|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
1-466 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 928.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 1 MKEYQTITEISGPLVFVETDEPVGYDDIVEIELSDGETRRGQVLESASDYVAIQVFEGTEGID-RDASVRFLGETMKMPV 79
Cdd:PRK04196 1 LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 80 TEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLA 159
Cdd:PRK04196 81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 160 LQIARQATVPEEEDGeddegseFAVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEY 239
Cdd:PRK04196 161 AQIARQAKVLGEEEN-------FAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 240 LAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPGDDDTHP 319
Cdd:PRK04196 234 LAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 320 IPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEGLTRADHADVKDQIFAAYAEGEDLRDLVNIVGREAL 399
Cdd:PRK04196 314 IPDLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEAL 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491102979 400 SELDNKYLDFADRFEEEFVDQGTDTARSIDETLELGWDLLSMLPKDALNRIDEDLIEEHYREDETAE 466
Cdd:PRK04196 394 SERDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRGKE 460
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
2-466 |
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: 900.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 2 KEYQTITEISGPLVFVETDEPVGYDDIVEIELSDGETRRGQVLESASDYVAIQVFEGTEGID-RDASVRFLGETMKMPVT 80
Cdd:COG1156 4 KEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSlKNTKVRFLGEPLELPVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 81 EDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLAL 160
Cdd:COG1156 84 EDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 161 QIARQATVPEEEDGeddegseFAVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYL 240
Cdd:COG1156 164 QIARQAKVRGEEEK-------FAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 241 AFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPGDDDTHPI 320
Cdd:COG1156 237 AFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDITHPI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 321 PDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEGLTRADHADVKDQIFAAYAEGEDLRDLVNIVGREALS 400
Cdd:COG1156 317 PDLTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEEALS 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491102979 401 ELDNKYLDFADRFEEEFVDQGTDTARSIDETLELGWDLLSMLPKDALNRIDEDLIEEHYREDETAE 466
Cdd:COG1156 397 ETDKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRAKE 462
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
3-466 |
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: 827.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 3 EYQTITEISGPLVFVETDEPVGYDDIVEIELSDGETRRGQVLESASDYVAIQVFEGTEGIDRDAS-VRFLGETMKMPVTE 81
Cdd:TIGR01041 1 EYSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTkVRFTGETLKLPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 82 DLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQ 161
Cdd:TIGR01041 81 DMLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 162 IARQATVPEEEDGeddegseFAVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLA 241
Cdd:TIGR01041 161 IARQATVRGEESE-------FAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 242 FEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPGDDDTHPIP 321
Cdd:TIGR01041 234 FEKDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 322 DLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEGLTRADHADVKDQIFAAYAEGEDLRDLVNIVGREALSE 401
Cdd:TIGR01041 314 DLTGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSE 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491102979 402 LDNKYLDFADRFEEEFVDQGTDTARSIDETLELGWDLLSMLPKDALNRIDEDLIEEHYREDETAE 466
Cdd:TIGR01041 394 RDRKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYHPKYRKKK 458
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
3-464 |
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: 639.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 3 EYQTITEISGPLVFVETDEPVGYDDIVEIELSDGETRRGQVLESASDYVAIQVFEGTEGID-RDASVRFLGETMKMPVTE 81
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDaKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 82 DLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQ 161
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 162 IARQATV--PEEEDGEDDEGSEFAVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEY 239
Cdd:TIGR01040 161 ICRQAGLvkLPTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 240 LAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPGDDDTHP 319
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 320 IPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEGLTRADHADVKDQIFAAYAEGEDLRDLVNIVGREAL 399
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491102979 400 SELDNKYLDFADRFEEEFVDQGTDTARSIDETLELGWDLLSMLPKDALNRIDEDLIEEHYREDET 464
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKSA 465
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
74-362 |
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: 565.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 74 TMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGL 153
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 154 PHNDLALQIARQATVPEEEDGeddegseFAVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLA 233
Cdd:cd01135 81 PHNELAAQIARQAGVVGSEEN-------FAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 234 LTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPG 313
Cdd:cd01135 154 LTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMPN 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 491102979 314 DDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIG 362
Cdd:cd01135 234 DDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
2-459 |
1.88e-134 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 394.79 E-value: 1.88e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 2 KEYQTITEISGPLVFVETdEPVGYDDIVEIELSDGeTRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTE 81
Cdd:PRK02118 3 KIYTKITDITGNVITVEA-EGVGYGELATVERKDG-SSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 82 DLLGRVMDGTGQPIDGGPEIVpDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQ 161
Cdd:PRK02118 81 SLLGRRFNGSGKPIDGGPELE-GEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 162 IARQATVPEeedgeddegsefaVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLA 241
Cdd:PRK02118 160 IALQAEADI-------------IILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 242 FEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGrEGSVTQLPILTMPGDDDTHPIP 321
Cdd:PRK02118 227 LEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHPVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 322 DLTGYITEGQIYIDRDlnsqGIQPpinvLPSLSRLMDDGIGEgLTRADHADVKD---QIFAAYAEGEDLRDLvnivGREa 398
Cdd:PRK02118 306 DNTGYITEGQFYLRRG----RIDP----FGSLSRLKQLVIGK-KTREDHGDLMNamiRLYADSREAKEKMAM----GFK- 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491102979 399 LSELDNKYLDFADRFEEEFVDqgTDTARSIDETLELGWDLLSMLPKDALNRIDEDLIEEHY 459
Cdd:PRK02118 372 LSNWDEKLLKFSELFESRLMD--LEVNIPLEEALDLGWKILAQCFHPEEVGIKEQLIDKYW 430
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
76-356 |
1.66e-112 |
|
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: 332.50 E-value: 1.66e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 76 KMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPH 155
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 156 NDLALQIARQATvpeeedgeddEGSEFAVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALT 235
Cdd:cd19476 81 TVLAMQLARNQA----------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 236 TAEYLAFEkDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPGDD 315
Cdd:cd19476 151 IAEYFRDN-GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGDD 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 491102979 316 DTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRL 356
Cdd:cd19476 230 LTDPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
129-354 |
1.78e-109 |
|
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: 322.38 E-value: 1.78e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 129 GVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQIARQATVPeeedgeddegsefAVIFGAMGITAEEANEFMDDFERTGA 208
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD-------------VVVYALIGERGREVREFIEELLGSGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 209 LERSVVFMNLADDPAVERTITPRLALTTAEYLAFeKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQ 288
Cdd:pfam00006 68 LKRTVVVVATSDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491102979 289 LYERAGRIEGREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLS 354
Cdd:pfam00006 147 LLERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
6-433 |
1.48e-63 |
|
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: 211.81 E-value: 1.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 6 TITEISGPLVFVE-TDEPVGydDIVEIELSDGETRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLL 84
Cdd:COG1157 22 RVTRVVGLLIEAVgPDASIG--ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 85 GRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASG-----LphndLA 159
Cdd:COG1157 100 GRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstL----LG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 160 lQIAR--QATVpeeedgeddegsefaVIFGAMGitaE---EANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLAL 234
Cdd:COG1157 176 -MIARntEADV---------------NVIALIG---ErgrEVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTAT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 235 TTAEYlaF-EKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRieGREGSVTQlpILT--M 311
Cdd:COG1157 237 AIAEY--FrDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITA--FYTvlV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 312 PGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDgigegLTRADH----ADVKdQIFAAYAEGEDL 387
Cdd:COG1157 311 EGDDMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPD-----IVSPEHralaRRLR-RLLARYEENEDL 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 491102979 388 RDlvniVGreALSELDNKYLDFA-DRFE--EEFVDQGTDTARSIDETLE 433
Cdd:COG1157 385 IR----IG--AYQPGSDPELDEAiALIPaiEAFLRQGMDERVSFEESLA 427
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
78-356 |
6.08e-56 |
|
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: 187.00 E-value: 6.08e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 78 PVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHND 157
Cdd:cd01136 3 PVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 158 LALQIARQATVPEeedgeddegsefaVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTA 237
Cdd:cd01136 83 LLGMIARNTDADV-------------NVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 238 EYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRieGREGSVTQLPILTMPGDDDT 317
Cdd:cd01136 150 EYFR-DQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVLVEGDDFN 226
|
250 260 270
....*....|....*....|....*....|....*....
gi 491102979 318 HPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRL 356
Cdd:cd01136 227 DPIADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
4-363 |
7.01e-49 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 172.95 E-value: 7.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 4 YQTITEISGPLVFVETDEP-VGydDIVEIELSD-GETRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTE 81
Cdd:PRK08472 19 FGSITKISPTIIEADGLNPsVG--DIVKIESSDnGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 82 DLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQ 161
Cdd:PRK08472 97 NLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 162 IARQATVPeeedgeddeGSEFAVIfgamGITAEEANEFMdDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLA 241
Cdd:PRK08472 177 IVKGCLAP---------IKVVALI----GERGREIPEFI-EKNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 242 fEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGReGSVTQLPILTMPGDDDTHPIP 321
Cdd:PRK08472 243 -NQGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLVEGDDMSDPIA 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 491102979 322 DLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGE 363
Cdd:PRK08472 321 DQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDIISP 362
|
|
| 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 ... |
364-458 |
4.26e-48 |
|
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: 160.29 E-value: 4.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 364 GLTRADHADVKDQIFAAYAEGEDLRDLVNIVGREALSELDNKYLDFADRFEEEFVDQGTDTARSIDETLELGWDLLSMLP 443
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 491102979 444 KDALNRIDEDLIEEH 458
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
60-387 |
3.15e-46 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 166.08 E-value: 3.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 60 EGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTL 139
Cdd:PRK06936 80 YGISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 140 VRGQKLPIFSASGLPHNDLALQIARQATVPeeedgeddegsefAVIFGAMGITAEEANEFMD-DFERTGaLERSVVFMNL 218
Cdd:PRK06936 160 GEGQRMGIFAAAGGGKSTLLASLIRSAEVD-------------VTVLALIGERGREVREFIEsDLGEEG-LRKAVLVVAT 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 219 ADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGriEG 298
Cdd:PRK06936 226 SDRPSMERAKAGFVATSIAEYFR-DQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QS 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 299 REGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIG-EGLTRADHAdvkDQI 377
Cdd:PRK06936 303 DKGSITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQIVSkEHKTWAGRL---REL 379
|
330
....*....|
gi 491102979 378 FAAYAEGEDL 387
Cdd:PRK06936 380 LAKYEEVELL 389
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
57-434 |
9.57e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 159.48 E-value: 9.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 57 EGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGM 136
Cdd:PRK08972 77 EELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAM 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 137 NTLVRGQKLPIFSASGLPHNDLALQIARQATVPeeedgeddegsefAVIFGAMGITAEEANEFMDDFERTGALERSVVFM 216
Cdd:PRK08972 157 LTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD-------------VIVVGLVGERGREVKEFIEEILGEEGRARSVVVA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 217 NLADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRI 296
Cdd:PRK08972 224 APADTSPLMRLKGCETATTIAEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNG 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 297 EGREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEgltraDHADVKDQ 376
Cdd:PRK08972 303 GPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVMPMVISE-----EHLEAMRR 377
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491102979 377 IFAAYAEGEDLRDLVNIvgrEALSELDNKYLDFADRFE---EEFVDQGTDTARSIDETLEL 434
Cdd:PRK08972 378 VKQVYSLYQQNRDLISI---GAYKQGSDPRIDNAIRLQpamNAFLQQTMKEAVPYDMSVNM 435
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
7-434 |
3.95e-43 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 157.62 E-value: 3.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 7 ITEISGPLVFVETDEpVGYDDIVEIELSDGE-TRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLG 85
Cdd:PRK09099 28 VVEVIGTLLRVSGLD-VTLGELCELRQRDGTlLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPALLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 86 RVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQIARQ 165
Cdd:PRK09099 107 RVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFARG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 166 ATVPEEedgeddegsefavIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLAfEKD 245
Cdd:PRK09099 187 TQCDVN-------------VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFR-DRG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 246 YHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRieGREGSVTQLpiLTMPGDDDT--HPIPDL 323
Cdd:PRK09099 253 LRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSITAL--YTVLAEDESgsDPIAEE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 324 TGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEGLTRAdhADVKDQIFAAYAEGEDL------RDLVNIVGRE 397
Cdd:PRK09099 329 VRGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQVVPREHVQA--AGRLRQLLAKHREVETLlqvgeyRAGSDPVADE 406
|
410 420 430
....*....|....*....|....*....|....*..
gi 491102979 398 ALSELDNKyldfadrfeEEFVDQGTDTARSIDETLEL 434
Cdd:PRK09099 407 AIAKIDAI---------RDFLSQRTDEYSDPDATLAA 434
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
60-387 |
2.33e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 156.04 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 60 EGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTL 139
Cdd:PRK05688 86 AGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTV 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 140 VRGQKLPIFSASGLPHNDLALQIARQATVPEeedgeddegsefaVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLA 219
Cdd:PRK05688 166 GRGQRLGLFAGTGVGKSVLLGMMTRFTEADI-------------IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 220 DDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGR 299
Cdd:PRK05688 233 DDAPLMRLRAAMYCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 300 EGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIG-EGLTRADHAdvkDQIF 378
Cdd:PRK05688 312 GGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVMPQVVDpEHLRRAQRF---KQLW 388
|
....*....
gi 491102979 379 AAYAEGEDL 387
Cdd:PRK05688 389 SRYQQSRDL 397
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
27-440 |
2.38e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 152.95 E-value: 2.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 27 DIVEIELSDGETR--RGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDG-----GP 99
Cdd:PRK07721 41 DVCYIHTKGGGDKaiKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGKPLEVKVGSGLIGQVLDALGEPLDGsalpkGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 100 EIVPDERrdivgEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQIARQATVpeeedgeddeg 179
Cdd:PRK07721 121 APVSTDQ-----DPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGSGVGKSTLMGMIARNTSA----------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 180 sEFAVIfGAMGITAEEANEFMD-DFERTGaLERSVVFMNLADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNY 258
Cdd:PRK07721 185 -DLNVI-ALIGERGREVREFIErDLGPEG-LKRSIVVVATSDQPALMRIKGAYTATAIAEYFR-DQGLNVMLMMDSVTRV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 259 CEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEgrEGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDL 338
Cdd:PRK07721 261 AMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSITAFYTVLVDGDDMNEPIADTVRGILDGHFVLDRQL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 339 NSQGIQPPINVLPSLSRLMDDgigegLTRADHADVKD---QIFAAYAEGEdlrDLVNIvgrEALSELDNKYLDFADRFEE 415
Cdd:PRK07721 339 ANKGQYPAINVLKSVSRVMNH-----IVSPEHKEAANrfrELLSTYQNSE---DLINI---GAYKRGSSREIDEAIQFYP 407
|
410 420
....*....|....*....|....*...
gi 491102979 416 ---EFVDQGTDTARSIDETLELGWDLLS 440
Cdd:PRK07721 408 qiiSFLKQGTDEKATFEESIQALLSLFG 435
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
40-440 |
5.71e-41 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 151.89 E-value: 5.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 40 RGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPeIVPDERRDIVGEAINPFSR 119
Cdd:PRK06820 62 LAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGP-PLTGQWRELDCPPPSPLTR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 120 EYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQIAR--QATVpeeedgeddegsefaVIFGAMGITAEEAN 197
Cdd:PRK06820 141 QPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCAdsAADV---------------MVLALIGERGREVR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 198 EFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRG 277
Cdd:PRK06820 206 EFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 278 YPGYMYTDLAQLYERAGRIEgrEGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLM 357
Cdd:PRK06820 285 FPPSVFANLPRLLERTGNSD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 358 DDGIGEGltRADHADVKDQIFAAYAEGEdlrdLVNIVGrEALSELDNKYLDFADRFE--EEFVDQGTDTARSIDETLELG 435
Cdd:PRK06820 363 PQIVSAG--QLAMAQKLRRMLACYQEIE----LLVRVG-EYQAGEDLQADEALQRYPaiCAFLQQDHSETAHLETTLEHL 435
|
....*
gi 491102979 436 WDLLS 440
Cdd:PRK06820 436 AQVVG 440
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
9-431 |
8.87e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 151.29 E-value: 8.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 9 EISGPLVFVEtdepVGydDIVEIELSDGETRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGRVM 88
Cdd:PRK08927 30 EVAGPIHALS----VG--ARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 89 DGTGQPIDG-GPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQIARQAT 167
Cdd:PRK08927 104 NALGEPIDGkGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 168 VpeeedgeddegsEFAVIfGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLAfEKDYH 247
Cdd:PRK08927 184 A------------DVSVI-GLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR-DQGKD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 248 VLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPGDDDTHPIPDLTGYI 327
Cdd:PRK08927 250 VLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDGDDHNEPVADAVRGI 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 328 TEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEgltrADHADVKD--QIFAAYAegeDLRDLVNIVGREALSeldNK 405
Cdd:PRK08927 330 LDGHIVMERAIAERGRYPAINVLKSVSRTMPGCNDP----EENPLVRRarQLMATYA---DMEELIRLGAYRAGS---DP 399
|
410 420
....*....|....*....|....*....
gi 491102979 406 YLDFADRFE---EEFVDQGTDTARSIDET 431
Cdd:PRK08927 400 EVDEAIRLNpalEAFLRQGKDEATSLAEG 428
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
27-388 |
2.16e-38 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 145.14 E-value: 2.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 27 DIVEIElSDGETRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGeTMKMPVTEDLLGRVMDGTGQPIDGGPEIVP-DE 105
Cdd:PRK06002 51 DFVAIR-ADGGTHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLAPgTR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 106 RRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQIARQAtvpeeedgeddegsEF-AV 184
Cdd:PRK06002 129 PMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARAD--------------AFdTV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 185 IFGAMGITAEEANEFMDDFERtGALERSVVFMNLADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNYCEALRE 264
Cdd:PRK06002 195 VIALVGERGREVREFLEDTLA-DNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFR-DRGENVLLIVDSVTRFAHAARE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 265 IGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQ 344
Cdd:PRK06002 273 VALAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRY 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 491102979 345 PPINVLPSLSRLmddgigegltrADHADVKDQ---------IFAAYAEGEDLR 388
Cdd:PRK06002 353 PAVDPLASISRL-----------ARHAWTPEQrklvsrlksMIARFEETRDLR 394
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
31-355 |
1.41e-37 |
|
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: 143.68 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 31 IELSDGetRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIv 110
Cdd:TIGR00962 52 IEFEGG--VQGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEFSPV- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 111 gEAINP--FSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQI---ARQATVpeeedgeddegsefAVI 185
Cdd:TIGR00962 129 -EKIAPgvIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTiinQKDSDV--------------YCI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 186 FGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLAFEKDyHVLVILTDMTNYCEALREI 265
Cdd:TIGR00962 194 YVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYFRDNGK-HALIIYDDLSKQAVAYRQI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 266 GAAREEVPGRRGYPGYMYTDLAQLYERAGRI--EGREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGI 343
Cdd:TIGR00962 273 SLLLRRPPGREAFPGDVFYLHSRLLERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGI 352
|
330
....*....|..
gi 491102979 344 QPPINVLPSLSR 355
Cdd:TIGR00962 353 RPAINVGLSVSR 364
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
31-393 |
9.79e-37 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 140.69 E-value: 9.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 31 IELSDGetrrGQVLESASDYVAI---QVF----EGTEGI-------DRDASVRFLGETMKMPVTEDLLGRVMDGTGQPID 96
Cdd:PRK07960 54 IERQNG----SETHEVESEVVGFngqRLFlmplEEVEGIlpgarvyARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 97 GGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQIAR--QATVpeeedg 174
Cdd:PRK07960 130 GLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARytQADV------ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 175 eddegsefaVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADdpavertITPRLALTTAEYLA-FEKDY-----HV 248
Cdd:PRK07960 204 ---------IVVGLIGERGREVKDFIENILGAEGRARSVVIAAPAD-------VSPLLRMQGAAYATrIAEDFrdrgqHV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 249 LVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQLPILTMPGDDDTHPIPDLTGYIT 328
Cdd:PRK07960 268 LLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAIL 347
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491102979 329 EGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEgltrADHADVKD--QIFAAYAEGedlRDLVNI 393
Cdd:PRK07960 348 DGHIVLSRRLAEAGHYPAIDIEASISRAMTALIDE----QHYARVRQfkQLLSSFQRN---RDLVSV 407
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
74-355 |
1.49e-36 |
|
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: 135.76 E-value: 1.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 74 TMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGL 153
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 154 PHNDLALQ-IARQAtvpeeedgeddeGSEFAVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRL 232
Cdd:cd01132 81 GKTAIAIDtIINQK------------GKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 233 ALTTAEYLAFEKDyHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRI--EGREGSVTQLPILT 310
Cdd:cd01132 149 GCAMGEYFRDNGK-HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLsdELGGGSLTALPIIE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 491102979 311 MPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSR 355
Cdd:cd01132 228 TQAGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
2-355 |
6.12e-36 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 138.89 E-value: 6.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 2 KEYQTITEISGPLVFVETDEPVGYDDIVEIElsdgETRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTE 81
Cdd:PRK13343 26 REIGRVESVGDGIAFVSGLPDAALDELLRFE----GGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 82 DLLGRVMDGTGQPIDGGPEIVPDERRDIvgEAINP--FSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLA 159
Cdd:PRK13343 102 GLLGRVIDPLGRPLDGGGPLQATARRPL--ERPAPaiIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 160 LQ-IARQATvpeeedgeddegSEFAVIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAE 238
Cdd:PRK13343 180 IDaIINQKD------------SDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 239 YLaFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRI--EGREGSVTQLPILTMPGDDD 316
Cdd:PRK13343 248 YF-RDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLspELGGGSLTALPIIETLAGEL 326
|
330 340 350
....*....|....*....|....*....|....*....
gi 491102979 317 THPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSR 355
Cdd:PRK13343 327 SAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
10-356 |
1.23e-34 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 133.97 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 10 ISGPLVFVETDEpVGYDDIVEIELSDGETR---RGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGR 86
Cdd:PRK08149 13 IQGPIIEAELPD-VAIGEICEIRAGWHSNEviaRAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 87 VMDGTGQ-------PIDGGPEIvpdERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLA 159
Cdd:PRK08149 92 VLDPTGKiverfdaPPTVGPIS---EERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 160 LQIARQATvpeeedgeddegsefAVIF--GAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTA 237
Cdd:PRK08149 169 NMLIEHSE---------------ADVFviGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 238 EYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIegREGSVTQLPILTMPGDDDT 317
Cdd:PRK08149 234 EYFR-DQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEP 310
|
330 340 350
....*....|....*....|....*....|....*....
gi 491102979 318 HPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRL 356
Cdd:PRK08149 311 DPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRV 349
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
56-434 |
2.38e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 130.87 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 56 FEGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDG 135
Cdd:PRK06793 70 FEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 136 MNTLVRGQKLPIFSASGLPHNDLALQIARQATVPEEedgeddegsefavIFGAMGITAEEANEFMDDFERTGALERSVVF 215
Cdd:PRK06793 150 MLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADIN-------------VISLVGERGREVKDFIRKELGEEGMRKSVVV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 216 MNLADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPgRRGYPGYMYTDLAQLYERAGR 295
Cdd:PRK06793 217 VATSDESHLMQLRAAKLATSIAEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELP-IGGKTLLMESYMKKLLERSGK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 296 IEgrEGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGIGEgltraDH---AD 372
Cdd:PRK06793 295 TQ--KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIMEEIVSP-----NHwqlAN 367
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491102979 373 VKDQIFAAYAEGEDLRDLVNIVGREalselDNKYLdFADR----FEEEFVDQGTDTARSIDETLEL 434
Cdd:PRK06793 368 EMRKILSIYKENELYFKLGTIQENA-----ENAYI-FECKnkveGINTFLKQGRSDSFQFDDIVEA 427
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
31-395 |
1.03e-32 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 128.86 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 31 IELSDGETRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIV 110
Cdd:PRK07196 44 IESVDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 111 GEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQIAR--QATVpeeedgeddegsefaVIFGA 188
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRytQADV---------------VVVGL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 189 MGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAA 268
Cdd:PRK07196 189 IGERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYR-DKGHDVLLLVDSLTRYAMAQREIALS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 269 REEVPGRRGYPGYMYTDLAQLYERAGRIEGrEGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPIN 348
Cdd:PRK07196 268 LGEPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAID 346
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 491102979 349 VLPSLSRLMDDGIGegltrADHADVKDQIFAAYAEGEDLRDLVNIVG 395
Cdd:PRK07196 347 ISQSISRCMSQVIG-----SQQAKAASLLKQCYADYMAIKPLIPLGG 388
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
67-355 |
1.36e-32 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 129.31 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 67 SVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLP 146
Cdd:CHL00059 66 SVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQREL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 147 IFSASGLPHNDLALQ-IARQATVpeeedgeddegsefAVI--FGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPA 223
Cdd:CHL00059 146 IIGDRQTGKTAVATDtILNQKGQ--------------NVIcvYVAIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 224 VERTITPRLALTTAEYLAFEKDyHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGR--EG 301
Cdd:CHL00059 212 TLQYLAPYTGAALAEYFMYRGR-HTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSSQlgEG 290
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 491102979 302 SVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSR 355
Cdd:CHL00059 291 SMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
42-363 |
6.00e-32 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 126.61 E-value: 6.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 42 QVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPeiVPDE-RRDIVGEAINPFSRE 120
Cdd:PRK07594 56 EVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRE--LPDVcWKDYDAMPPPAMVRQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 121 YPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLalqIARQATVPEEEDGeddegsefavIFGAMGITAEEANEFM 200
Cdd:PRK07594 134 PITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL---LAMLCNAPDADSN----------VLVLIGERGREVREFI 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 201 DDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG 280
Cdd:PRK07594 201 DFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 281 YMYTDLAQLYERAGRieGREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDG 360
Cdd:PRK07594 280 GVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVFPVV 357
|
...
gi 491102979 361 IGE 363
Cdd:PRK07594 358 TSH 360
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
77-433 |
6.50e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 123.86 E-value: 6.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 77 MPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHN 156
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 157 DLALQIAR--QATVPeeedgeddegsefavIFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLAL 234
Cdd:PRK05922 172 SLLSTIAKgsKSTIN---------------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAM 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 235 TTAEYLAfEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEgrEGSVTQL-PILTMPg 313
Cdd:PRK05922 237 TIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYP- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 314 dddTHP--IPDLTGYITEGQIYidrdLNSQG---IQPPINVLPSLSRlmddgIGEGLTRADHadvkdqifaaYAEGEDLR 388
Cdd:PRK05922 313 ---NHPdiFTDYLKSLLDGHFF----LTPQGkalASPPIDILTSLSR-----SARQLALPHH----------YAAAEELR 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 491102979 389 DL-------VNIVGREALSELDNKYLDFADRFE---EEFVDQGTDTARSIDETLE 433
Cdd:PRK05922 371 SLlkayheaLDIIQLGAYVPGQDAHLDRAVKLLpsiKQFLSQPLSSYCALHNTLK 425
|
|
| 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 ... |
3-73 |
1.94e-30 |
|
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: 112.52 E-value: 1.94e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491102979 3 EYQTITEISGPLVFVETDEPVGYDDIVEIELSDGETRRGQVLESASDYVAIQVFEGTEGIDRD-ASVRFLGE 73
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKgTKVRFTGE 72
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
7-452 |
3.07e-28 |
|
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: 116.74 E-value: 3.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 7 ITEISGPLVFVETDE---PVGYDDIvEIELSDGETrrgQVLESAS----DYVAIQVFEGTEGIDRDASVRFLGETMKMPV 79
Cdd:TIGR01039 5 VVQVIGPVVDVEFEQgelPRIYNAL-KVQNRAESE---LTLEVAQhlgdDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 80 TEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASG------- 152
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGvgktvli 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 153 --LPHNdlalqIARQatvpeeedgeddeGSEFAViFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITP 230
Cdd:TIGR01039 161 qeLINN-----IAKE-------------HGGYSV-FAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 231 RLALTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIegREGSVTQLPILT 310
Cdd:TIGR01039 222 LTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITST--KTGSITSVQAVY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 311 MPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMDDGI-GEgltraDHADVKDQIFAAYAEGEDLRD 389
Cdd:TIGR01039 300 VPADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVvGE-----EHYDVARGVQQILQRYKELQD 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 390 LVNIVGREALSELDNKYLDFADRFE----------EEFVDQG------TDTARSIDETLELGWDllsMLPKDA---LNRI 450
Cdd:TIGR01039 375 IIAILGMDELSEEDKLTVERARRIQrflsqpffvaEVFTGQPgkyvplKDTIRGFKEILEGKYD---HLPEQAfymVGTI 451
|
..
gi 491102979 451 DE 452
Cdd:TIGR01039 452 EE 453
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
6-355 |
3.81e-25 |
|
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: 107.82 E-value: 3.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 6 TITEISGPLVFVETDEPVGYDDIVEIElsDGetRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLG 85
Cdd:COG0056 30 TVLSVGDGIARVYGLPNAMAGELLEFP--GG--VYGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 86 RVMDGTGQPIDGGPEIVPDERRDIvgEAINP--FSREYPEEFIQTGVSAIDGMNTLVRGQK-LPIfsasGlphnDlalqi 162
Cdd:COG0056 106 RVVDPLGRPIDGKGPIEAEERRPV--ERPAPgvIDRQPVHEPLQTGIKAIDAMIPIGRGQReLII----G----D----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 163 aRQ---ATVpeeedgeddegsefAV-------------IFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVER 226
Cdd:COG0056 171 -RQtgkTAI--------------AIdtiinqkgkdvicIYVAIGQKASTVAQVVETLEEHGAMEYTIVVAATASDPAPLQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 227 TITPRLALTTAEYlaF-EKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG---YMYtdlAQLYERAGRI--EGRE 300
Cdd:COG0056 236 YIAPYAGCAMGEY--FmDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLH---SRLLERAAKLsdELGG 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491102979 301 GSVTQLPIL-TMPGdddthpipDLTGY-------ITEGQIYIDRDLNSQGIQPPINVLPSLSR 355
Cdd:COG0056 311 GSLTALPIIeTQAG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
31-355 |
6.00e-24 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 104.38 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 31 IELSDGetRRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIv 110
Cdd:PRK09281 53 LEFPGG--VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETRPV- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 111 gEAINP--FSREYPEEFIQTGVSAIDGMNTLVRGQK-LPIfsasGlphnDlalqiaRQ---ATVpeeedgeddegsefAV 184
Cdd:PRK09281 130 -ERKAPgvIDRKSVHEPLQTGIKAIDAMIPIGRGQReLII----G----D------RQtgkTAI--------------AI 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 185 -------------IFGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYlaF-EKDYHVLV 250
Cdd:PRK09281 181 dtiinqkgkdvicIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEY--FmDNGKDALI 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 251 ILTDMTNYCEALREIGAAREEVPGRRGYPG---YMYtdlAQLYERAGRI--EGREGSVTQLPIL-TMPGDddthpipdLT 324
Cdd:PRK09281 259 VYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLH---SRLLERAAKLsdELGGGSLTALPIIeTQAGD--------VS 327
|
330 340 350
....*....|....*....|....*....|....*...
gi 491102979 325 GY-------ITEGQIYIDRDLNSQGIQPPINVLPSLSR 355
Cdd:PRK09281 328 AYiptnvisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
184-420 |
5.45e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 96.63 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 184 VIFGAMGITAEEANEFMDDFER-----TGA--LERSVVFMNLADDPAVERTITPRLALTTAEYLAfEKDYHVLVILTDMT 256
Cdd:PRK14698 685 VIYIGCGERGNEMTDVLEEFPKlkdpkTGKplMERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 257 NYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRI-----EGREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQ 331
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVF 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 332 IYIDRDLNSQGIQPPINVLPSLSrLMDDGIGEGLTR---ADHADVKDQIFAAYAEGEDLRDLVNIVGREALSELDNKYLD 408
Cdd:PRK14698 844 WALDADLARRRHFPAINWLTSYS-LYVDAVKDWWHKnvdPEWKAMRDKAMELLQKEAELQEIVRIVGPDALPERERAILL 922
|
250
....*....|..
gi 491102979 409 FADRFEEEFVDQ 420
Cdd:PRK14698 923 VARMLREDYLQQ 934
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
6-403 |
1.56e-20 |
|
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: 94.00 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 6 TITEISGPLVFVETDE---PVGYDdIVEIELSDGETRrgqVLEsasdyVAIQVFEG---------TEGIDRDASVRFLGE 73
Cdd:COG0055 7 KIVQVIGPVVDVEFPEgelPAIYN-ALEVENEGGGEL---VLE-----VAQHLGDNtvrciamdsTDGLVRGMEVIDTGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 74 TMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAiNPFSREYPE-EFIQTGVSAIDGMNTLVRGQKLPIFSASG 152
Cdd:COG0055 78 PISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPA-PPFEEQSTKtEILETGIKVIDLLAPYAKGGKIGLFGGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 153 ---------LPHNdlalqIARQatvpeeedgeddeGSEFAViFGAMGITAEEANEFMDDFERTGALERSV-VF--MNlad 220
Cdd:COG0055 157 vgktvlimeLIHN-----IAKE-------------HGGVSV-FAGVGERTREGNDLYREMKESGVLDKTAlVFgqMN--- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 221 DPAVERTITPRLALTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYEragRI-EGR 299
Cdd:COG0055 215 EPPGARLRVALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQE---RItSTK 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 300 EGSVTQLPILTMPGDDDTHPIP-------DLTgyitegqIYIDRDLNSQGIQPPINVLPSLSRLMDDGI-GEgltraDHA 371
Cdd:COG0055 292 KGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvGE-----EHY 359
|
410 420 430
....*....|....*....|....*....|..
gi 491102979 372 DVKDQIFAAYAEGEDLRDLVNIVGREALSELD 403
Cdd:COG0055 360 RVAREVQRILQRYKELQDIIAILGMDELSEED 391
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
76-358 |
1.28e-18 |
|
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: 85.73 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 76 KMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRDIVGEAiNPFSREYPE-EFIQTGVSAIDGMNTLVRGQKLPIFSASG-- 152
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREA-PEFVELSTEqEILETGIKVVDLLAPYAKGGKIGLFGGAGvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 153 -------LPHNdlalqIARQATVpeeedgeddegseFAViFGAMGITAEEANEFMDDFERTGALER------SVVF--MN 217
Cdd:cd01133 80 ktvlimeLINN-----IAKAHGG-------------YSV-FAGVGERTREGNDLYHEMKESGVINLdglskvALVYgqMN 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 218 ladDPAVERTITPRLALTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIe 297
Cdd:cd01133 141 ---EPPGARARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST- 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491102979 298 gREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMD 358
Cdd:cd01133 217 -KKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILD 276
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
23-356 |
1.70e-18 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 88.17 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 23 VGYDDIVEIELSDGETRRGQVLESASD-YVAIQVFEGTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGpeI 101
Cdd:PTZ00185 62 VAYNTIIMIQVSPTTFAAGLVFNLEKDgRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVG--L 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 102 VPDERRDIVGE---------AINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNDLALqiarqATVPEEE 172
Cdd:PTZ00185 140 LTRSRALLESEqtlgkvdagAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAV-----STIINQV 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 173 DGEDDEGSEFAVI--FGAMGITAEEANEFMDDFERTGALERSVVFMNLADDPAVERTITPRLALTTAEYLaFEKDYHVLV 250
Cdd:PTZ00185 215 RINQQILSKNAVIsiYVSIGQRCSNVARIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYF-MNRGRHCLC 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 251 ILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREG--SVTQLPILTMPGDDDTHPIPDLTGYIT 328
Cdd:PTZ00185 294 VYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGggSVTALPIVETLSNDVTAYIVTNVISIT 373
|
330 340
....*....|....*....|....*...
gi 491102979 329 EGQIYIDRDLNSQGIQPPINVLPSLSRL 356
Cdd:PTZ00185 374 DGQIYLDTKLFTGGQRPAVNIGLSVSRV 401
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
83-320 |
6.98e-18 |
|
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: 83.78 E-value: 6.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 83 LLGRVMDGTGQPIdggpEIVPDERRDIVGEAIN----------PFSREY-PEEFIQTGVSAIDGMNTLVRGQKLPIFSAS 151
Cdd:cd01134 10 LLGSIFDGIQRPL----EVIAETGSIFIPRGVNvqrwpvrqprPVKEKLpPNVPLLTGQRVLDTLFPVAKGGTAAIPGPF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 152 GLPHNDLALQIARQATVPeeedgeddegsefAVIFGAMGITAEEANEFMDDF-----ERTGA--LERSVVFMNLADDPAV 224
Cdd:cd01134 86 GCGKTVISQSLSKWSNSD-------------VVIYVGCGERGNEMAEVLEEFpelkdPITGEslMERTVLIANTSNMPVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 225 ERTITPRLALTTAEYLafeKD--YHVLvILTDMTN-YCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIE---- 297
Cdd:cd01134 153 AREASIYTGITIAEYF---RDmgYNVS-LMADSTSrWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRclgs 228
|
250 260
....*....|....*....|....
gi 491102979 298 -GREGSVTQLPILTMPGDDDTHPI 320
Cdd:cd01134 229 pGREGSVTIVGAVSPPGGDFSEPV 252
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
80-355 |
3.95e-17 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 83.87 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 80 TEDLLGRVMDGTGQ---PIDGGPEIVPDERRD--IVGEAINPFSREYPEEFIQTGVSAIDGMNTLVRGQKLPIF--SASG 152
Cdd:PRK07165 76 SKEYFGKIIDIDGNiiyPEAQNPLSKKFLPNTssIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIgdRQTG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 153 LPHndLALQ-IARQATvpeeedgeddegSEFAVIFGAMGITAEEANEFMDDFERTGALERSVVfMNLADDPAVERTITPR 231
Cdd:PRK07165 156 KTH--IALNtIINQKN------------TNVKCIYVAIGQKRENLSRIYETLKEHDALKNTII-IDAPSTSPYEQYLAPY 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 232 LALTTAEYLAFEKDyhVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREgSVTQLPILTM 311
Cdd:PRK07165 221 VAMAHAENISYNDD--VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK-TITALPILQT 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 491102979 312 PGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSR 355
Cdd:PRK07165 298 VDNDITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
6-401 |
6.82e-16 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 80.21 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 6 TITEISGPLVFVETDEPVGYDDIVEIelsdGETR-RGQVLESASDYVAIQVFEGTEGIDRDASVRFLGEtmkmPVTEDL- 83
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRV----GEEGlIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGE----PLSVELg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 84 ---LGRVMDGTGQPID-----GGPEI--------VPDERR----------------DIVG-----EAIN-----PFSREY 121
Cdd:PRK04192 78 pglLGSIFDGIQRPLDelaekSGDFLergvyvpaLDREKKweftptvkvgdkveagDILGtvqetPSIEhkimvPPGVSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 122 -------------------------------------------------PEEFIQTGVSAIDGMNTLVRGQKLPI---Fs 149
Cdd:PRK04192 158 tvkeivsegdytvddtiavlededgegveltmmqkwpvrrprpykeklpPVEPLITGQRVIDTFFPVAKGGTAAIpgpF- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 150 ASG---LPHndlalQIARQATVPEeedgeddegsefaVIFGAMGitaEEANEFMDDFE--------RTGA--LERSVVFM 216
Cdd:PRK04192 237 GSGktvTQH-----QLAKWADADI-------------VIYVGCG---ERGNEMTEVLEefpelidpKTGRplMERTVLIA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 217 NLADDPAVERTITPRLALTTAEYLafeKD--YHVLvILTDMTN-YCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERA 293
Cdd:PRK04192 296 NTSNMPVAAREASIYTGITIAEYY---RDmgYDVL-LMADSTSrWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 294 GRIE---GREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSLSRLMD--DGIGEGLTRA 368
Cdd:PRK04192 372 GRVKtlgGEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDqvAPWWEENVDP 451
|
490 500 510
....*....|....*....|....*....|...
gi 491102979 369 DHADVKDQIFAAYAEGEDLRDLVNIVGREALSE 401
Cdd:PRK04192 452 DWRELRDEAMDLLQREAELQEIVRLVGPDALPE 484
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
7-72 |
5.25e-13 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 63.72 E-value: 5.25e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491102979 7 ITEISGPLVFVETDEPV--GYDDIVEIELSDGET-RRGQVLESASDYVAIQVFEGTEGIDRDASVRFLG 72
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRlpGLLNALEVELVEFGSlVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
370-436 |
5.27e-13 |
|
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: 64.00 E-value: 5.27e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491102979 370 HADVKDQIFAAYAEGEDLRDLVNIVGREALSELDNKYLDFADRFeEEFVDQGTDTARSIDETLELGW 436
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRL-EEFLQQGQFEPETIEDTLEKLY 66
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
58-403 |
3.43e-10 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 61.98 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 58 GTEGIDRDASVRFLGETMKMPVTEDLLGRVMDGTGQPIDGGPEIVPDERRdivgeainPFSREYPEeFIQ---------T 128
Cdd:CHL00060 77 ATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS--------PIHRSAPA-FIQldtklsifeT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 129 GVSAIDGMNTLVRGQKLPIFSASGLPHNDLALQ----IAR-QATVPeeedgeddegsefavIFGAMGITAEEANEFMDDF 203
Cdd:CHL00060 148 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMElinnIAKaHGGVS---------------VFGGVGERTREGNDLYMEM 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 204 ERTGALER--------SVVF--MNladDPAVERTITPRLALTTAEYLAFEKDYHVLVILTDMTNYCEALREIGAAREEVP 273
Cdd:CHL00060 213 KESGVINEqniaeskvALVYgqMN---EPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMP 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491102979 274 GRRGYPGYMYTDLAQLYERAGRIegREGSVTQLPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIQPPINVLPSL 353
Cdd:CHL00060 290 SAVGYQPTLSTEMGSLQERITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDST 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 491102979 354 SRLMDDGI-GEgltraDHAD----VKdQIFAAYAEgedLRDLVNIVGREALSELD 403
Cdd:CHL00060 368 STMLQPRIvGE-----EHYEtaqrVK-QTLQRYKE---LQDIIAILGLDELSEED 413
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
4-73 |
4.12e-09 |
|
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: 53.08 E-value: 4.12e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491102979 4 YQTITEISGPLVFVETDEPVGYDDIVEIELSDGET---RRGQVLESASDYVAIQVFEGTEGIDRDASVRFLGE 73
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGNNetvLKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
