
Cdd:PRK07960 189 SVLLGMMARytQADV---------------IVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 239 LTVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKGSVTQIPILSMPD 318
Cdd:PRK07960 254 TRIAEDFR-DRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEG 332
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499486693 319 DDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVGKGKTREdhKQVSDQLYSAYANGVDI 392
Cdd:PRK07960 333 DDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDEQHYAR--VRQFKQLLSSFQRNRDL 404
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
36-450 |
2.49e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 144.87 E-value: 2.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 36 KDGTGRVRGgQVIEVSEEYAVIQVFEETTGLDLAttsvSLVEDVA---RLGVSKEMLGRRFNGIGKPIDG--LPP-ITPe 109
Cdd:PRK07721 49 GGGDKAIKA-EVVGFKDEHVLLMPYTEVAEIAPG----CLVEATGkplEVKVGSGLIGQVLDALGEPLDGsaLPKgLAP- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 110 krLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQATVrpDLSgegekeepfav 189
Cdd:PRK07721 123 --VSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSA--DLN----------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 190 VFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYCEALRE 269
Cdd:PRK07721 188 VIALIGERGREVREFIERDLGPEGLKRSIVVVATSDQPALMRIKGAYTATAIAEYFR-DQGLNVMLMMDSVTRVAMAQRE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 270 IGAAREEIPGRRGYPGYMYTDLATIYERAGVVEgkKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIY 349
Cdd:PRK07721 267 IGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 350 PPIDPLPSLSRLMNNGVgkgktREDHKQVSD---QLYSAYANGVDirklvaIIGEDALTENDRRYLQFADAFERF---FI 423
Cdd:PRK07721 345 PAINVLKSVSRVMNHIV-----SPEHKEAANrfrELLSTYQNSED------LINIGAYKRGSSREIDEAIQFYPQiisFL 413
|
410 420
....*....|....*....|....*...
gi 499486693 424 NQG-QQNRSIEESLQiawALLSMLPQGE 450
Cdd:PRK07721 414 KQGtDEKATFEESIQ---ALLSLFGKGE 438
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
46-420 |
2.70e-36 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 139.26 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 46 QVIEVSEEYAVIQVFEETTGLdLATTSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARR 125
Cdd:PRK07196 55 QVVGFDRDITYLMPFKHPGGV-LGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 126 KPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIAR--QATVrpdlsgegekeepfaVVFAAMGITQRELSY 203
Cdd:PRK07196 134 AVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRytQADV---------------VVVGLIGERGREVKE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 204 FIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGY 283
Cdd:PRK07196 199 FIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYR-DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGY 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 284 PGYMYTDLATIYERAGVVEGkKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMN 363
Cdd:PRK07196 278 PPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499486693 364 NGVGKgktreDHKQVSDQLYSAYANGVDIRKLVA----IIGEDALTENDRRYLQFADAFER 420
Cdd:PRK07196 357 QVIGS-----QQAKAASLLKQCYADYMAIKPLIPlggyVAGADPMADQAVHYYPAITQFLR 412
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
84-421 |
3.89e-36 |
|
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: 139.08 E-value: 3.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 84 VSKEMLGRRFNGIGKPIDGLPPITPEKRLPItglplnpvaRRKPEQFIQ---------TGISTIDVMNTLVRGQKLPIFS 154
Cdd:TIGR01039 80 VGKETLGRIFNVLGEPIDEKGPIPAKERWPI---------HRKAPSFEEqstkveileTGIKVIDLLAPYAKGGKIGLFG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 155 GSGLPAN----EIAAQIARQAtvrpdlSGEGekeepfavVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIE 230
Cdd:TIGR01039 151 GAGVGKTvliqELINNIAKEH------GGYS--------VFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 231 RILTPRMALTVAEYLAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERagVVEGKKGSVTQ 310
Cdd:TIGR01039 217 RMRVALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQER--ITSTKTGSITS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 311 IPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMN-NGVGkgktrEDHKQVSDQLYSAYANG 389
Cdd:TIGR01039 295 VQAVYVPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDpSVVG-----EEHYDVARGVQQILQRY 369
|
330 340 350
....*....|....*....|....*....|..
gi 499486693 390 VDIRKLVAIIGEDALTENDRRYLQFADAFERF 421
Cdd:TIGR01039 370 KELQDIIAILGMDELSEEDKLTVERARRIQRF 401
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
46-406 |
3.04e-34 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 133.54 E-value: 3.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 46 QVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDvARLGVSKEMLGRRFNGIGKPIDGLP-PITPEKRLpiTGLPLNPVAR 124
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGLHCGQQVMALRRR-HQVPVGEALLGRVIDGFGRPLDGRElPDVCWKDY--DAMPPPAMVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 125 RKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQatvrPDLSgegekeepfAVVFAAMGITQRELSYF 204
Cdd:PRK07594 133 QPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAMLCNA----PDAD---------SNVLVLIGERGREVREF 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 205 IQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYP 284
Cdd:PRK07594 200 IDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYP 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 285 GYMYTDLATIYERAGVveGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNN 364
Cdd:PRK07594 279 PGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPV 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499486693 365 GVGkgktrEDHKQVSDQLYSAYANGVDIRKLVAI----IGEDALTE 406
Cdd:PRK07594 357 VTS-----HEHRQLAAILRRCLALYQEVELLIRIgeyqRGVDTDTD 397
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
46-461 |
5.72e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 129.71 E-value: 5.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 46 QVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDVArLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARR 125
Cdd:PRK06793 56 EVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVV-IPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFERE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 126 KPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQAtvRPDLSgegekeepfavVFAAMGITQRELSYFI 205
Cdd:PRK06793 135 EITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNA--KADIN-----------VISLVGERGREVKDFI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 206 QEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPgRRGYPG 285
Cdd:PRK06793 202 RKELGEEGMRKSVVVVATSDESHLMQLRAAKLATSIAEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELP-IGGKTL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 286 YMYTDLATIYERAGvvEGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNG 365
Cdd:PRK06793 280 LMESYMKKLLERSG--KTQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 366 VGkgktrEDHKQVSDQlysayangvdIRKLVAIIGEDALTendrrylqfadaFERFFINQGQQNRSIEESLQIAWALLSM 445
Cdd:PRK06793 358 VS-----PNHWQLANE----------MRKILSIYKENELY------------FKLGTIQENAENAYIFECKNKVEGINTF 410
|
410
....*....|....*.
gi 499486693 446 LPQGELKRISKDHIGK 461
Cdd:PRK06793 411 LKQGRSDSFQFDDIVE 426
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
30-382 |
1.52e-31 |
|
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: 126.73 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 30 GAIVDIKDGTGRVRG------GQVIEVSE-EYAVIQVFEETT--------GLDLAT-TSVSLVEDVARLGVSKEMLGRRF 93
Cdd:TIGR00962 28 GTVVSVGDGIARVYGlenvmsGELIEFEGgVQGIALNLEEDSvgavimgdYSDIREgSTVKRTGRILEVPVGDGLLGRVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 94 NGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSG--SGLPANEIAAQIArqa 171
Cdd:TIGR00962 108 NALGEPIDGKGPIDSDEFSPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDrqTGKTAVAIDTIIN--- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 172 tvrpdlsgegEKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLaFEHDY 251
Cdd:TIGR00962 185 ----------QKDSDVYCIYVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYF-RDNGK 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 252 HVLVILTDMTNYCEALREIGAAREEIPGRRGYPG---YMYTDLatiYERAGVV--EGKKGSVTQIPILSMPDDDRTHPIP 326
Cdd:TIGR00962 254 HALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGdvfYLHSRL---LERAAKLndEKGGGSLTALPIIETQAGDVSAYIP 330
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 499486693 327 DLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRlmnngVGKGKTREDHKQVSDQL 382
Cdd:TIGR00962 331 TNVISITDGQIFLESDLFNSGIRPAINVGLSVSR-----VGGAAQIKAMKQVAGSL 381
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
14-361 |
1.50e-30 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 122.80 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 14 ISGPLLFVEnAKDLAYGAIVDIKdgtgrvRGGQVIEVSEEYAVIQVFEETTGLDLATTSVSLVEDVA--------RLGVS 85
Cdd:PRK08149 13 IQGPIIEAE-LPDVAIGEICEIR------AGWHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQVVlkptgkplSVWVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 86 KEMLGRRFNGIGKPIDGL-PPITPE---KRLPITGLPLnPVARRKP--EQFIqTGISTIDVMNTLVRGQKLPIFSGSGLP 159
Cdd:PRK08149 86 EALLGAVLDPTGKIVERFdAPPTVGpisEERVIDVAPP-SYAERRPirEPLI-TGVRAIDGLLTCGVGQRMGIFASAGCG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 160 ANEIAAQIARQAtvrpdlsgegekeEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMAL 239
Cdd:PRK08149 164 KTSLMNMLIEHS-------------EADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVAT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 240 TVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVVegKKGSVTQIPILSMPDD 319
Cdd:PRK08149 231 TVAEYFR-DQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESE 307
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 499486693 320 DRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRL 361
Cdd:PRK08149 308 EEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| 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 ... |
7-73 |
7.16e-29 |
|
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: 108.29 E-value: 7.16e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499486693 7 EYTGITYISGPLLFVENAKDLAYGAIVDIKDGTGRVRGGQVIEVSEEYAVIQVFEETTGLDLATTSV 73
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKGTKV 67
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
84-363 |
8.21e-29 |
|
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: 114.62 E-value: 8.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 84 VSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGlPLNPVARRKPEQFI-QTGISTIDVMNTLVRGQKLPIFSGSGLPAN- 161
Cdd:cd01133 4 VGEETLGRIFNVLGEPIDERGPIKAKERWPIHR-EAPEFVELSTEQEIlETGIKVVDLLAPYAKGGKIGLFGGAGVGKTv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 162 ---EIAAQIARQATVRpdlsgegekeepfaVVFAAMGITQRELSYFIQEFERTG-----ALSRSVLFLNKADDPTIERIL 233
Cdd:cd01133 83 limELINNIAKAHGGY--------------SVFAGVGERTREGNDLYHEMKESGvinldGLSKVALVYGQMNEPPGARAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 234 TPRMALTVAEYLAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERagVVEGKKGSVTQIPI 313
Cdd:cd01133 149 VALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQER--ITSTKKGSITSVQA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 499486693 314 LSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMN 363
Cdd:cd01133 227 VYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILD 276
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
56-403 |
9.47e-28 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 115.00 E-value: 9.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 56 VIQVFEETTgLDLATT---SVSLVEDV------ARLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRK 126
Cdd:PRK05922 58 VIGFHNRTT-LLMSLSpihYVALGAEVlplrrpPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQP 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 127 PEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIAR--QATVRpdlsgegekeepfavVFAAMGITQRELSYF 204
Cdd:PRK05922 137 IQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKgsKSTIN---------------VIALIGERGREVREY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 205 IQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYP 284
Cdd:PRK05922 202 IEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 285 GYMYTDLATIYERAGvvEGKKGSVTQI-PILSMPDddrtHP--IPDLTGYITEGQIQLSRElHRKGIYPPIDPLPSLSRl 361
Cdd:PRK05922 281 ASVFHHVSEFTERAG--NNDKGSITALyAILHYPN----HPdiFTDYLKSLLDGHFFLTPQ-GKALASPPIDILTSLSR- 352
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499486693 362 mnngVGKGKTREDHKQVSDQLYS---AYANGVDIRKLVAII-GEDA 403
Cdd:PRK05922 353 ----SARQLALPHHYAAAEELRSllkAYHEALDIIQLGAYVpGQDA 394
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
84-360 |
4.12e-27 |
|
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: 109.96 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 84 VSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEI 163
Cdd:cd01132 6 VGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTGKTAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 164 AAQ-IARQatvrpdlsgegeKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVA 242
Cdd:cd01132 86 AIDtIINQ------------KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 243 EYLAFEHDyHVLVILTDMTNYCEALREIGAAREEIPGRRGYPG---YMYTDLatiYERAGVV--EGKKGSVTQIPILSMP 317
Cdd:cd01132 154 EYFRDNGK-HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 499486693 318 DDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSR 360
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
9-387 |
1.31e-25 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 109.23 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 9 TGITYISGpllfVENAkdlAYGAIVDIKDGtgrvRGGQVIEVSEEYAVIQVFEETTGLdLATTSVSLVEDVARLGVSKEM 88
Cdd:PRK13343 36 DGIAFVSG----LPDA---ALDELLRFEGG----SRGFAFNLEEELVGAVLLDDTADI-LAGTEVRRTGRVLEVPVGDGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 89 LGRRFNGIGKPIDGLPPITPEKRLPITGlPLNPVARRKP-EQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQ- 166
Cdd:PRK13343 104 LGRVIDPLGRPLDGGGPLQATARRPLER-PAPAIIERDFvTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDa 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 167 IARQatvrpdlsgegeKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLa 246
Cdd:PRK13343 183 IINQ------------KDSDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYF- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 247 FEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVV--EGKKGSVTQIPILSMPDDDRTHP 324
Cdd:PRK13343 250 RDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLspELGGGSLTALPIIETLAGELSAY 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499486693 325 IPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRlmnngVGkGKTREDH-KQVSDQLYSAYA 387
Cdd:PRK13343 330 IPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR-----VG-GKAQHPAiRKESGRLRLDYA 387
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
84-421 |
1.28e-24 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 106.28 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 84 VSKEMLGRRFNGIGKPIDGLPPITPEKRLPItglplnpvaRRKPEQFIQ---------TGISTIDVMNTLVRGQKLPIFS 154
Cdd:CHL00060 98 VGGATLGRIFNVLGEPVDNLGPVDTRTTSPI---------HRSAPAFIQldtklsifeTGIKVVDLLAPYRRGGKIGLFG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 155 GSGLPAN----EIAAQIArqatvrpdlsgegeKEEPFAVVFAAMGITQRELSYFIQEFERTGAL-------SRSVLFLNK 223
Cdd:CHL00060 169 GAGVGKTvlimELINNIA--------------KAHGGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSKVALVYGQ 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 224 ADDPTIERILTPRMALTVAEYLAFEHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERagVVEG 303
Cdd:CHL00060 235 MNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQER--ITST 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 304 KKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRLMNNGVgkgktredhkqVSDQLY 383
Cdd:CHL00060 313 KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRI-----------VGEEHY 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499486693 384 SAyANGV--------DIRKLVAIIGEDALTENDRRYLQFADAFERF 421
Cdd:CHL00060 382 ET-AQRVkqtlqrykELQDIIAILGLDELSEEDRLTVARARKIERF 426
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
84-422 |
2.10e-23 |
|
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: 102.48 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 84 VSKEMLGRRFNGIGKPIDGLPPITPEKRLPITGLPLnPVARRKPEQFI-QTGISTIDVMNTLVRGQKLPIFSGSG----- 157
Cdd:COG0055 83 VGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAP-PFEEQSTKTEIlETGIKVIDLLAPYAKGGKIGLFGGAGvgktv 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 158 LpaneIAAQIARQATVRPDLSgegekeepfavVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRM 237
Cdd:COG0055 162 L----IMELIHNIAKEHGGVS-----------VFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALT 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 238 ALTVAEYlaFEHDYH--VLVILTDMTNYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERagVVEGKKGSVTQIPILS 315
Cdd:COG0055 227 ALTMAEY--FRDEEGqdVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQER--ITSTKKGSITSVQAVY 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 316 MPDDDRTHPIP-------DLTgyitegqIQLSRELHRKGIYPPIDPLPSLSRLMN-NGVGkgktrEDHKQVsdqlysayA 387
Cdd:COG0055 303 VPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDpLIVG-----EEHYRV--------A 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 499486693 388 NGV-----------DIrklVAIIGEDALTENDRRYLQFADAFERFF 422
Cdd:COG0055 363 REVqrilqrykelqDI---IAILGMDELSEEDKLTVARARKIQRFL 405
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
71-382 |
1.83e-21 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 96.96 E-value: 1.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 71 TSVSLVEDVARLGVSKEMLGRRFNGIGKPIDGLPPI-TPEKRL---PITGLplnpVARRKPEQFIQTGISTIDVMNTLVR 146
Cdd:CHL00059 65 SSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEIsASESRLiesPAPGI----ISRRSVYEPLQTGLIAIDSMIPIGR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 147 GQKLPIFSGSGLPANEIAAQ-IARQatvrpdlsgegeKEEPFAVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKAD 225
Cdd:CHL00059 141 GQRELIIGDRQTGKTAVATDtILNQ------------KGQNVICVYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETAD 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 226 DPTIERILTPRMALTVAEYLAFEhDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPG---YMYTDLatiYERAGVVE 302
Cdd:CHL00059 209 SPATLQYLAPYTGAALAEYFMYR-GRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 303 GK--KGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSRlmnngVGKGKTREDHKQVSD 380
Cdd:CHL00059 285 SQlgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR-----VGSAAQIKAMKQVAG 359
|
..
gi 499486693 381 QL 382
Cdd:CHL00059 360 KL 361
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
189-425 |
3.15e-19 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 91.24 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 189 VVFAAMGITQRELSYFIQEFER-----TGA--LSRSVLFLNKADDPTIERILTPRMALTVAEYLAfEHDYHVLVILTDMT 261
Cdd:PRK14698 685 VIYIGCGERGNEMTDVLEEFPKlkdpkTGKplMERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 262 NYCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVV-----EGKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQ 336
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVF 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 337 IQLSRELHRKGIYPPIDPLPSLSRLMN--NGVGKGKTREDHKQVSDQLYSAYANGVDIRKLVAIIGEDALTENDRRYLQF 414
Cdd:PRK14698 844 WALDADLARRRHFPAINWLTSYSLYVDavKDWWHKNVDPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILLV 923
|
250
....*....|.
gi 499486693 415 ADAFERFFINQ 425
Cdd:PRK14698 924 ARMLREDYLQQ 934
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
121-360 |
9.56e-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: 86.47 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 121 PVARR-KPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIAAQIARQATVRpdlsgegekeepfAVVFAAMGITQR 199
Cdd:cd01134 49 PVKEKlPPNVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD-------------VVIYVGCGERGN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 200 ELSYFIQEF-----ERTGA--LSRSVLFLNKADDPTIERILTPRMALTVAEYLafeHD--YHVLvILTDMTN-YCEALRE 269
Cdd:cd01134 116 EMAEVLEEFpelkdPITGEslMERTVLIANTSNMPVAAREASIYTGITIAEYF---RDmgYNVS-LMADSTSrWAEALRE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 270 IGAAREEIPGRRGYPGYMYTDLATIYERAGVVE-----GKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELH 344
Cdd:cd01134 192 ISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRclgspGREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLA 271
|
250
....*....|....*.
gi 499486693 345 RKGIYPPIDPLPSLSR 360
Cdd:cd01134 272 QRRHFPSINWLISYSK 287
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
11-429 |
4.77e-18 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 86.76 E-value: 4.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 11 ITYISGPLLFVENAKDLAYGAIVDIkDGTGRVrgGQVIEVSEEYAVIQVFEETTGL---DLATTSVSLVEdvARLGVSke 87
Cdd:PRK04192 7 IVRVSGPLVVAEGMGGARMYEVVRV-GEEGLI--GEIIRIEGDKATIQVYEETSGIkpgEPVEFTGEPLS--VELGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 88 MLGRRFNGIGKPID--------------GLPPITPEKR---------------------LPITGL-------PLN----- 120
Cdd:PRK04192 80 LLGSIFDGIQRPLDelaeksgdflergvYVPALDREKKweftptvkvgdkveagdilgtVQETPSiehkimvPPGvsgtv 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 121 -------------PVAR-------------------RKPEQFIQ---------TGISTIDVMNTLVRGQKLPI---FsGS 156
Cdd:PRK04192 160 keivsegdytvddTIAVlededgegveltmmqkwpvRRPRPYKEklppvepliTGQRVIDTFFPVAKGGTAAIpgpF-GS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 157 GLPANEiaAQIARQATVRpdlsgegekeepfAVVFAAMGitQR--ELSYFIQEFE-----RTGA--LSRSVLFLNKADDP 227
Cdd:PRK04192 239 GKTVTQ--HQLAKWADAD-------------IVIYVGCG--ERgnEMTEVLEEFPelidpKTGRplMERTVLIANTSNMP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 228 TIER---ILTprmALTVAEYLafeHD--YHVLvILTDMTN-YCEALREIGAAREEIPGRRGYPGYMYTDLATIYERAGVV 301
Cdd:PRK04192 302 VAAReasIYT---GITIAEYY---RDmgYDVL-LMADSTSrWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRV 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 302 E---GKKGSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIYPPIDPLPSLSrLMNNGVGK---GKTREDH 375
Cdd:PRK04192 375 KtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYS-LYLDQVAPwweENVDPDW 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 499486693 376 KQVSDQLYSAYANGVDIRKLVAIIGEDALTENDRRYLQFADaferfFINQG--QQN 429
Cdd:PRK04192 454 RELRDEAMDLLQREAELQEIVRLVGPDALPEEDRLILEVAR-----LIREDflQQN 504
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
113-360 |
2.70e-17 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 84.25 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 113 PITGLPLNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIF--SGSG---LPANEIAAQiaRQATVRpdlsgegekeepf 187
Cdd:PRK07165 109 SIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIgdRQTGkthIALNTIINQ--KNTNVK------------- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 188 aVVFAAMGITQRELSYFIQEFERTGALSRSVLFLNKADDPtIERILTPRMALTVAEYLAFEHDyhVLVILTDMTNYCEAL 267
Cdd:PRK07165 174 -CIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMAHAENISYNDD--VLIVFDDLTKHANIY 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 268 REIGAAREEIPGRRGYPGYMYTDLATIYERAGVVEGKKgSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKG 347
Cdd:PRK07165 250 REIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK-TITALPILQTVDNDITSLISSNIISITDGQIVTSSDLFASG 328
|
250
....*....|...
gi 499486693 348 IYPPIDPLPSLSR 360
Cdd:PRK07165 329 KLPAIDIDLSVSR 341
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
84-360 |
1.06e-14 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 76.26 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 84 VSKEMLGRRFNGIGKPIDGLPPITPEKRLPITgLPLNPVARRKP-EQFIQTGISTIDVMNTLVRGQK-LPIfsG---SGL 158
Cdd:PRK09281 99 VGEALLGRVVNPLGQPIDGKGPIEATETRPVE-RKAPGVIDRKSvHEPLQTGIKAIDAMIPIGRGQReLII--GdrqTGK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 159 PANEIAAQIArqatvrpdlsgegEKEEPFAVVFAAMGitQRELSY--FIQEFERTGALSRSVLFLNKADDPTIERILTPR 236
Cdd:PRK09281 176 TAIAIDTIIN-------------QKGKDVICIYVAIG--QKASTVaqVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPY 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 237 MALTVAEYlaF-EHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPG---YMYTDLatiYERAGVV--EGKKGSVTQ 310
Cdd:PRK09281 241 AGCAMGEY--FmDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLsdELGGGSLTA 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499486693 311 IPIlsmpdddrthpIP----DLTGY-------ITEGQIQLSRELHRKGIYPPIDPLPSLSR 360
Cdd:PRK09281 316 LPI-----------IEtqagDVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
79-360 |
1.63e-13 |
|
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: 72.38 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 79 VARLGVSKEMLGRRFNGIGKPIDGLPPITPEKRLPITgLPLNPVARRKP-EQFIQTGISTIDVMNTLVRGQK-LPIfsG- 155
Cdd:COG0056 94 ILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERRPVE-RPAPGVIDRQPvHEPLQTGIKAIDAMIPIGRGQReLII--Gd 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 156 --SGLPAneIA-----AQiarqatvrpdlsgegeKEEPFAVVFAAMGitQRELSY--FIQEFERTGALSRSVLFLNKADD 226
Cdd:COG0056 171 rqTGKTA--IAidtiiNQ----------------KGKDVICIYVAIG--QKASTVaqVVETLEEHGAMEYTIVVAATASD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 227 PTIERILTPRMALTVAEYlaF-EHDYHVLVILTDMTNYCEALREIGAAREEIPGRRGYPG---YMYTDLatiYERAGVV- 301
Cdd:COG0056 231 PAPLQYIAPYAGCAMGEY--FmDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLHSRL---LERAAKLs 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499486693 302 -EGKKGSVTQIPIlsmpdddrthpIP----DLTGY-------ITEGQIQLSRELHRKGIYPPIDPLPSLSR 360
Cdd:COG0056 306 dELGGGSLTALPI-----------IEtqagDVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
115-397 |
5.91e-12 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 67.76 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 115 TGLPlNPVARRKPEQFIQTGISTIDVMNTLVRGQKLPIFSGSGLPANEIA-AQIARQATVRPDLSGEGekeepfAVVFAA 193
Cdd:PTZ00185 158 AGAP-NIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAvSTIINQVRINQQILSKN------AVISIY 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 194 MGITQR--ELSYFIQEFERTGALSRSVLFLNKADDPTIERILTPRMALTVAEYLaFEHDYHVLVILTDMTNYCEALREIG 271
Cdd:PTZ00185 231 VSIGQRcsNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYF-MNRGRHCLCVYDDLSKQAVAYRQIS 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 272 AAREEIPGRRGYPGYMYTDLATIYERAGVVEGKK--GSVTQIPILSMPDDDRTHPIPDLTGYITEGQIQLSRELHRKGIY 349
Cdd:PTZ00185 310 LLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQR 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 499486693 350 PPIDPLPSLSRlmnngVGKGKTREDHKQVSDQLYSAYAngvDIRKLVA 397
Cdd:PTZ00185 390 PAVNIGLSVSR-----VGSSAQNVAMKAVAGKLKGILA---EYRKLAA 429
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
375-443 |
1.11e-11 |
|
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: 60.15 E-value: 1.11e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 375 HKQVSDQLYSAYANGVDIRKLVAIIGEDALTENDRRYLQFADAFERFfINQGQQ-NRSIEESLQIAWALL 443
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEF-LQQGQFePETIEDTLEKLYPIK 69
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
11-67 |
6.64e-07 |
|
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: 46.38 E-value: 6.64e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 499486693 11 ITYISGPLLFVENAKDLAYGAIVDIKDGT---GRVRGGQVIEVSEEYAVIQVFEETTGLD 67
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVELvefGSLVLGEVLNLGGDKVRVQVFGGTSGLS 60
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
14-67 |
2.57e-04 |
|
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: 39.22 E-value: 2.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499486693 14 ISGPLLFVENAKDLAYGAIVDIKDG---TGRVRGGQVIEVSEEYAVIQVFEETTGLD 67
Cdd:cd01426 7 VNGPLVEAELEGEVAIGEVCEIERGdgnNETVLKAEVIGFRGDRAILQLFESTRGLS 63
|
|
| 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 ... |
11-66 |
3.96e-04 |
|
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: 38.66 E-value: 3.96e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 499486693 11 ITYISGPLLFVENAKDLAYGAIVDIkdgtGRVR-GGQVIEVSEEYAVIQVFEETTGL 66
Cdd:cd18119 4 IYRVSGPVVVAEGMSGAAMYELVRV----GEEGlIGEIIRLEGDKATIQVYEETSGL 56
|
|
| |
