|
Name |
Accession |
Description |
Interval |
E-value |
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
6-446 |
0e+00 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 815.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 6 VRYSKILEIIGDIIRVQVpdtahqqeNSPRFGDLAVVENSDGSlSLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHP 85
Cdd:PRK02118 3 KIYTKITDITGNVITVEA--------EGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 86 MKVTYSENILGRVFRGTGEPIDGGPELSQDPkVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEP 165
Cdd:PRK02118 74 MQVTYSESLLGRRFNGSGKPIDGGPELEGEP-IEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 166 FNPFLARIGVQADADIVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAVEEGKR 245
Cdd:PRK02118 153 YNALLARIALQAEADIIILGGMGLTFDDYLFFKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFALEGKKK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 246 VLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYAQGGSVTVLTVTTMPGDDVTHPVPDNTGYIT 325
Cdd:PRK02118 233 VLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDFEDGGSITIIAVTTMPGDDVTHPVPDNTGYIT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 326 EGQFYLHDGKLDPFGSLSRLKQNVIGKVTREDHGQIMNTMIRFYSGATDAEQKQAMAFDLSEYDHKLLKFGELFQTRFMD 405
Cdd:PRK02118 313 EGQFYLRRGRIDPFGSLSRLKQLVIGKKTREDHGDLMNAMIRLYADSREAKEKMAMGFKLSNWDEKLLKFSELFESRLMD 392
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1233828039 406 INVSLALEQALDLAWQTLSECFEPQELLMKQALINKYFPKK 446
Cdd:PRK02118 393 LEVNIPLEEALDLGWKILAQCFHPEEVGIKEQLIDKYWPKN 433
|
|
| NtpB |
COG1156 |
Archaeal/vacuolar-type H+-ATPase subunit B/Vma2 [Energy production and conversion]; Archaeal ... |
6-450 |
1.44e-145 |
|
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: 423.40 E-value: 1.44e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 6 VRYSKILEIIGDIIRVQ-VPDTAhqqensprFGDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGIST-DSSVSFLG 83
Cdd:COG1156 4 KEYRTISEIAGPLLFVEgVEGVG--------YGELVEIELPDGERRRGQVLEVSEDKAVVQVFEGTTGLSLkNTKVRFLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 84 HPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSG 163
Cdd:COG1156 76 EPLELPVSEDMLGRVFNGLGRPIDGGPPIIPEKRLDINGSPINPVAREYPREFIQTGISAIDGLNTLVRGQKLPIFSGSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 164 EPFNPFLARIGVQA---DAD---IVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEH 237
Cdd:COG1156 156 LPHNELAAQIARQAkvrGEEekfAVVFAAMGITHDEANFFREEFEETGALDRVVMFLNLADDPAIERIITPRMALTAAEY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 238 FAVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAadyaqG------GSVTVLTVTTMPGD 311
Cdd:COG1156 236 LAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYSDLASLYERA-----GrikgrkGSITQIPILTMPND 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 312 DVTHPVPDNTGYITEGQFYLH---DGK-----LDPFGSLSRLKQNVIGK-VTREDHGQIMNTMIRFYSGATDAeqkQAMA 382
Cdd:COG1156 311 DITHPIPDLTGYITEGQIVLSrdlHRKgiyppIDVLPSLSRLMKDGIGEgKTREDHADVANQLYAAYARGQEV---RELA 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1233828039 383 F-----DLSEYDHKLLKFGELFQTRFM----DINVSlaLEQALDLAWQTLSECfePQELL--MKQALINKYFPKKLESK 450
Cdd:COG1156 388 AivgeeALSETDKKYLKFADAFERRFVnqgfDENRS--IEETLDLGWELLSIL--PREELkrIDDEYIEKYYPKKRAKE 462
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
5-450 |
8.55e-142 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 413.84 E-value: 8.55e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 5 LVRYSKILEIIGDIIRVQ-VPDTAhqqensprFGDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGIST-DSSVSFL 82
Cdd:PRK04196 1 LKEYRTVSEIKGPLLFVEgVEGVA--------YGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLkDTKVRFT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 83 GHPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVS 162
Cdd:PRK04196 73 GEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 163 GEPFNPFLARIGVQA------DADIVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAE 236
Cdd:PRK04196 153 GLPHNELAAQIARQAkvlgeeENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 237 HFAVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAAdYAQG--GSVTVLTVTTMPGDDVT 314
Cdd:PRK04196 233 YLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAG-RIKGkkGSITQIPILTMPDDDIT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 315 HPVPDNTGYITEGQFYLhDGKL---------DPFGSLSRLKQNVIGK-VTREDHGQIMNTMIRFYSGATDAEQKQAM--A 382
Cdd:PRK04196 312 HPIPDLTGYITEGQIVL-SRELhrkgiyppiDVLPSLSRLMKDGIGEgKTREDHKDVANQLYAAYARGKDLRELAAIvgE 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1233828039 383 FDLSEYDHKLLKFGELFQTRFM----DINVSlaLEQALDLAWQTLSECfePQELL--MKQALINKYFPKKLESK 450
Cdd:PRK04196 391 EALSERDRKYLKFADAFEREFVnqgfDENRS--IEETLDLGWELLSIL--PESELkrIKDEYIEKYHPKYRGKE 460
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
85-351 |
1.98e-137 |
|
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: 395.82 E-value: 1.98e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 85 PMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGE 164
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 165 PFNPFLARIGVQA------DADIVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHF 238
Cdd:cd01135 81 PHNELAAQIARQAgvvgseENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 239 AVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYA-QGGSVTVLTVTTMPGDDVTHPV 317
Cdd:cd01135 161 AYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRVEgRKGSITQIPILTMPNDDITHPI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1233828039 318 PDNTGYITEGQFYLhDGKL---------DPFGSLSRLKQNVIG 351
Cdd:cd01135 241 PDLTGYITEGQIYL-DRDLhnkgiyppiDVLPSLSRLMKSGIG 282
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
34-446 |
7.63e-107 |
|
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: 324.75 E-value: 7.63e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 34 PRFGDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGI-STDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPEL 112
Cdd:TIGR01040 21 PRFAEIVNLTLPDGTVRSGQVLEVSGNKAVVQVFEGTSGIdAKKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPPV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 113 SQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFLARIGVQA------DADI----- 181
Cdd:TIGR01040 101 LAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAglvklpTKDVhdghe 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 182 ----VVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAVEEGKRVLVLLSDMTAFA 257
Cdd:TIGR01040 181 dnfaIVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTTAEYLAYQCEKHVLVILTDMSSYA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 258 DALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYA-QGGSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFY----LH 332
Cdd:TIGR01040 261 DALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYvdrqLH 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 333 DGKLDP----FGSLSRLKQNVIGK-VTREDHGQIMNTMIRFYSGATDAEQKQAMAFD--LSEYDHKLLKFGELFQTRFMD 405
Cdd:TIGR01040 341 NRQIYPpinvLPSLSRLMKSAIGEgMTRKDHSDVSNQLYACYAIGKDVQAMKAVVGEeaLSSEDLLYLEFLDKFEKNFIA 420
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1233828039 406 INV--SLALEQALDLAWQTLSecFEPQELLMK--QALINKYFPKK 446
Cdd:TIGR01040 421 QGPyeNRTIFESLDIAWQLLR--IFPKEMLKRipAKILEEFYPRK 463
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
87-345 |
8.36e-62 |
|
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: 201.92 E-value: 8.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 87 KVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPF 166
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 167 NPF---LARIGVQADADIVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEG 243
Cdd:cd19476 81 TVLamqLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFR-DNG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 244 KRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADY-AQGGSVTVLTVTTMPGDDVTHPVPDNTG 322
Cdd:cd19476 160 QHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVkDGGGSITAIPAVSTPGDDLTDPIPDNTF 239
|
250 260 270
....*....|....*....|....*....|.
gi 1233828039 323 YITEGQFYL--------HDGKLDPFGSLSRL 345
Cdd:cd19476 240 AILDGQIVLsrelarkgIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
144-343 |
1.39e-61 |
|
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: 199.12 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 144 IDIFNCLVESQKIPIFSVSGEPFNPFLARIGVQADADIVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVE 223
Cdd:pfam00006 5 IDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDEPPLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 224 RMLIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAA-DYAQGGSVTV 302
Cdd:pfam00006 85 RYRAPYTALTIAEYFR-DQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGrVKGKGGSITA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1233828039 303 LTVTTMPGDDVTHPVPDNTGYITEGQFYLhDGKL---------DPFGSLS 343
Cdd:pfam00006 164 LPTVLVPGDDITDPIPDNTRSILDGQIVL-SRDLaekghypaiDVLASVS 212
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
6-424 |
6.03e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 162.29 E-value: 6.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 6 VRY-SKILEIIGDIIRVQVPDtAHQqensprfGDLAVVENSDgslSLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGH 84
Cdd:PRK06820 27 LRYrGPIVEIGPTLLRASLPG-VAQ-------GELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGH 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 85 PMKVTYSENILGRVFRGTGEPIDGGPELSQDPKvTIGGPSVNPMRRILASKMIRTNVPMID-IFNClVESQKIPIFSVSG 163
Cdd:PRK06820 96 MHQVQVGADLAGRILDGLGAPIDGGPPLTGQWR-ELDCPPPSPLTRQPIEQMLTTGIRAIDgILSC-GEGQRIGIFAAAG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 164 EPFNPFLARIGVQADADIVVfggLGLIFDDYYFFRQAFE---DAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAv 240
Cdd:PRK06820 174 VGKSTLLGMLCADSAADVMV---LALIGERGREVREFLEqvlTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFR- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 241 EEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYAQgGSVTVLTVTTMPGDDVTHPVPDN 320
Cdd:PRK06820 250 DRGKKVLLMADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDR-GSITAFYTVLVEGDDMNEPVADE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 321 TGYITEGQFYL--------HDGKLDPFGSLSRLKQNVIGKVTREdHGQIMNTMIRFYsgatdaeQKQAMAFDLSEY---- 388
Cdd:PRK06820 329 VRSLLDGHIVLsrrlagagHYPAIDIAASVSRIMPQIVSAGQLA-MAQKLRRMLACY-------QEIELLVRVGEYqage 400
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1233828039 389 ----DHKLLKFGELFQTRFMDINVSLALEQALDLAWQTLS 424
Cdd:PRK06820 401 dlqaDEALQRYPAICAFLQQDHSETAHLETTLEHLAQVVG 440
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
10-382 |
8.82e-42 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 153.75 E-value: 8.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 10 KILEIIGDIIRVQVPDTahqqenspRFGDLAVVENSDGSLSL-AQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKV 88
Cdd:PRK06936 26 RVTQVTGTILKAVVPGV--------RIGELCYLRNPDNSLSLqAEVIGFAQHQALLTPLGEMYGISSNTEVSPTGTMHQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 89 TYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMID-IFNClVESQKIPIFSVSGEPFN 167
Cdd:PRK06936 98 GVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDgLLTC-GEGQRMGIFAAAGGGKS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 168 PFLARIGVQADADIVVfggLGLIFDDYYFFRQAFE-DAGV--FSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGK 244
Cdd:PRK06936 177 TLLASLIRSAEVDVTV---LALIGERGREVREFIEsDLGEegLRKAVLVVATSDRPSMERAKAGFVATSIAEYFR-DQGK 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 245 RVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADyAQGGSVTVLTVTTMPGDDVTHPVPDNTGYI 324
Cdd:PRK06936 253 RVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQ-SDKGSITALYTVLVEGDDMTEPVADETRSI 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1233828039 325 TEGQFYL--------HDGKLDPFGSLSRLKQNVIGKVTREDHGQIMNTMIRF-----------YSGATDAEQKQAMA 382
Cdd:PRK06936 332 LDGHIILsrklaaanHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYeevelllqigeYQKGQDKEADQAIE 408
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
2-370 |
1.37e-36 |
|
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: 139.40 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 2 LQALVRYSKILEIIGDIIRVQVPDTahqqenspRFGDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGISTDSSVSF 81
Cdd:COG1157 14 LPPVRVSGRVTRVVGLLIEAVGPDA--------SIGELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPGARVVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 82 LGHPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSV 161
Cdd:COG1157 86 TGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRIGIFAG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 162 SGepf---npfLARigvQADADIVVfggLGLI---------FDDyyffrqafEDAG--VFSRTVMFVNLASDPIVERMLI 227
Cdd:COG1157 166 SGvgkstllgmIAR---NTEADVNV---IALIgergrevreFIE--------DDLGeeGLARSVVVVATSDEPPLMRLRA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 228 PDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADyAQGGSVT----VL 303
Cdd:COG1157 232 AYTATAIAEYFR-DQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGN-GGKGSITafytVL 309
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1233828039 304 TvttmPGDDVTHPVPDNTGYITEGQFYLhDGKL---------DPFGSLSRlkqnVIGKVTREDHGQIMNTMIRFYS 370
Cdd:COG1157 310 V----EGDDMNDPIADAVRGILDGHIVL-SRKLaerghypaiDVLASISR----VMPDIVSPEHRALARRLRRLLA 376
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
4-360 |
8.82e-35 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 134.51 E-value: 8.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 4 ALVRYSKILEIIGDIIRVQVPDTahqqenspRFGDLAVVENSDGSL-SLAQVINLKEDTVALQVFKGTKGISTDSSVSFL 82
Cdd:PRK09099 21 AVRRTGKVVEVIGTLLRVSGLDV--------TLGELCELRQRDGTLlQRAEVVGFSRDVALLSPFGELGGLSRGTRVIGL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 83 GHPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVS 162
Cdd:PRK09099 93 GRPLSVPVGPALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 163 G---EPFNPFLARiGVQADAD-IVVFGGLGLIFDDyyFFRQAFEDAGVfSRTVMFVNLASDPIVERMLIPDMALAVAEHF 238
Cdd:PRK09099 173 GvgkSTLMGMFAR-GTQCDVNvIALIGERGREVRE--FIELILGEDGM-ARSVVVCATSDRSSIERAKAAYVATAIAEYF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 239 AvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAAdYAQGGSVTVLTVTTMPGDDVTHPVP 318
Cdd:PRK09099 249 R-DRGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAG-MGETGSITALYTVLAEDESGSDPIA 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1233828039 319 DNTGYITEGQFYLHDG--------KLDPFGSLSRlkqnVIGKVTREDHGQ 360
Cdd:PRK09099 327 EEVRGILDGHMILSREiaarnqypAIDVLGSLSR----VMPQVVPREHVQ 372
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
35-383 |
4.51e-34 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 132.81 E-value: 4.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 35 RFGDLaVVENSDGSLSLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGhPMKVTYSENILGRVFRGTGEPIDGGPELSQ 114
Cdd:PRK06002 48 RLGDF-VAIRADGGTHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFRKG-PLRIRPDPSWKGRVINALGEPIDGLGPLAP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 115 DPKVTIGGPSVNP-MRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFLARIGVQADADIVVfggLGLIFDD 193
Cdd:PRK06002 126 GTRPMSIDATAPPaMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAMLARADAFDTVV---IALVGER 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 194 YYFFRQAFED--AGVFSRTVMFVNlASD--PIVERMlIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQ 269
Cdd:PRK06002 203 GREVREFLEDtlADNLKKAVAVVA-TSDesPMMRRL-APLTATAIAEYFR-DRGENVLLIVDSVTRFAHAAREVALAAGE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 270 VPANRGYPGDLYSQLARRYEKAADYAQG-GSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYL-----HDGK---LDPFG 340
Cdd:PRK06002 280 PPVARGYPPSVFSELPRLLERAGPGAEGgGSITGIFSVLVDGDDHNDPVADSIRGTLDGHIVLdraiaEQGRypaVDPLA 359
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1233828039 341 SLSRLKQNViGKVTREDHGQIMNTMI-RF-----------YSGATDAEQKQAMAF 383
Cdd:PRK06002 360 SISRLARHA-WTPEQRKLVSRLKSMIaRFeetrdlrliggYRAGSDPDLDQAVDL 413
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
91-345 |
4.12e-31 |
|
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: 120.36 E-value: 4.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 91 SENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFL 170
Cdd:cd01136 5 GDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGKSTLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 171 ARIGVQADADIVVFgglGLIFDDYYFFRQAFED---AGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVL 247
Cdd:cd01136 85 GMIARNTDADVNVI---ALIGERGREVREFIEKdlgEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFR-DQGKKVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 248 VLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADyAQGGSVTVLTVTTMPGDDVTHPVPDNTGYITEG 327
Cdd:cd01136 161 LLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGN-GEKGSITAFYTVLVEGDDFNDPIADEVRSILDG 239
|
250 260
....*....|....*....|....*.
gi 1233828039 328 QFYL--------HDGKLDPFGSLSRL 345
Cdd:cd01136 240 HIVLsrrlaergHYPAIDVLASISRV 265
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
7-376 |
8.10e-30 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 120.44 E-value: 8.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 7 RYSKILEIIGDIIRVQVPDTAhqqensprFGDLAVVENSDGslsLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPM 86
Cdd:PRK07594 21 RWGRIQDVSATLLNAWLPGVF--------MGELCCIKPGEE---LAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 87 KVTYSENILGRVFRGTGEPIDGGPeLSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPF 166
Cdd:PRK07594 90 QVPVGEALLGRVIDGFGRPLDGRE-LPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 167 NPFLARIGVQADADIVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRV 246
Cdd:PRK07594 169 STLLAMLCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFR-DNGKRV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 247 LVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAAdYAQGGSVTVLTVTTMPGDDVTHPVPDNTGYITE 326
Cdd:PRK07594 248 VLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTG-MGEKGSITAFYTVLVEGDDMNEPLADEVRSLLD 326
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1233828039 327 GQFYL--------HDGKLDPFGSLSRlkqnVIGKVTREDHGQIMNTMIRFYSGATDAE 376
Cdd:PRK07594 327 GHIVLsrrlaergHYPAIDVLATLSR----VFPVVTSHEHRQLAAILRRCLALYQEVE 380
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
37-370 |
1.20e-28 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 117.30 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 37 GDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPELSQDP 116
Cdd:PRK07196 39 GQRCRIESVDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGST 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 117 KVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFLARIGVQADADIVVFGGLGLIFDDYY- 195
Cdd:PRK07196 119 PLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQADVVVVGLIGERGREVKe 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 196 FFRQAFEDAGVfSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRG 275
Cdd:PRK07196 199 FIEHSLQAAGM-AKSVVVAAPADESPLMRIKATELCHAIATYYR-DKGHDVLLLVDSLTRYAMAQREIALSLGEPPATKG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 276 YPGDLYSQLARRYEKAADYAQGGSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYL--------HDGKLDPFGSLSRLKQ 347
Cdd:PRK07196 277 YPPSAFSIIPRLAESAGNSSGNGTMTAIYTVLAEGDDQQDPIVDCARAVLDGHIVLsrklaeagHYPAIDISQSISRCMS 356
|
330 340
....*....|....*....|...
gi 1233828039 348 NVIGKvtreDHGQIMNTMIRFYS 370
Cdd:PRK07196 357 QVIGS----QQAKAASLLKQCYA 375
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
1-376 |
9.51e-27 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 111.74 E-value: 9.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 1 MLQALVRYSKILEIIGDIIRVQVPDTAhqqensprFGDLAVV---ENSDGSLsLAQVINLKEDTVALQVFKGTKGISTDS 77
Cdd:PRK07721 12 TLDPYKRYGKVSRVIGLMIESKGPESS--------IGDVCYIhtkGGGDKAI-KAEVVGFKDEHVLLMPYTEVAEIAPGC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 78 SVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIP 157
Cdd:PRK07721 83 LVEATGKPLEVKVGSGLIGQVLDALGEPLDGSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 158 IFSVSGEPFNPFLARIGVQADADIVVfggLGLIFDDYYFFRQAFE-DAGV--FSRTVMFVNLASDPIVERMLIPDMALAV 234
Cdd:PRK07721 163 IFAGSGVGKSTLMGMIARNTSADLNV---IALIGERGREVREFIErDLGPegLKRSIVVVATSDQPALMRIKGAYTATAI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 235 AEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYAQgGSVTVLTVTTMPGDDVT 314
Cdd:PRK07721 240 AEYFR-DQGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNAS-GSITAFYTVLVDGDDMN 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1233828039 315 HPVPDNTGYITEGQFYLhDGKLDPFG---------SLSRLKQNVIgkvtREDHGQIMNTMIRFYSGATDAE 376
Cdd:PRK07721 318 EPIADTVRGILDGHFVL-DRQLANKGqypainvlkSVSRVMNHIV----SPEHKEAANRFRELLSTYQNSE 383
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
37-350 |
9.82e-26 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 109.05 E-value: 9.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 37 GDLAVVENSDGSLSL---AQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPELS 113
Cdd:PRK05688 49 GSRCLVINDDSYHPVqveAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMK 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 114 QDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFLARIGVQADADIVVfggLGLIFDD 193
Cdd:PRK05688 129 AEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEADIIV---VGLIGER 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 194 ----YYFFRQAFEDAGVfSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQ 269
Cdd:PRK05688 206 grevKEFIEHILGEEGL-KRSVVVASPADDAPLMRLRAAMYCTRIAEYFR-DKGKNVLLLMDSLTRFAQAQREIALAIGE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 270 VPANRGYPGDLYSQLARRYEKAADYAQG-GSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYL--------HDGKLDPFG 340
Cdd:PRK05688 284 PPATKGYPPSVFAKLPKLVERAGNAEPGgGSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLsrrlaeegHYPAIDIEA 363
|
330
....*....|
gi 1233828039 341 SLSRLKQNVI 350
Cdd:PRK05688 364 SISRVMPQVV 373
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
2-388 |
1.90e-25 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 107.77 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 2 LQALVRYSKILEIIGDIIRVQVPDTAhqqensprFGDLAVVE---NSDGSLSLAQVINLKEDTVALQVFKGTKGISTDSS 78
Cdd:PRK08149 1 LRLLQRLAHPLRIQGPIIEAELPDVA--------IGEICEIRagwHSNEVIARAQVVGFQRERTILSLIGNAQGLSRQVV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 79 VSFLGHPMKVTYSENILGRVFRGTGE------------------PIDGGPelsqdpkvtiggPSVNpMRRILASKMIrTN 140
Cdd:PRK08149 73 LKPTGKPLSVWVGEALLGAVLDPTGKiverfdapptvgpiseerVIDVAP------------PSYA-ERRPIREPLI-TG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 141 VPMID-IFNCLVeSQKIPIFSVSGEPFNPFLARIGVQADADIVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMfVNLASD 219
Cdd:PRK08149 139 VRAIDgLLTCGV-GQRMGIFASAGCGKTSLMNMLIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVL-VYATSD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 220 -PIVERMLIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYaQGG 298
Cdd:PRK08149 217 fSSVDRCNAALVATTVAEYFR-DQGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGAT-LAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 299 SVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYL--------HDGKLDPFGSLSRlkqnVIGKVTREDHGQIMNtmiRFYS 370
Cdd:PRK08149 295 SITAFYTVLLESEEEPDPIGDEIRSILDGHIYLsrklaakgHYPAIDVLKSVSR----VFGQVTDPKHRQLAA---AFRK 367
|
410
....*....|....*...
gi 1233828039 371 GATDAEQKQaMAFDLSEY 388
Cdd:PRK08149 368 LLTRLEELQ-LFIDLGEY 384
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
37-370 |
2.11e-25 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 107.86 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 37 GDLAVVENSDGSLsLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPELSQDP 116
Cdd:PRK08972 47 GSLCSIETMAGEL-EAEVVGFDGDLLYLMPIEELRGVLPGARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 117 KVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFLARIGVQADADIVVfggLGLIFDDYYF 196
Cdd:PRK08972 126 RASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMGLFAGSGVGKSVLLGMMTRGTTADVIV---VGLVGERGRE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 197 FRQAFEDA-GVFSRTVMFVNLA---SDPIVeRMLIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPA 272
Cdd:PRK08972 203 VKEFIEEIlGEEGRARSVVVAApadTSPLM-RLKGCETATTIAEYFR-DQGLNVLLLMDSLTRYAQAQREIALAVGEPPA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 273 NRGYPGDLYSQLARRYEKAADYAQG-GSVTVL-TVTTmPGDDVTHPVPDNTGYITEGQFYL--------HDGKLDPFGSL 342
Cdd:PRK08972 281 TKGYPPSVFAKLPALVERAGNGGPGqGSITAFyTVLT-EGDDLQDPIADASRAILDGHIVLsreladsgHYPAIDIEASI 359
|
330 340
....*....|....*....|....*...
gi 1233828039 343 SRlkqnVIGKVTREDHGQIMNTMIRFYS 370
Cdd:PRK08972 360 SR----VMPMVISEEHLEAMRRVKQVYS 383
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
2-327 |
3.27e-24 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 104.29 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 2 LQALVRYSKILEIIGDIIRVQVPDTAHqqenspRFGDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGISTDSSVSF 81
Cdd:PRK08927 12 IDTLVIYGRVVAVRGLLVEVAGPIHAL------SVGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 82 LGHPMKVTYSENILGRVFRGTGEPIDGGPELSQdpkvtigGPSVNPMR--------RILASKMIRTNVPMIDIFNCLVES 153
Cdd:PRK08927 86 ANAAAAVRPSRAWLGRVVNALGEPIDGKGPLPQ-------GPVPYPLRappppahsRARVGEPLDLGVRALNTFLTCCRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 154 QKIPIFSVSGEPFNPFLARIGVQADADIVVfggLGLIFDDYYFFRQAFED----AGVfSRTVMFVNLASDPIVERMLIPD 229
Cdd:PRK08927 159 QRMGIFAGSGVGKSVLLSMLARNADADVSV---IGLIGERGREVQEFLQDdlgpEGL-ARSVVVVATSDEPALMRRQAAY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 230 MALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYAQG-GSVTVLTVTTM 308
Cdd:PRK08927 235 LTLAIAEYFR-DQGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAGPGPIGeGTITGLFTVLV 313
|
330
....*....|....*....
gi 1233828039 309 PGDDVTHPVPDNTGYITEG 327
Cdd:PRK08927 314 DGDDHNEPVADAVRGILDG 332
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
51-370 |
1.85e-23 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 101.98 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 51 LAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRR 130
Cdd:PRK06793 54 LCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFER 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 131 ILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFLARIGVQADADIVVFGGLG----LIFDdyyFFRQAFEDAGV 206
Cdd:PRK06793 134 EEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKADINVISLVGergrEVKD---FIRKELGEEGM 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 207 fSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANrGYPGDLYSQLAR 286
Cdd:PRK06793 211 -RKSVVVVATSDESHLMQLRAAKLATSIAEYFR-DQGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKK 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 287 RYEKAADyAQGGSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYL--------HDGKLDPFGSLSRLKQNVIGkvtrEDH 358
Cdd:PRK06793 288 LLERSGK-TQKGSITGIYTVLVDGDDLNGPVPDLARGILDGHIVLkrelatlsHYPAISVLDSVSRIMEEIVS----PNH 362
|
330
....*....|..
gi 1233828039 359 GQIMNTMIRFYS 370
Cdd:PRK06793 363 WQLANEMRKILS 374
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
33-370 |
6.71e-22 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 97.45 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 33 SPRFGDLAVVENSDGSLS-LAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPE 111
Cdd:PRK08472 36 NPSVGDIVKIESSDNGKEcLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLLGRVVDPLGRPIDGKGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 112 LSQDPKVTIGGPSVNPMRRILASKMIRTNVPMID-IFNCLVeSQKIPIFSVSGEPFNPFLARIGVQADADIVVfggLGLI 190
Cdd:PRK08472 116 IDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDgLLTCGK-GQKLGIFAGSGVGKSTLMGMIVKGCLAPIKV---VALI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 191 ---------FDDYYFfrqafedAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALK 261
Cdd:PRK08472 192 gergreipeFIEKNL-------GGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFK-NQGLDVLFIMDSVTRFAMAQR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 262 EISISMDQVPANRGYPGDLYSQLARRYEKAADYAQGGSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYLHDgKLDPFG- 340
Cdd:PRK08472 264 EIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEGKGSITAFFTVLVEGDDMSDPIADQSRSILDGHIVLSR-ELTDFGi 342
|
330 340 350
....*....|....*....|....*....|....*...
gi 1233828039 341 --------SLSRlkqnVIGKVTREDHGQIMNTMIRFYS 370
Cdd:PRK08472 343 yppinilnSASR----VMNDIISPEHKLAARKFKRLYS 376
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
8-321 |
8.43e-21 |
|
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: 94.40 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 8 YSKILEIIGDIIRVQVPDTAhqqenSPRFGD-LAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPM 86
Cdd:TIGR01039 2 KGKVVQVIGPVVDVEFEQGE-----LPRIYNaLKVQNRAESELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 87 KVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSG--- 163
Cdd:TIGR01039 77 SVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGvgk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 164 -----EPFNpflaRIGvQADADIVVFGGLGLIF---DDYYFfrqAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVA 235
Cdd:TIGR01039 157 tvliqELIN----NIA-KEHGGYSVFAGVGERTregNDLYH---EMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 236 EHFAVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADyAQGGSVTVLTVTTMPGDDVTH 315
Cdd:TIGR01039 229 EYFRDEQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITS-TKTGSITSVQAVYVPADDLTD 307
|
....*.
gi 1233828039 316 PVPDNT 321
Cdd:TIGR01039 308 PAPATT 313
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
36-344 |
9.51e-19 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 88.04 E-value: 9.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 36 FGDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPELSQD 115
Cdd:PRK05922 40 LGELCQISLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 116 PKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFLARIGVQADADIVVFGGLGLIFDDYY 195
Cdd:PRK05922 120 HLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 196 FFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRG 275
Cdd:PRK05922 200 EYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAEYFR-DQGHRVLFIMDSLSRWIAALQEVALARGETLSAHH 278
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1233828039 276 YPGDLYSQLARRYEKAADYAQGGSVTVLTVTTMPgddvTHP--VPDNTGYITEGQFYL-HDGK------LDPFGSLSR 344
Cdd:PRK05922 279 YAASVFHHVSEFTERAGNNDKGSITALYAILHYP----NHPdiFTDYLKSLLDGHFFLtPQGKalasppIDILTSLSR 352
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
3-331 |
5.14e-18 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 86.12 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 3 QALVRYS---KILEI-----IGD-IIRVQ-VPDTAhqqensprFGDLAVVENSdgslSLAQVINLKEDTVALQVFKGTKG 72
Cdd:PRK13343 14 QRIARYEpqpDAREIgrvesVGDgIAFVSgLPDAA--------LDELLRFEGG----SRGFAFNLEEELVGAVLLDDTAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 73 ISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFnclve 152
Cdd:PRK13343 82 ILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDAL----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 153 sqkIPIfsvsgepfnpflAR------IG---------------VQADADIV-VFGGLGLifDDYYFFR--QAFEDAGVFS 208
Cdd:PRK13343 157 ---IPI------------GRgqreliIGdrqtgktaiaidaiiNQKDSDVIcVYVAIGQ--KASAVARviETLREHGALE 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 209 RTVMFVNLASDPIVERMLIPDMALAVAEHFaVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRY 288
Cdd:PRK13343 220 YTTVVVAEASDPPGLQYLAPFAGCAIAEYF-RDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLL 298
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1233828039 289 EKAADYAQ---GGSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYL 331
Cdd:PRK13343 299 ERAAKLSPelgGGSLTALPIIETLAGELSAYIPTNLISITDGQIYL 344
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
94-350 |
1.97e-17 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 84.06 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 94 ILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSGEPFNPFLARI 173
Cdd:PRK07960 116 LLGRVLDGSGKPLDGLPAPDTGETGALITPPFNPLQRTPIEHVLDTGVRAINALLTVGRGQRMGLFAGSGVGKSVLLGMM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 174 GVQADADIVVFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLVLLSDM 253
Cdd:PRK07960 196 ARYTQADVIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQGAAYATRIAEDFR-DRGQHVLLIMDSL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 254 TAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYAQ-GGSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYL- 331
Cdd:PRK07960 275 TRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNGISgGGSITAFYTVLTEGDDQQDPIADSARAILDGHIVLs 354
|
250 260
....*....|....*....|....*.
gi 1233828039 332 -------HDGKLDPFGSLSRLKQNVI 350
Cdd:PRK07960 355 rrlaeagHYPAIDIEASISRAMTALI 380
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
86-331 |
1.01e-15 |
|
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: 77.21 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 86 MKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFnclvesqkIPI------- 158
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSL--------IPIgrgqrel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 159 ---------FSVSgepfnpfLARIGVQADADIV-VFGGLGLIFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIP 228
Cdd:cd01132 74 iigdrqtgkTAIA-------IDTIINQKGKKVYcIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 229 DMALAVAEHFAvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGD---LYSQLARRYEKAADYAQGGSVTVLTV 305
Cdd:cd01132 147 YAGCAMGEYFR-DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDvfyLHSRLLERAAKLSDELGGGSLTALPI 225
|
250 260
....*....|....*....|....*.
gi 1233828039 306 TTMPGDDVTHPVPDNTGYITEGQFYL 331
Cdd:cd01132 226 IETQAGDVSAYIPTNVISITDGQIFL 251
|
|
| 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 ... |
354-442 |
2.04e-13 |
|
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: 65.92 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 354 TREDHGQIMNTMIRFYSGATDAeqkQAMAF-----DLSEYDHKLLKFGELFQTRFM--DINVSLALEQALDLAWQTLSEC 426
Cdd:cd18112 3 TREDHRDVSNQLYAAYARGKDV---RALAAivgeeALSEEDRLYLEFADRFEREFInqGFYENRSIEETLDLGWELLSIL 79
|
90
....*....|....*...
gi 1233828039 427 fePQELL--MKQALINKY 442
Cdd:cd18112 80 --PKEELkrISEEYIDKY 95
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
177-321 |
4.46e-13 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 71.59 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 177 ADADIVVFGGLGL-------IFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLVL 249
Cdd:PRK14698 680 SDAQVVIYIGCGErgnemtdVLEEFPKLKDPKTGKPLMERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYDVALM 758
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1233828039 250 LSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKA-------ADYaQGGSVTVLTVTTMPGDDVTHPVPDNT 321
Cdd:PRK14698 759 ADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDY-RVGSVSVIGAVSPPGGDFSEPVVQNT 836
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
42-331 |
1.22e-12 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 69.61 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 42 VENSDGSLSLAqvINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIG 121
Cdd:CHL00059 32 VEFEDGTIGIA--LNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 122 GPSvnP---MRR---------ILA-SKMI-----------------RTNVPMIDIFNclvesQKipifsvsGEPFNPFLA 171
Cdd:CHL00059 110 SPA--PgiiSRRsvyeplqtgLIAiDSMIpigrgqreliigdrqtgKTAVATDTILN-----QK-------GQNVICVYV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 172 RIGVQAD--ADIVvfgglglifddyyffrQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFaVEEGKRVLVL 249
Cdd:CHL00059 176 AIGQKASsvAQVV----------------TTLQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYF-MYRGRHTLII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 250 LSDMTAFADALKEISISMDQVPANRGYPGD---LYSQLARRYEKAADYAQGGSVTVLTVTTMPGDDVTHPVPDNTGYITE 326
Cdd:CHL00059 239 YDDLSKQAQAYRQMSLLLRRPPGREAYPGDvfyLHSRLLERAAKLSSQLGEGSMTALPIVETQAGDVSAYIPTNVISITD 318
|
....*
gi 1233828039 327 GQFYL 331
Cdd:CHL00059 319 GQIFL 323
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
177-336 |
1.66e-11 |
|
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: 64.52 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 177 ADADIVVFGGLGL-------IFDDYYFFRQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLvL 249
Cdd:cd01134 100 SNSDVVIYVGCGErgnemaeVLEEFPELKDPITGESLMERTVLIANTSNMPVAAREASIYTGITIAEYFR-DMGYNVS-L 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 250 LSDMTA-FADALKEISISMDQVPANRGYPGDLYSQLARRYEKAA------DYAQGGSVTVLTVTTMPGDDVTHPVPDNTG 322
Cdd:cd01134 178 MADSTSrWAEALREISGRLEEMPAEEGYPAYLGARLAEFYERAGrvrclgSPGREGSVTIVGAVSPPGGDFSEPVTQATL 257
|
170
....*....|....
gi 1233828039 323 YITeGQFYLHDGKL 336
Cdd:cd01134 258 RIV-QVFWGLDKKL 270
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
10-321 |
2.09e-10 |
|
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: 62.41 E-value: 2.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 10 KILEIIGDIIRVQVPDtahqqENSPRFGDLAVVENSDGS---LSLAQviNLKEDTV---ALQvfkGTKGISTDSSVSFLG 83
Cdd:COG0055 7 KIVQVIGPVVDVEFPE-----GELPAIYNALEVENEGGGelvLEVAQ--HLGDNTVrciAMD---STDGLVRGMEVIDTG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 84 HPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSVNPMRRILASKMIRTNVPMIDIFNCLVESQKIPIFSVSG 163
Cdd:COG0055 77 APISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 164 --------EPFNpflaRIgVQADADIVVFGGLG--------LIFDdyyffrqaFEDAGVFSRTVMFVNLASDPIVERMLI 227
Cdd:COG0055 157 vgktvlimELIH----NI-AKEHGGVSVFAGVGertregndLYRE--------MKESGVLDKTALVFGQMNEPPGARLRV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 228 PDMALAVAEHFAVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADyAQGGSVTVLTVTT 307
Cdd:COG0055 224 ALTALTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITS-TKKGSITSVQAVY 302
|
330
....*....|....
gi 1233828039 308 MPGDDVTHPVPDNT 321
Cdd:COG0055 303 VPADDLTDPAPATT 316
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
87-321 |
6.39e-10 |
|
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: 59.93 E-value: 6.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 87 KVTYSENILGRVFRGTGEPIDGGPELSQDPKVTI--GGPSVNPMRriLASKMIRTNVPMIDIFNCLVESQKIPIFSVSG- 163
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIhrEAPEFVELS--TEQEILETGIKVVDLLAPYAKGGKIGLFGGAGv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 164 -------EPFNpflaRIgVQADADIVVFGGLGLIF----DDYYFFRQA-FEDAGVFSRTVMFVNLASDPIVERMLIPDMA 231
Cdd:cd01133 79 gktvlimELIN----NI-AKAHGGYSVFAGVGERTregnDLYHEMKESgVINLDGLSKVALVYGQMNEPPGARARVALTG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 232 LAVAEHFAVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADyAQGGSVTVLTVTTMPGD 311
Cdd:cd01133 154 LTMAEYFRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITS-TKKGSITSVQAVYVPAD 232
|
250
....*....|
gi 1233828039 312 DVTHPVPDNT 321
Cdd:cd01133 233 DLTDPAPATT 242
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
205-336 |
7.27e-10 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 61.21 E-value: 7.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 205 GVFSRTVMFVNLASDPIVERMLIPDMALAVAEHFaVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQL 284
Cdd:PTZ00185 251 GALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYF-MNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLH 329
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1233828039 285 ARRYEKAADYAQ---GGSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYLhDGKL 336
Cdd:PTZ00185 330 SRLLERAAMLSPgkgGGSVTALPIVETLSNDVTAYIVTNVISITDGQIYL-DTKL 383
|
|
| 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 ... |
8-84 |
1.58e-09 |
|
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: 53.97 E-value: 1.58e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1233828039 8 YSKILEIIGDIIRVQ-VPDtahqqensPRFGDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGISTD-SSVSFLGH 84
Cdd:cd18118 2 YRTVSEINGPLVIVEgVKG--------VKYGEIVEITLPDGEVRRGQVLEVSGDKAVVQVFEGTSGLDLKgTKVRFTGE 72
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
10-321 |
4.72e-09 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 58.64 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 10 KILEIIGDIIRVQVPDTAHQQEnsprfgdlaVVENSDGSLsLAQVINLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVT 89
Cdd:PRK04192 6 KIVRVSGPLVVAEGMGGARMYE---------VVRVGEEGL-IGEIIRIEGDKATIQVYEETSGIKPGEPVEFTGEPLSVE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 90 YSENILGRVFRG-----------TGEPIDGG---PELSQD------PKVTIG--------------GPSVN--------- 126
Cdd:PRK04192 76 LGPGLLGSIFDGiqrpldelaekSGDFLERGvyvPALDREkkweftPTVKVGdkveagdilgtvqeTPSIEhkimvppgv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 127 --------------------------------------PMRR-ILASKMIRTNVPM------IDIFNCLVESQK--IPif 159
Cdd:PRK04192 156 sgtvkeivsegdytvddtiavlededgegveltmmqkwPVRRpRPYKEKLPPVEPLitgqrvIDTFFPVAKGGTaaIP-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 160 svsGepfnPF----------LARigvQADADIVVFGGLGlifddyyffrqafEDAG----VF----------------SR 209
Cdd:PRK04192 234 ---G----PFgsgktvtqhqLAK---WADADIVIYVGCG-------------ERGNemteVLeefpelidpktgrplmER 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 210 TVMFVNLASDPIVERMLIPDMALAVAEHFAvEEGKRVLvLLSDMTA-FADALKEISISMDQVPANRGYPGDLYSQLARRY 288
Cdd:PRK04192 291 TVLIANTSNMPVAAREASIYTGITIAEYYR-DMGYDVL-LMADSTSrWAEALREISGRLEEMPGEEGYPAYLASRLAEFY 368
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1233828039 289 EKAadyaqG---------GSVTVLTVTTMPGDDVTHPVPDNT 321
Cdd:PRK04192 369 ERA-----GrvktlggeeGSVTIIGAVSPPGGDFSEPVTQNT 405
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
42-331 |
1.50e-07 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 53.53 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 42 VENSDGSLSLAQviNLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGgpelsqdpkvtiG 121
Cdd:PRK09281 53 LEFPGGVYGIAL--NLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDG------------K 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 122 GPSVNPMRRilaskmirtnvpmidifncLVESQKIPIF---SVSgEPFNpflarIGVQA-DADIVVfgGLG---LIFDDy 194
Cdd:PRK09281 119 GPIEATETR-------------------PVERKAPGVIdrkSVH-EPLQ-----TGIKAiDAMIPI--GRGqreLIIGD- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 195 yffRQ--------------------------------------AFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAE 236
Cdd:PRK09281 171 ---RQtgktaiaidtiinqkgkdviciyvaigqkastvaqvvrKLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 237 HFaVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGD---LYSQLARRYEKAADYAQGGSVTVLTVT-TMPGdD 312
Cdd:PRK09281 248 YF-MDNGKDALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDvfyLHSRLLERAAKLSDELGGGSLTALPIIeTQAG-D 325
|
330
....*....|....*....
gi 1233828039 313 VTHPVPDNTGYITEGQFYL 331
Cdd:PRK09281 326 VSAYIPTNVISITDGQIFL 344
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
41-331 |
6.04e-07 |
|
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: 51.58 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 41 VVENSDGSLSLAQviNLKEDTVALQVFKGTKGISTDSSVSFLGHPMKVTYSENILGRVFRGTGEPIDGGPElsqdpkvtI 120
Cdd:COG0056 52 LLEFPGGVYGMAL--NLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGP--------I 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 121 GGPSVNPMRRILASKMIRTNV--PM------ID----------------------------IFNclvesQK----IPIFs 160
Cdd:COG0056 122 EAEERRPVERPAPGVIDRQPVhePLqtgikaIDamipigrgqreliigdrqtgktaiaidtIIN-----QKgkdvICIY- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 161 VSgepfnpflarIGVQAD--ADIVvfgglglifddyyffrQAFEDAGVFSRTVMFVNLASDPIVERMLIPDMALAVAEHF 238
Cdd:COG0056 196 VA----------IGQKAStvAQVV----------------ETLEEHGAMEYTIVVAATASDPAPLQYIAPYAGCAMGEYF 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 239 AvEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGD---LYSQLARRYEKAADYAQGGSVTVL-TVTTMPGdDVT 314
Cdd:COG0056 250 M-DQGKDVLIVYDDLSKHAVAYRELSLLLRRPPGREAYPGDvfyLHSRLLERAAKLSDELGGGSLTALpIIETQAG-DVS 327
|
330
....*....|....*..
gi 1233828039 315 HPVPDNTGYITEGQFYL 331
Cdd:COG0056 328 AYIPTNVISITDGQIFL 344
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
10-321 |
1.14e-06 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 50.81 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 10 KILEIIGDIIRVQVPDtahqqENSPRFGDLAVVENSDGSLSLAQVI--------NLKEDTVALQvfkGTKGISTDSSVSF 81
Cdd:CHL00060 18 RITQIIGPVLDVAFPP-----GKMPNIYNALVVKGRDTAGQEINVTcevqqllgNNRVRAVAMS---ATDGLMRGMEVID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 82 LGHPMKVTYSENILGRVFRGTGEPIDGGPELSQDPKVTIGGPSvnPMRRILASK--MIRTNVPMIDIFNCLVESQKIPIF 159
Cdd:CHL00060 90 TGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA--PAFIQLDTKlsIFETGIKVVDLLAPYRRGGKIGLF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 160 SVSG--------EPFNPFlarigVQADADIVVFGGLGLI----FDDYyffrQAFEDAGVF-------SRTVMFVNLASDP 220
Cdd:CHL00060 168 GGAGvgktvlimELINNI-----AKAHGGVSVFGGVGERtregNDLY----MEMKESGVIneqniaeSKVALVYGQMNEP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 221 IVERMLIPDMALAVAEHFAVEEGKRVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKAADYAQgGSV 300
Cdd:CHL00060 239 PGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKE-GSI 317
|
330 340
....*....|....*....|.
gi 1233828039 301 TVLTVTTMPGDDVTHPVPDNT 321
Cdd:CHL00060 318 TSIQAVYVPADDLTDPAPATT 338
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
11-83 |
5.44e-06 |
|
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: 44.07 E-value: 5.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1233828039 11 ILEIIGDIIRVQVPdtahqQENSPRFGDLAVVENSD-GSLSLAQVINLKEDTVALQVFKGTKGISTDSSVSFLG 83
Cdd:pfam02874 1 IVQVIGPVVDVEFG-----IGRLPGLLNALEVELVEfGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
8-84 |
1.36e-05 |
|
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: 43.07 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 8 YSKILEIIGDIIRVQVPdtahqqeNSPRFGDLAVVENSDGSLSL---AQVINLKEDTVALQVFKGTKGISTDSSVSFLGH 84
Cdd:cd01426 1 KGRVIRVNGPLVEAELE-------GEVAIGEVCEIERGDGNNETvlkAEVIGFRGDRAILQLFESTRGLSRGALVEPTGR 73
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
7-83 |
1.55e-05 |
|
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the 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 FliI ATPase is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of F1-ATP synthase. Although they both are proton driven rotary molecular devices, 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: 349741 [Multi-domain] Cd Length: 70 Bit Score: 42.51 E-value: 1.55e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1233828039 7 RYSKILEIIGDIIRVQVPDTahqqenspRFGDLAVVENSDGSLSLAQVINLKEDTVALQVFKGTKGISTDSSVSFLG 83
Cdd:cd18117 1 VYGRVVRVVGLLLEAVGPQA--------PIGELCLIETADGLSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLG 69
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
212-452 |
2.79e-05 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 46.50 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 212 MFVNLASDPIVERMLIPDMALAVAEHFAVEEGkrVLVLLSDMTAFADALKEISISMDQVPANRGYPGDLYSQLARRYEKA 291
Cdd:PRK07165 203 IIIDAPSTSPYEQYLAPYVAMAHAENISYNDD--VLIVFDDLTKHANIYREIALLTNKPVGKEAFPGDMFFAHSKLLERA 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 292 ADYAQGGSVTVLTVTTMPGDDVTHPVPDNTGYITEGQFYLH-----DGKL---DPFGSLSRLKQNVIGKVTREDHGQImN 363
Cdd:PRK07165 281 GKFKNRKTITALPILQTVDNDITSLISSNIISITDGQIVTSsdlfaSGKLpaiDIDLSVSRTGSSVQSKTITKVAGEI-S 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1233828039 364 TMIRFYsgatdaeQKQA----MAFDLSEYDHKLLKFGELFQTRFMDINVSLALEQALDL-----AWQTLSECFEPQELLM 434
Cdd:PRK07165 360 KIYRAY-------KRQLklsmLDYDLNKETSDLLFKGKMIEKMFNQKGFSLYSYRFVLLiskliSWGLLKDVKDEQKALD 432
|
250
....*....|....*...
gi 1233828039 435 kqaLINKYFPKKLESKSV 452
Cdd:PRK07165 433 ---FIDYLIENDPDAKKI 447
|
|
| |
