|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
1-463 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 942.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 1 MKEYQTITEISGPLVFAEVDEPIGYDEIVEIETPQGETKRGQVLESSEGLVAIQVFEGTTGID-RNASVRFLGETLKMPV 79
Cdd:PRK04196 1 LKEYRTVSEIKGPLLFVEGVEGVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDlKDTKVRFTGEPLKLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 80 TEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLA 159
Cdd:PRK04196 81 SEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 160 LQIARQATVPEDEDSgeeseFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLA 239
Cdd:PRK04196 161 AQIARQAKVLGEEEN-----FAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 240 FDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDTHPIP 319
Cdd:PRK04196 236 FEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRIKGKKGSITQIPILTMPDDDITHPIP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 320 DLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDGIGEGLTREDHADVSDQMYAAYAEGEDLRDLVNIVGREALSE 399
Cdd:PRK04196 316 DLTGYITEGQIVLSRELHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHKDVANQLYAAYARGKDLRELAAIVGEEALSE 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756975214 400 RDNKYLDFAERFEAEFVNQGFDTDRSIEDTLDIGWDLLSMLPKSELNRIDEELIEDYYEEDAES 463
Cdd:PRK04196 396 RDRKYLKFADAFEREFVNQGFDENRSIEETLDLGWELLSILPESELKRIKDEYIEKYHPKYRGK 459
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
2-464 |
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: 916.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 2 KEYQTITEISGPLVFAEVDEPIGYDEIVEIETPQGETKRGQVLESSEGLVAIQVFEGTTGID-RNASVRFLGETLKMPVT 80
Cdd:COG1156 4 KEYRTISEIAGPLLFVEGVEGVGYGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSlKNTKVRFLGEPLELPVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 81 EDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLAL 160
Cdd:COG1156 84 EDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 161 QIARQATVPEDEDSgeeseFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAF 240
Cdd:COG1156 164 QIARQAKVRGEEEK-----FAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEYLAF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 241 DKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDTHPIPD 320
Cdd:COG1156 239 EKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERAGRIKGRKGSITQIPILTMPNDDITHPIPD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 321 LTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDGIGEGLTREDHADVSDQMYAAYAEGEDLRDLVNIVGREALSER 400
Cdd:COG1156 319 LTGYITEGQIVLSRDLHRKGIYPPIDVLPSLSRLMKDGIGEGKTREDHADVANQLYAAYARGQEVRELAAIVGEEALSET 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756975214 401 DNKYLDFAERFEAEFVNQGFDTDRSIEDTLDIGWDLLSMLPKSELNRIDEELIEDYYEEDAESV 464
Cdd:COG1156 399 DKKYLKFADAFERRFVNQGFDENRSIEETLDLGWELLSILPREELKRIDDEYIEKYYPKKRAKE 462
|
|
| ATP_syn_B_arch |
TIGR01041 |
ATP synthase archaeal, B subunit; Archaeal ATP synthase shares extensive sequence similarity ... |
3-464 |
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: 864.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 3 EYQTITEISGPLVFAEVDEPIGYDEIVEIETPQGETKRGQVLESSEGLVAIQVFEGTTGIDRNAS-VRFLGETLKMPVTE 81
Cdd:TIGR01041 1 EYSTITEIAGPLVFVEGVEPVAYNEIVEIETPDGEKRRGQVLDSSEGIAVVQVFEGTTGLDPTGTkVRFTGETLKLPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 82 DLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQ 161
Cdd:TIGR01041 81 DMLGRILNGSGEPIDGGPEIVPDERRDINGAPINPYAREYPEEFIQTGISAIDGMNTLVRGQKLPIFSGSGLPHNELAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 162 IARQATVPEDEDSgeeseFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAFD 241
Cdd:TIGR01041 161 IARQATVRGEESE-----FAVVFAAMGITYEEANFFMKDFEETGALERAVVFLNLADDPAVERIVTPRMALTAAEYLAFE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 242 KDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDTHPIPDL 321
Cdd:TIGR01041 236 KDMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGRVKGKKGSITQMPILTMPGDDITHPIPDL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 322 TGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDGIGEGLTREDHADVSDQMYAAYAEGEDLRDLVNIVGREALSERD 401
Cdd:TIGR01041 316 TGYITEGQIVLSRELHRKGIYPPINVLPSLSRLMKDGIGEGKTREDHKDVSDQLYAAYAEGRDLRGLVAIVGEEALSERD 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 756975214 402 NKYLDFAERFEAEFVNQGFDTDRSIEDTLDIGWDLLSMLPKSELNRIDEELIEDYYEEDAESV 464
Cdd:TIGR01041 396 RKYLKFADLFERKFVRQGFNENRSIEETLDIGWELLSILPESELKRIDEEYIEKYHPKYRKKK 458
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
3-461 |
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: 640.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 3 EYQTITEISGPLVFAEVDEPIGYDEIVEIETPQGETKRGQVLESSEGLVAIQVFEGTTGID-RNASVRFLGETLKMPVTE 81
Cdd:TIGR01040 1 EYRTVSGVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIDaKKTTCEFTGDILRTPVSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 82 DLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQ 161
Cdd:TIGR01040 81 DMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 162 IARQATV----PEDEDSGEESEFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEY 237
Cdd:TIGR01040 161 ICRQAGLvklpTKDVHDGHEDNFAIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 238 LAFDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDTHP 317
Cdd:TIGR01040 241 LAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 318 IPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDGIGEGLTREDHADVSDQMYAAYAEGEDLRDLVNIVGREAL 397
Cdd:TIGR01040 321 IPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEEAL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756975214 398 SERDNKYLDFAERFEAEFVNQGFDTDRSIEDTLDIGWDLLSMLPKSELNRIDEELIEDYYEEDA 461
Cdd:TIGR01040 401 SSEDLLYLEFLDKFEKNFIAQGPYENRTIFESLDIAWQLLRIFPKEMLKRIPAKILEEFYPRKS 464
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
74-360 |
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 756975214 74 TLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGL 153
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 154 PHNNLALQIARQATVPEDEDSgeeseFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALT 233
Cdd:cd01135 81 PHNELAAQIARQAGVVGSEEN-----FAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 234 TAEYLAFDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDD 313
Cdd:cd01135 156 TAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEGRKGSITQIPILTMPNDD 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 756975214 314 DTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDGIG 360
Cdd:cd01135 236 ITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSRLMKSGIG 282
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
2-457 |
2.58e-137 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 402.10 E-value: 2.58e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 2 KEYQTITEISGPLVFAEVdEPIGYDEIVEIETPQGeTKRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTE 81
Cdd:PRK02118 3 KIYTKITDITGNVITVEA-EGVGYGELATVERKDG-SSLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 82 DLLGRVLDGSGQPIDGGPEIVpDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQ 161
Cdd:PRK02118 81 SLLGRRFNGSGKPIDGGPELE-GEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 162 IARQATVPEdedsgeesefaVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAFD 241
Cdd:PRK02118 160 IALQAEADI-----------IILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 242 KDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGrEGSVTQIPILTMPGDDDTHPIPDL 321
Cdd:PRK02118 229 GKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFED-GGSITIIAVTTMPGDDVTHPVPDN 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 322 TGYITEGQIYIDRDlnsqgirpPINPLPSLSRLMDDGIGEgLTREDHADVSDQM---YAAYAEGEDLRDLvnivGREaLS 398
Cdd:PRK02118 308 TGYITEGQFYLRRG--------RIDPFGSLSRLKQLVIGK-KTREDHGDLMNAMirlYADSREAKEKMAM----GFK-LS 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 756975214 399 ERDNKYLDFAERFEAEFVNqgFDTDRSIEDTLDIGWDLLSMLPKSELNRIDEELIEDYY 457
Cdd:PRK02118 374 NWDEKLLKFSELFESRLMD--LEVNIPLEEALDLGWKILAQCFHPEEVGIKEQLIDKYW 430
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
76-354 |
6.25e-117 |
|
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: 343.67 E-value: 6.25e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 76 KMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPH 155
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 156 NNLALQIARQATvpededsgEESEFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTA 235
Cdd:cd19476 81 TVLAMQLARNQA--------KAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 236 EYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDT 315
Cdd:cd19476 153 EYFR-DNGQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVKDGGGSITAIPAVSTPGDDLT 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 756975214 316 HPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRL 354
Cdd:cd19476 232 DPIPDNTFAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
129-352 |
8.13e-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: 325.85 E-value: 8.13e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 129 GVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQIARQATVPededsgeesefAVVFGAMGITQEEANEFMEDFERTGALE 208
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASAD-----------VVVYALIGERGREVREFIEELLGSGALK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 209 RSVVFTNLADDPAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLY 288
Cdd:pfam00006 70 RTVVVVATSDEPPLARYRAPYTALTIAEYFR-DQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 756975214 289 ERAGRIEGREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLS 352
Cdd:pfam00006 149 ERAGRVKGKGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
6-431 |
5.52e-68 |
|
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: 223.37 E-value: 5.52e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 6 TITEISGPLVFAE-VDEPIGydEIVEIETPQGETKRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLL 84
Cdd:COG1157 22 RVTRVVGLLIEAVgPDASIG--ELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVPTGRPLSVPVGDGLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 85 GRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASG-----LphnnLA 159
Cdd:COG1157 100 GRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAGSGvgkstL----LG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 160 lQIAR--QATVpededsgeesefaVVFGAMGitqE---EANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTT 234
Cdd:COG1157 176 -MIARntEADV-------------NVIALIG---ErgrEVREFIEDDLGEEGLARSVVVVATSDEPPLMRLRAAYTATAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 235 AEYlaF-DKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRieGREGSVTQI-PILTmPGD 312
Cdd:COG1157 239 AEY--FrDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN--GGKGSITAFyTVLV-EGD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 313 DDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDgigegLTREDH-ADVSD--QMYAAYAEGEDLRDlv 389
Cdd:COG1157 314 DMNDPIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVMPD-----IVSPEHrALARRlrRLLARYEENEDLIR-- 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 756975214 390 niVGreALSERDNKYLDFA-ERFEA--EFVNQGFDTDRSIEDTLD 431
Cdd:COG1157 387 --IG--AYQPGSDPELDEAiALIPAieAFLRQGMDERVSFEESLA 427
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
78-354 |
3.38e-57 |
|
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: 190.08 E-value: 3.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 78 PVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNN 157
Cdd:cd01136 3 PVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKST 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 158 LALQIARQATVPEdedsgeesefaVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEY 237
Cdd:cd01136 83 LLGMIARNTDADV-----------NVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 238 LAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRieGREGSVTQIPILTMPGDDDTHP 317
Cdd:cd01136 152 FR-DQGKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN--GEKGSITAFYTVLVEGDDFNDP 228
|
250 260 270
....*....|....*....|....*....|....*..
gi 756975214 318 IPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRL 354
Cdd:cd01136 229 IADEVRSILDGHIVLSRRLAERGHYPAIDVLASISRV 265
|
|
| 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 ... |
362-456 |
1.13e-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: 179.94 E-value: 1.13e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 362 GLTREDHADVSDQMYAAYAEGEDLRDLVNIVGREALSERDNKYLDFAERFEAEFVNQGFDTDRSIEDTLDIGWDLLSMLP 441
Cdd:cd18112 1 GKTREDHRDVSNQLYAAYARGKDVRALAAIVGEEALSEEDRLYLEFADRFEREFINQGFYENRSIEETLDLGWELLSILP 80
|
90
....*....|....*
gi 756975214 442 KSELNRIDEELIEDY 456
Cdd:cd18112 81 KEELKRISEEYIDKY 95
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
4-432 |
1.54e-48 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 172.18 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 4 YQTITEISGPLVFAEVDEP-IGydEIVEIETPQ-GETKRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTE 81
Cdd:PRK08472 19 FGSITKISPTIIEADGLNPsVG--DIVKIESSDnGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 82 DLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQ 161
Cdd:PRK08472 97 NLLGRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGM 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 162 IARQATVPEDedsgeesefavVFGAMGITQEEANEFMEdFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAfD 241
Cdd:PRK08472 177 IVKGCLAPIK-----------VVALIGERGREIPEFIE-KNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK-N 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 242 KDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGReGSVTQIPILTMPGDDDTHPIPDL 321
Cdd:PRK08472 244 QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGK-GSITAFFTVLVEGDDMSDPIADQ 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 322 TGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDGIgeglTREDHADVSD--QMYA------------AYAEGEDlRD 387
Cdd:PRK08472 323 SRSILDGHIVLSRELTDFGIYPPINILNSASRVMNDII----SPEHKLAARKfkRLYSllkenevlirigAYQKGND-KE 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 756975214 388 LvnivgREALSERdnkylDFAERFEAEFVNQGFDTDRSIEDTLDI 432
Cdd:PRK08472 398 L-----DEAISKK-----EFMEQFLKQNPNELFPFEQTFEQLEEI 432
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
61-430 |
3.18e-48 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 171.47 E-value: 3.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 61 GIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLV 140
Cdd:PRK06936 81 GISSNTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCG 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 141 RGQKLPIFSASGLPHNNLALQIARQATVPededsgeesefAVVFGAMGITQEEANEFME-DFERTGaLERSVVFTNLADD 219
Cdd:PRK06936 161 EGQRMGIFAAAGGGKSTLLASLIRSAEVD-----------VTVLALIGERGREVREFIEsDLGEEG-LRKAVLVVATSDR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 220 PAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGriEGREG 299
Cdd:PRK06936 229 PSMERAKAGFVATSIAEYFR-DQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAG--QSDKG 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 300 SVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDgigegLTREDHADVSDQMYAAY 379
Cdd:PRK06936 306 SITALYTVLVEGDDMTEPVADETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMNQ-----IVSKEHKTWAGRLRELL 380
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 756975214 380 AEGEDLRDLVNIvgREALSERDNKYLDFAERFEA--EFVNQGFDTDRSIEDTL 430
Cdd:PRK06936 381 AKYEEVELLLQI--GEYQKGQDKEADQAIERIGAirGFLRQGTHELSHFNETL 431
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
22-391 |
6.89e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 167.95 E-value: 6.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 22 PIGydEIVEIETPQGETKrGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEI 101
Cdd:PRK08972 45 PVG--SLCSIETMAGELE-AEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 102 VPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQIARQATVPededsgeesefA 181
Cdd:PRK08972 122 YTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTAD-----------V 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 182 VVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALR 261
Cdd:PRK08972 191 IVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCETATTIAEYFR-DQGLNVLLLMDSLTRYAQAQR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 262 EIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGI 341
Cdd:PRK08972 270 EIALAVGEPPATKGYPPSVFAKLPALVERAGNGGPGQGSITAFYTVLTEGDDLQDPIADASRAILDGHIVLSRELADSGH 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 756975214 342 RPPINPLPSLSRLMddgigEGLTREDHADVS---DQMYAAYAEGedlRDLVNI 391
Cdd:PRK08972 350 YPAIDIEASISRVM-----PMVISEEHLEAMrrvKQVYSLYQQN---RDLISI 394
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
7-391 |
6.86e-46 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 165.33 E-value: 6.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 7 ITEISGPLV-FAEVDEPIGydEIVEIETPQGE-TKRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLL 84
Cdd:PRK09099 28 VVEVIGTLLrVSGLDVTLG--ELCELRQRDGTlLQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVGPALL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 85 GRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQIAR 164
Cdd:PRK09099 106 GRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMGMFAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 165 QATVPEDedsgeesefavVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAfDKDY 244
Cdd:PRK09099 186 GTQCDVN-----------VIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIERAKAAYVATAIAEYFR-DRGL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 245 HVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRieGREGSVTqiPILTMPGDDDT--HPIPDLT 322
Cdd:PRK09099 254 RVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGM--GETGSIT--ALYTVLAEDESgsDPIAEEV 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 756975214 323 GYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDgigegLTREDHADVSDQMYAAYAEGEDLRDLVNI 391
Cdd:PRK09099 330 RGILDGHMILSREIAARNQYPAIDVLGSLSRVMPQ-----VVPREHVQAAGRLRQLLAKHREVETLLQV 393
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
56-438 |
4.52e-43 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 157.67 E-value: 4.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 56 FEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPeIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDG 135
Cdd:PRK06820 78 FASSDGLRCGQWVTPLGHMHQVQVGADLAGRILDGLGAPIDGGP-PLTGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 136 MNTLVRGQKLPIFSASGLPHNNLALQIAR--QATVpededsgeesefaVVFGAMGITQEEANEFMEDFERTGALERSVVF 213
Cdd:PRK06820 157 ILSCGEGQRIGIFAAAGVGKSTLLGMLCAdsAADV-------------MVLALIGERGREVREFLEQVLTPEARARTVVV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 214 TNLADDPAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGR 293
Cdd:PRK06820 224 VATSDRPALERLKGLSTATTIAEYFR-DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGN 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 294 IEgrEGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDGIGEGltREDHADVSD 373
Cdd:PRK06820 303 SD--RGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIVLSRRLAGAGHYPAIDIAASVSRIMPQIVSAG--QLAMAQKLR 378
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756975214 374 QMYAAYAEGEdlrdLVNIVGrEALSERDNKYLDFAERFEA--EFVNQGFDTDRSIEDTLDIGWDLLS 438
Cdd:PRK06820 379 RMLACYQEIE----LLVRVG-EYQAGEDLQADEALQRYPAicAFLQQDHSETAHLETTLEHLAQVVG 440
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
61-421 |
6.76e-43 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 157.20 E-value: 6.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 61 GIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLV 140
Cdd:PRK05688 87 GIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 141 RGQKLPIFSASGLPHNNLALQIARQATVPEdedsgeesefaVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDP 220
Cdd:PRK05688 167 RGQRLGLFAGTGVGKSVLLGMMTRFTEADI-----------IVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPADDA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 221 AVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGS 300
Cdd:PRK05688 236 PLMRLRAAMYCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPGGGS 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 301 VTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMddgigEGLTREDH---ADVSDQMYA 377
Cdd:PRK05688 315 ITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-----PQVVDPEHlrrAQRFKQLWS 389
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 756975214 378 AYAEGedlRDLVNIVGREALSERDnkyLDFA-ERFE--AEFVNQGFD 421
Cdd:PRK05688 390 RYQQS---RDLISVGAYVAGGDPE---TDLAiARFPhlVQFLRQGLR 430
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
72-431 |
1.69e-42 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 156.04 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 72 GETLKMPVTEDLLGRVLDGSGQPIDG-----GPEIVPDERrdivgAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLP 146
Cdd:PRK07721 88 GKPLEVKVGSGLIGQVLDALGEPLDGsalpkGLAPVSTDQ-----DPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 147 IFSASGLPHNNLALQIARQATVPEDedsgeesefavVFGAMGITQEEANEFME-DFERTGaLERSVVFTNLADDPAVERT 225
Cdd:PRK07721 163 IFAGSGVGKSTLMGMIARNTSADLN-----------VIALIGERGREVREFIErDLGPEG-LKRSIVVVATSDQPALMRI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 226 VTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEgrEGSVTQIP 305
Cdd:PRK07721 231 KGAYTATAIAEYFR-DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNA--SGSITAFY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 306 ILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDgigegLTREDHADVSD---QMYAAYAEG 382
Cdd:PRK07721 308 TVLVDGDDMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVMNH-----IVSPEHKEAANrfrELLSTYQNS 382
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 756975214 383 EdlrDLVNIvgrEALSERDNKYLDFAERFEA---EFVNQGFDTDRSIEDTLD 431
Cdd:PRK07721 383 E---DLINI---GAYKRGSSREIDEAIQFYPqiiSFLKQGTDEKATFEESIQ 428
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
4-355 |
1.51e-41 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 153.60 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 4 YQTITEISGPLVfaEVDEPIGYDEI---VEIETPQGETKRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVT 80
Cdd:PRK08927 18 YGRVVAVRGLLV--EVAGPIHALSVgarIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 81 EDLLGRVLDGSGQPIDG-GPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLA 159
Cdd:PRK08927 96 RAWLGRVVNALGEPIDGkGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 160 LQIARQATVPededsgeesefAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLA 239
Cdd:PRK08927 176 SMLARNADAD-----------VSVIGLIGERGREVQEFLQDDLGPEGLARSVVVVATSDEPALMRRQAAYLTLAIAEYFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 240 fDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDTHPIP 319
Cdd:PRK08927 245 -DQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGEGTITGLFTVLVDGDDHNEPVA 323
|
330 340 350
....*....|....*....|....*....|....*.
gi 756975214 320 DLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLM 355
Cdd:PRK08927 324 DAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM 359
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
27-386 |
5.05e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 149.38 E-value: 5.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 27 EIVEIETpQGETKRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGeTLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDER 106
Cdd:PRK06002 51 DFVAIRA-DGGTHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLAPGTR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 107 RDIVGAAINP-YSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQIARQAtvpededsgeesEF-AVVF 184
Cdd:PRK06002 129 PMSIDATAPPaMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARAD------------AFdTVVI 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 185 GAMGITQEEANEFMEDFERtGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIG 264
Cdd:PRK06002 197 ALVGERGREVREFLEDTLA-DNLKKAVAVVATSDESPMMRRLAPLTATAIAEYFR-DRGENVLLIVDSVTRFAHAAREVA 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 265 AAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPP 344
Cdd:PRK06002 275 LAAGEPPVARGYPPSVFSELPRLLERAGPGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLDRAIAEQGRYPA 354
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 756975214 345 INPLPSLSRLMDdgigEGLTREDHADVSD--QMYAAYAEGEDLR 386
Cdd:PRK06002 355 VDPLASISRLAR----HAWTPEQRKLVSRlkSMIARFEETRDLR 394
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
44-391 |
4.10e-39 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 147.24 E-value: 4.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 44 LESSEGLVAiqvfeGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPE 123
Cdd:PRK07960 82 LEEVEGILP-----GARVYARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 124 EFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQIAR--QATVpededsgeesefaVVFGAMGITQEEANEFMEDF 201
Cdd:PRK07960 157 HVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMMARytQADV-------------IVVGLIGERGREVKDFIENI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 202 ERTGALERSVVFTNLADdpavertVTPRLALTTAEYLA------FDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRG 275
Cdd:PRK07960 224 LGAEGRARSVVIAAPAD-------VSPLLRMQGAAYATriaedfRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKG 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 276 YPGYMYTDLAQLYERAGRIEGREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLM 355
Cdd:PRK07960 297 YPPSVFAKLPALVERAGNGISGGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM 376
|
330 340 350
....*....|....*....|....*....|....*...
gi 756975214 356 DDGIGEgltrEDHADVSD--QMYAAYAEGedlRDLVNI 391
Cdd:PRK07960 377 TALIDE----QHYARVRQfkQLLSSFQRN---RDLVSV 407
|
|
| atpA |
TIGR00962 |
proton translocating ATP synthase, F1 alpha subunit; The sequences of ATP synthase F1 alpha ... |
27-353 |
3.95e-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: 142.53 E-value: 3.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 27 EIVEIETPQgetkRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDER 106
Cdd:TIGR00962 50 ELIEFEGGV----QGIALNLEEDSVGAVIMGDYSDIREGSTVKRTGRILEVPVGDGLLGRVVNALGEPIDGKGPIDSDEF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 107 RDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQI---ARQATVpededsgeesefAVV 183
Cdd:TIGR00962 126 SPVEKIAPGVIERKSVHEPLQTGIKAIDAMIPIGRGQRELIIGDRQTGKTAVAIDTiinQKDSDV------------YCI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 184 FGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLaFDKDYHVLVILTDMTNYCEALREI 263
Cdd:TIGR00962 194 YVAIGQKASTVAQVVRKLEEHGAMAYTIVVAATASDSASLQYLAPYTGCTMGEYF-RDNGKHALIIYDDLSKQAVAYRQI 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 264 GAAREEVPGRRGYPGYMYTDLAQLYERAGRI--EGREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGI 341
Cdd:TIGR00962 273 SLLLRRPPGREAFPGDVFYLHSRLLERAAKLndEKGGGSLTALPIIETQAGDVSAYIPTNVISITDGQIFLESDLFNSGI 352
|
330
....*....|..
gi 756975214 342 RPPINPLPSLSR 353
Cdd:TIGR00962 353 RPAINVGLSVSR 364
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
10-431 |
9.09e-37 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 140.13 E-value: 9.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 10 ISGPLVFAEVDE-PIGydEIVEIETPQGETK---RGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLLG 85
Cdd:PRK08149 13 IQGPIIEAELPDvAIG--EICEIRAGWHSNEviaRAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 86 RVLDGSGQ-------PIDGGPEIvpdERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNL 158
Cdd:PRK08149 91 AVLDPTGKiverfdaPPTVGPIS---EERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 159 ALQIARQATvpededsgeesefAVVF--GAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAE 236
Cdd:PRK08149 168 MNMLIEHSE-------------ADVFviGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 237 YLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIegREGSVTQIPILTMPGDDDTH 316
Cdd:PRK08149 235 YFR-DQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT--LAGSITAFYTVLLESEEEPD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 317 PIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDgigegLTREDHADVSDQMYAAYAEGEDLRDLVNIvG--R 394
Cdd:PRK08149 312 PIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFGQ-----VTDPKHRQLAAAFRKLLTRLEELQLFIDL-GeyR 385
|
410 420 430
....*....|....*....|....*....|....*..
gi 756975214 395 EALSERDNKYLDFAERFEAeFVNQGFDTDRSIEDTLD 431
Cdd:PRK08149 386 RGENADNDRAMDKRPALEA-FLKQDVAEKSSFSDTLE 421
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
74-353 |
7.27e-35 |
|
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: 131.14 E-value: 7.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 74 TLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGL 153
Cdd:cd01132 1 IVEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 154 PHNNLALQ-IARQAtvpededsgeESEFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLAL 232
Cdd:cd01132 81 GKTAIAIDtIINQK----------GKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGC 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 233 TTAEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRI--EGREGSVTQIPILTMP 310
Cdd:cd01132 151 AMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLsdELGGGSLTALPIIETQ 229
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 756975214 311 GDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSR 353
Cdd:cd01132 230 AGDVSAYIPTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
56-431 |
1.96e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 133.56 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 56 FEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDG 135
Cdd:PRK06793 70 FEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 136 MNTLVRGQKLPIFSASGLPHNNLALQIARQATVPEDedsgeesefavVFGAMGITQEEANEFMEDFERTGALERSVVFTN 215
Cdd:PRK06793 150 MLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADIN-----------VISLVGERGREVKDFIRKELGEEGMRKSVVVVA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 216 LADDPAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPgRRGYPGYMYTDLAQLYERAGRIE 295
Cdd:PRK06793 219 TSDESHLMQLRAAKLATSIAEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELP-IGGKTLLMESYMKKLLERSGKTQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 296 grEGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMddgigEGLTREDHADVSDQM 375
Cdd:PRK06793 297 --KGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIM-----EEIVSPNHWQLANEM 369
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 756975214 376 ---YAAYAEGEDLRDLVNIVGREalserDNKYLdFAERFEAEFVNQGFDTDRSIEDTLD 431
Cdd:PRK06793 370 rkiLSIYKENELYFKLGTIQENA-----ENAYI-FECKNKVEGINTFLKQGRSDSFQFD 422
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
2-353 |
3.68e-34 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 133.89 E-value: 3.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 2 KEYQTITEISGPLVFAEVDEPIGYDEIVEIEtpqgETKRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTE 81
Cdd:PRK13343 26 REIGRVESVGDGIAFVSGLPDAALDELLRFE----GGSRGFAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 82 DLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQ 161
Cdd:PRK13343 102 GLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAID 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 162 -IARQATvpededsgeeSEFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLaF 240
Cdd:PRK13343 182 aIINQKD----------SDVICVYVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAPFAGCAIAEYF-R 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 241 DKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRI--EGREGSVTQIPILTMPGDDDTHPI 318
Cdd:PRK13343 251 DQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKLspELGGGSLTALPIIETLAGELSAYI 330
|
330 340 350
....*....|....*....|....*....|....*
gi 756975214 319 PDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSR 353
Cdd:PRK13343 331 PTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
31-393 |
2.58e-33 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 130.40 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 31 IETPQGETKRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIV 110
Cdd:PRK07196 44 IESVDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLQQQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 111 GAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQIAR--QATVpededsgeesefaVVFGAMG 188
Cdd:PRK07196 124 LPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRytQADV-------------VVVGLIG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 189 ITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIGAARE 268
Cdd:PRK07196 191 ERGREVKEFIEHSLQAAGMAKSVVVAAPADESPLMRIKATELCHAIATYYR-DKGHDVLLLVDSLTRYAMAQREIALSLG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 269 EVPGRRGYPGYMYTDLAQLYERAGRIEGrEGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPL 348
Cdd:PRK07196 270 EPPATKGYPPSAFSIIPRLAESAGNSSG-NGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDIS 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 756975214 349 PSLSRLMDDGIGegltrEDHADVSDQMYAAYAEGEDLRDLVNIVG 393
Cdd:PRK07196 349 QSISRCMSQVIG-----SQQAKAASLLKQCYADYMAIKPLIPLGG 388
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
34-361 |
2.40e-31 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 125.07 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 34 PQGETKRGQVLESSEGLVAiqVFEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPeiVPDE-RRDIVGA 112
Cdd:PRK07594 50 PGEELAEVVGINGSKALLS--PFTSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLDGRE--LPDVcWKDYDAM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 113 AINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLalqIARQATVPEDEDSgeesefavVFGAMGITQE 192
Cdd:PRK07594 126 PPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTL---LAMLCNAPDADSN--------VLVLIGERGR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 193 EANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPG 272
Cdd:PRK07594 195 EVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRVVLLADSLTRYARAAREIALAAGETAV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 273 RRGYPGYMYTDLAQLYERAGRieGREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLS 352
Cdd:PRK07594 274 SGEYPPGVFSALPRLLERTGM--GEKGSITAFYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLS 351
|
....*....
gi 756975214 353 RLMDDGIGE 361
Cdd:PRK07594 352 RVFPVVTSH 360
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
41-353 |
3.25e-31 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 125.46 E-value: 3.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 41 GQVLESSEGLVAIQ----------VFEGT-TGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDI 109
Cdd:CHL00059 29 GELVEFEDGTIGIAlnlesnnvgvVLMGDgLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 110 VGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQ-IARQATVpededsgeesEFAVVFGAMG 188
Cdd:CHL00059 109 ESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTAVATDtILNQKGQ----------NVICVYVAIG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 189 ITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLAFdKDYHVLVILTDMTNYCEALREIGAARE 268
Cdd:CHL00059 179 QKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFMY-RGRHTLIIYDDLSKQAQAYRQMSLLLR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 269 EVPGRRGYPGYMYTDLAQLYERAGRIEGR--EGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPIN 346
Cdd:CHL00059 258 RPPGREAYPGDVFYLHSRLLERAAKLSSQlgEGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAIN 337
|
....*..
gi 756975214 347 PLPSLSR 353
Cdd:CHL00059 338 VGISVSR 344
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
7-420 |
5.47e-31 |
|
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: 124.45 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 7 ITEISGPLV---FAEVDEPIGYDEIvEIETPQGETkrgQVLESS----EGLVAIQVFEGTTGIDRNASVRFLGETLKMPV 79
Cdd:TIGR01039 5 VVQVIGPVVdveFEQGELPRIYNAL-KVQNRAESE---LTLEVAqhlgDDTVRTIAMGSTDGLVRGLEVIDTGAPISVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 80 TEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASG------- 152
Cdd:TIGR01039 81 GKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGvgktvli 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 153 --LPHNnlalqIARQatvpededsgeeSEFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRL 230
Cdd:TIGR01039 161 qeLINN-----IAKE------------HGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 231 ALTTAEYLAFDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIegREGSVTQIPILTMP 310
Cdd:TIGR01039 224 GLTMAEYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITST--KTGSITSVQAVYVP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 311 GDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMDDGIgeglTREDHADVSDQMYAAYAEGEDLRDLVN 390
Cdd:TIGR01039 302 ADDLTDPAPATTFAHLDATTVLSRKIAELGIYPAVDPLDSTSRLLDPSV----VGEEHYDVARGVQQILQRYKELQDIIA 377
|
410 420 430
....*....|....*....|....*....|
gi 756975214 391 IVGREALSERDNKYLDFAERFEaEFVNQGF 420
Cdd:TIGR01039 378 ILGMDELSEEDKLTVERARRIQ-RFLSQPF 406
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
77-431 |
8.91e-31 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 123.48 E-value: 8.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 77 MPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHN 156
Cdd:PRK05922 92 LHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKS 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 157 NLALQIAR--QATVPededsgeesefavVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTT 234
Cdd:PRK05922 172 SLLSTIAKgsKSTIN-------------VIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTI 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 235 AEYLAfDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEgrEGSVTQI-PILTMPgdd 313
Cdd:PRK05922 239 AEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNND--KGSITALyAILHYP--- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 314 dTHP--IPDLTGYITEGQIYidrdLNSQG---IRPPINPLPSLSRlmddgIGEGLTREDHadvsdqmyaaYAEGEDLRDL 388
Cdd:PRK05922 313 -NHPdiFTDYLKSLLDGHFF----LTPQGkalASPPIDILTSLSR-----SARQLALPHH----------YAAAEELRSL 372
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 756975214 389 -------VNIVGREALSERDNKYLDFAERFEA---EFVNQGFDTDRSIEDTLD 431
Cdd:PRK05922 373 lkayheaLDIIQLGAYVPGQDAHLDRAVKLLPsikQFLSQPLSSYCALHNTLK 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 |
1.37e-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: 110.21 E-value: 1.37e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 756975214 3 EYQTITEISGPLVFAEVDEPIGYDEIVEIETPQGETKRGQVLESSEGLVAIQVFEGTTGID-RNASVRFLGE 73
Cdd:cd18118 1 EYRTVSEINGPLVIVEGVKGVKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDlKGTKVRFTGE 72
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
24-353 |
9.55e-24 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 103.58 E-value: 9.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 24 GYDEIVEIETPQgetkRGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVP 103
Cdd:COG0056 48 MAGELLEFPGGV----YGMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 104 DERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQK---------------------------LPIFSASGlphn 156
Cdd:COG0056 124 EERRPVERPAPGVIDRQPVHEPLQTGIKAIDAMIPIGRGQReliigdrqtgktaiaidtiinqkgkdvICIYVAIG---- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 157 nlalQiaRQATVpededsgeesefavvfgamgitqeeANeFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAE 236
Cdd:COG0056 200 ----Q--KASTV-------------------------AQ-VVETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 237 YlaF-DKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPG---YMYtdlAQLYERAGRI--EGREGSVTQIPIL-TM 309
Cdd:COG0056 248 Y--FmDQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGdvfYLH---SRLLERAAKLsdELGGGSLTALPIIeTQ 322
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 756975214 310 PGdddthpipDLTGY-------ITEGQIYIDRDLNSQGIRPPINPLPSLSR 353
Cdd:COG0056 323 AG--------DVSAYiptnvisITDGQIFLESDLFNAGIRPAINVGLSVSR 365
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
182-421 |
7.25e-23 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 102.41 E-value: 7.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 182 VVFGAMGITQEEANEFMEDFER-----TGA--LERSVVFTNLADDPAVERTVTPRLALTTAEYLAfDKDYHVLVILTDMT 254
Cdd:PRK14698 685 VIYIGCGERGNEMTDVLEEFPKlkdpkTGKplMERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALMADSTS 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 255 NYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRI-----EGREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQ 329
Cdd:PRK14698 764 RWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAGRVvtlgsDYRVGSVSVIGAVSPPGGDFSEPVVQNTLRVVKVF 843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 330 IYIDRDLNSQGIRPPINPLPSLSRLMD---DGIGEGLTREDHADVSDQMYAAYAEGEdLRDLVNIVGREALSERDNKYLD 406
Cdd:PRK14698 844 WALDADLARRRHFPAINWLTSYSLYVDavkDWWHKNVDPEWKAMRDKAMELLQKEAE-LQEIVRIVGPDALPERERAILL 922
|
250
....*....|....*.
gi 756975214 407 FAERFEAEFVNQ-GFD 421
Cdd:PRK14698 923 VARMLREDYLQQdAFD 938
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
6-401 |
1.31e-22 |
|
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: 100.16 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 6 TITEISGPLV---FA-----------EVDEPIGYDEIVEIETPQGETK-RGQVLESSEGLVaiqvfegttgidRNASVRF 70
Cdd:COG0055 7 KIVQVIGPVVdveFPegelpaiynalEVENEGGGELVLEVAQHLGDNTvRCIAMDSTDGLV------------RGMEVID 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 71 LGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSA 150
Cdd:COG0055 75 TGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 151 SG---------LPHNnlalqIARQatvpededsgeeSEFAVVFGAMGITQEEANEFMEDFERTGALERSV-VFTNLADDP 220
Cdd:COG0055 155 AGvgktvlimeLIHN-----IAKE------------HGGVSVFAGVGERTREGNDLYREMKESGVLDKTAlVFGQMNEPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 221 AVertvtpRL-----ALTTAEYLAFDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYEragRI- 294
Cdd:COG0055 218 GA------RLrvaltALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQE---RIt 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 295 EGREGSVTQIPILTMPGDDDTHPIP-------DLTgyitegqIYIDRDLNSQGIRPPINPLPSLSRLMDDGI-GegltrE 366
Cdd:COG0055 289 STKKGSITSVQAVYVPADDLTDPAPattfahlDAT-------TVLSRKIAELGIYPAVDPLDSTSRILDPLIvG-----E 356
|
410 420 430
....*....|....*....|....*....|....*
gi 756975214 367 DHADVSDQMYAAYAEGEDLRDLVNIVGREALSERD 401
Cdd:COG0055 357 EHYRVAREVQRILQRYKELQDIIAILGMDELSEED 391
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
25-353 |
8.15e-22 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 97.83 E-value: 8.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 25 YDEIVEIEtpqGETKrGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPD 104
Cdd:PRK09281 49 AGELLEFP---GGVY-GIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEAT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 105 ERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKlpifsasglphnnlALQIA-RQ---ATVpededsgeesef 180
Cdd:PRK09281 125 ETRPVERKAPGVIDRKSVHEPLQTGIKAIDAMIPIGRGQR--------------ELIIGdRQtgkTAI------------ 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 181 AV-------------VFGAMGitQEEAN--EFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYlaF-DKDY 244
Cdd:PRK09281 179 AIdtiinqkgkdvicIYVAIG--QKASTvaQVVRKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEY--FmDNGK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 245 HVLVILTDMTNYCEALREIGAAREEVPGRRGYPG---YMYtdlAQLYERAGRI--EGREGSVTQIPIL-TMPGDddthpi 318
Cdd:PRK09281 255 DALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGdvfYLH---SRLLERAAKLsdELGGGSLTALPIIeTQAGD------ 325
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 756975214 319 pdLTGY-------ITEGQIYIDRDLNSQGIRPPINPLPSLSR 353
Cdd:PRK09281 326 --VSAYiptnvisITDGQIFLESDLFNAGIRPAINVGISVSR 365
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
6-401 |
2.98e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 96.77 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 6 TITEISGPLVFAEVDEPIGYDEIVEIetpqGETK-RGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLL 84
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYEVVRV----GEEGlIGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVELGPGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 85 GRVLDG-----------SG---------QPID------------------GG------------------P--------E 100
Cdd:PRK04192 82 GSIFDGiqrpldelaekSGdflergvyvPALDrekkweftptvkvgdkveAGdilgtvqetpsiehkimvPpgvsgtvkE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 101 IVPD----------ERRDIVGAAIN-------------PYS-REYPEEFIQTGVSAIDGMNTLVRGQKLPI---FsASG- 152
Cdd:PRK04192 162 IVSEgdytvddtiaVLEDEDGEGVEltmmqkwpvrrprPYKeKLPPVEPLITGQRVIDTFFPVAKGGTAAIpgpF-GSGk 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 153 --LPHnnlalQIARQATVPEdedsgeesefaVVFGAMGitqEEANEFMEDFE--------RTGA--LERSVVFTNLADDP 220
Cdd:PRK04192 241 tvTQH-----QLAKWADADI-----------VIYVGCG---ERGNEMTEVLEefpelidpKTGRplMERTVLIANTSNMP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 221 AVERTVTPRLALTTAEYlaF-DKDYHVLvILTDMTN-YCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIE--- 295
Cdd:PRK04192 302 VAAREASIYTGITIAEY--YrDMGYDVL-LMADSTSrWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERAGRVKtlg 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 296 GREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMD--DGIGEGLTREDHADVSD 373
Cdd:PRK04192 379 GEEGSVTIIGAVSPPGGDFSEPVTQNTLRIVKVFWALDAELADRRHFPAINWLTSYSLYLDqvAPWWEENVDPDWRELRD 458
|
490 500
....*....|....*....|....*...
gi 756975214 374 QMYAAYAEGEDLRDLVNIVGREALSERD 401
Cdd:PRK04192 459 EAMDLLQREAELQEIVRLVGPDALPEED 486
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
83-353 |
3.24e-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: 87.63 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 83 LLGRVLDGSGQPIdggpEIVPDERRDIVGAAIN----------PYSREY-PEEFIQTGVSAIDGMNTLVRGQKLPIFSAS 151
Cdd:cd01134 10 LLGSIFDGIQRPL----EVIAETGSIFIPRGVNvqrwpvrqprPVKEKLpPNVPLLTGQRVLDTLFPVAKGGTAAIPGPF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 152 GLPHNNLALQIARQATVPededsgeesefAVVFGAMGitqEEANEFME---DF-----ERTGA--LERSVVFTNLADDPA 221
Cdd:cd01134 86 GCGKTVISQSLSKWSNSD-----------VVIYVGCG---ERGNEMAEvleEFpelkdPITGEslMERTVLIANTSNMPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 222 VERTVTPRLALTTAEYLAfDKDYHVLvILTDMTN-YCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIE----- 295
Cdd:cd01134 152 AAREASIYTGITIAEYFR-DMGYNVS-LMADSTSrWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGRVRclgsp 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 756975214 296 GREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSR 353
Cdd:cd01134 230 GREGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRRHFPSINWLISYSK 287
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
14-354 |
9.89e-19 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 88.94 E-value: 9.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 14 LVFAEVDEPIGYDEIVEIETPQGETKRGQVLE-SSEGLVAIQVFEGTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSG 92
Cdd:PTZ00185 53 LIPAPGNPGVAYNTIIMIQVSPTTFAAGLVFNlEKDGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 93 QPIDGGpeIVPDERR---------DIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQ-I 162
Cdd:PTZ00185 133 HEVPVG--LLTRSRAlleseqtlgKVDAGAPNIVSRSPVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTSIAVStI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 163 ARQATVPEDEDSGEesefAVVFGAMGITQEEAN--EFMEDFERTGALERSVVFTNLADDPAVERTVTPRLALTTAEYLaF 240
Cdd:PTZ00185 211 INQVRINQQILSKN----AVISIYVSIGQRCSNvaRIHRLLRSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYF-M 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 241 DKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREG--SVTQIPILTMPGDDDTHPI 318
Cdd:PTZ00185 286 NRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLERAAMLSPGKGggSVTALPIVETLSNDVTAYI 365
|
330 340 350
....*....|....*....|....*....|....*.
gi 756975214 319 PDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRL 354
Cdd:PTZ00185 366 VTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSRV 401
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
76-356 |
1.03e-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: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 76 KMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRDIVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASG--- 152
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGvgk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 153 ------LPHNnlalqIARQATVpededsgeesefAVVFGAMGITQEEANEFMEDFERTGALER------SVVFTNLADDP 220
Cdd:cd01133 81 tvlimeLINN-----IAKAHGG------------YSVFAGVGERTREGNDLYHEMKESGVINLdglskvALVYGQMNEPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 221 AVeRTVTPRLALTTAEYLAFDKDYHVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIegREGS 300
Cdd:cd01133 144 GA-RARVALTGLTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITST--KKGS 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 756975214 301 VTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSRLMD 356
Cdd:cd01133 221 ITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILD 276
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
80-353 |
1.74e-17 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 84.64 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 80 TEDLLGRVLDGSGQ---PIDGGPEIVPDERRD--IVGAAINPYSREYPEEFIQTGVSAIDGMNTLVRGQKLPIFSASGLP 154
Cdd:PRK07165 76 SKEYFGKIIDIDGNiiyPEAQNPLSKKFLPNTssIFNLAHGLMTVKTLNEQLYTGIIAIDLLIPIGKGQRELIIGDRQTG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 155 HNNLALQ-IARQATvpededsgeeSEFAVVFGAMGITQEEANEFMEDFERTGALERSVVFTNLADDPaVERTVTPRLALT 233
Cdd:PRK07165 156 KTHIALNtIINQKN----------TNVKCIYVAIGQKRENLSRIYETLKEHDALKNTIIIDAPSTSP-YEQYLAPYVAMA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 234 TAEYLAFDKDyhVLVILTDMTNYCEALREIGAAREEVPGRRGYPGYMYTDLAQLYERAGRIEGREgSVTQIPILTMPGDD 313
Cdd:PRK07165 225 HAENISYNDD--VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERAGKFKNRK-TITALPILQTVDND 301
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 756975214 314 DTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSR 353
Cdd:PRK07165 302 ITSLISSNIISITDGQIVTSSDLFASGKLPAIDIDLSVSR 341
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
368-437 |
2.10e-15 |
|
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: 70.55 E-value: 2.10e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 368 HADVSDQMYAAYAEGEDLRDLVNIVGREALSERDNKYLDFAERFEaEFVNQGFDTDRSIEDTLDIGWDLL 437
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLE-EFLQQGQFEPETIEDTLEKLYPIK 69
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
58-420 |
2.84e-13 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 71.61 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 58 GTTGIDRNASVRFLGETLKMPVTEDLLGRVLDGSGQPIDGGPEIVPDERRdivgaainPYSREYPEeFIQ---------T 128
Cdd:CHL00060 77 ATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTS--------PIHRSAPA-FIQldtklsifeT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 129 GVSAIDGMNTLVRGQKLPIFSASGLPHNNLALQ----IAR-QATVPededsgeesefavVFGAMGITQEEANEFMEDFER 203
Cdd:CHL00060 148 GIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMElinnIAKaHGGVS-------------VFGGVGERTREGNDLYMEMKE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 204 TGALER--------SVVFTNLADDPAVERTV--TprlALTTAEYLAFDKDYHVLVILTDMTNYCEALREIGAAREEVPGR 273
Cdd:CHL00060 215 SGVINEqniaeskvALVYGQMNEPPGARMRVglT---ALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSA 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 756975214 274 RGYPGYMYTDLAQLYERAGRIegREGSVTQIPILTMPGDDDTHPIPDLTGYITEGQIYIDRDLNSQGIRPPINPLPSLSR 353
Cdd:CHL00060 292 VGYQPTLSTEMGSLQERITST--KEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTST 369
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 756975214 354 LMDDGIgeglTREDHADVSDQMYAAYAEGEDLRDLVNIVGREALSERDNKYLDFAERFEaEFVNQGF 420
Cdd:CHL00060 370 MLQPRI----VGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIE-RFLSQPF 431
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
7-72 |
1.47e-12 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 62.56 E-value: 1.47e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 756975214 7 ITEISGPLVFAEVDEP--IGYDEIVEIETPQGETKR-GQVLESSEGLVAIQVFEGTTGIDRNASVRFLG 72
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGrlPGLLNALEVELVEFGSLVlGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| 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 |
1.53e-07 |
|
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: 48.46 E-value: 1.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 756975214 4 YQTITEISGPLVFAEVDEPIGYDEIVEIETPQGETK---RGQVLESSEGLVAIQVFEGTTGIDRNASVRFLGE 73
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGEVAIGEVCEIERGDGNNEtvlKAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| |
