|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
1-434 |
0e+00 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 814.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 1 MTHLQEETLLIHQWRPYRECGILSRISGSLLEAQGLSACLGELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIG 80
Cdd:PRK05922 1 MTHLQEEKLLIHQWQPYRECGLLSRVSGNLLEAQGLSACLGELCQISLSKSPPILAEVIGFHNRTTLLMSLSPIHYVALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 81 AEVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRV 160
Cdd:PRK05922 81 AEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPKTHLKPLFSSPPSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 161 GIFSEPGGGKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAE 240
Cdd:PRK05922 161 GVFSEPGSGKSSLLSTIAKGSKSTINVIALIGERGREVREYIEQHKEGLAAQRTIIIASPAHETAPTKVIAGRAAMTIAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 241 YFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYANHPDIFTD 320
Cdd:PRK05922 241 YFRDQGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASVFHHVSEFTERAGNNDKGSITALYAILHYPNHPDIFTD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 321 YVKSLLDGHFFLSPQEKSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAI 400
Cdd:PRK05922 321 YLKSLLDGHFFLTPQGKALASPPIDILTSLSRSARQLALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAHLDRAV 400
|
410 420 430
....*....|....*....|....*....|....
gi 497559136 401 RLLPSVKQFLSQPYSHYSAIHETIEQLCQLLKHE 434
Cdd:PRK05922 401 KLLPSIKQFLSQPLSSYCALHNTLKQLEALLKHE 434
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
1-431 |
4.75e-177 |
|
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: 501.48 E-value: 4.75e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 1 MTHLQEETLLIHQWRPYRECGILSRISGSLLEAQGLSACLGELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIG 80
Cdd:COG1157 1 LDRLARLLARLEELPPVRVSGRVTRVVGLLIEAVGPDASIGELCEIETADGRPVLAEVVGFRGDRVLLMPLGDLEGISPG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 81 AEVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRV 160
Cdd:COG1157 81 ARVVPTGRPLSVPVGDGLLGRVLDGLGRPLDGKGPLPGEERRPLDAPPPNPLERARITEPLDTGVRAIDGLLTVGRGQRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 161 GIFSEPGGGKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQH--KEGLAaqRTVIIASTAYETAASKVIAGRAAITI 238
Cdd:COG1157 161 GIFAGSGVGKSTLLGMIARNTEADVNVIALIGERGREVREFIEDDlgEEGLA--RSVVVVATSDEPPLMRLRAAYTATAI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 239 AEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYA-NHPDI 317
Cdd:COG1157 239 AEYFRDQGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSITAFYTVLVEGdDMNDP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 318 FTDYVKSLLDGHFFLSPQ--EKS-FssPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDA 394
Cdd:COG1157 319 IADAVRGILDGHIVLSRKlaERGhY--PAIDVLASISRVMPDIVSPEHRALARRLRRLLARYEENEDLIRIGAYQPGSDP 396
|
410 420 430
....*....|....*....|....*....|....*..
gi 497559136 395 HLDRAIRLLPSVKQFLSQPYSHYSAIHETIEQLCQLL 431
Cdd:COG1157 397 ELDEAIALIPAIEAFLRQGMDERVSFEESLAQLAELL 433
|
|
| III_secr_ATP |
TIGR02546 |
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and ... |
15-431 |
4.29e-176 |
|
type III secretion apparatus H+-transporting two-sector ATPase; [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274191 [Multi-domain] Cd Length: 422 Bit Score: 498.77 E-value: 4.29e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 15 RPYRECGILSRISGSLLEAQGLSACLGELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPL 94
Cdd:TIGR02546 1 QPVRVRGRVTEVSGTLLKAVLPGARVGELCLIRRRDPSQLLAEVVGFTGDEALLSPLGELHGISPGSEVIPTGRPLSIRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 95 SNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSS--PMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSS 172
Cdd:TIGR02546 81 GEALLGRVLDGFGRPLDGKGELPAGEIETRPLDADPppPMSRQPIDQPLPTGVRAIDGLLTCGEGQRIGIFAGAGVGKST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 173 LLSTIAKGSQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFT 252
Cdd:TIGR02546 161 LLGMIARGASADVNVIALIGERGREVREFIEHHLGEEGRKRSVLVVSTSDRPSLERLKAAYTATAIAEYFRDQGKRVLLM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 253 MDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYA-NHPDIFTDYVKSLLDGHFF 331
Cdd:TIGR02546 241 MDSLTRFARALREIGLAAGEPPARGGYPPSVFSSLPRLLERAGNGEKGSITALYTVLVEGdDMNDPIADEVRSILDGHIV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 332 LSP-QEKSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFL 410
Cdd:TIGR02546 321 LSRaLAERNHYPAIDVLASLSRVMSQVVSTEHRRAAGKLRRLLATYKEVELLIRLGEYQPGSDPETDDAIDKIDAIRAFL 400
|
410 420
....*....|....*....|.
gi 497559136 411 SQPYSHYSAIHETIEQLCQLL 431
Cdd:TIGR02546 401 RQSTDEYSPYEETLEQLHALV 421
|
|
| FliI_clade1 |
TIGR03496 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
21-427 |
4.27e-131 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274607 [Multi-domain] Cd Length: 411 Bit Score: 383.75 E-value: 4.27e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 21 GILSRISGSLLEAQGLSACLGELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLLG 100
Cdd:TIGR03496 1 GRVTRVVGLVLEAVGLRAPVGSRCEIESSDGDPIEAEVVGFRGDRVLLMPLEDVEGLRPGARVFPLGGPLRLPVGDSLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 101 RVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKG 180
Cdd:TIGR03496 81 RVIDGLGRPLDGKGPLDAGERVPLYAPPINPLKRAPIDEPLDVGVRAINGLLTVGRGQRMGIFAGSGVGKSTLLGMMARY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 181 SQQTINVIALIGERGREVRDYVNQH--KEGLAaqRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSR 258
Cdd:TIGR03496 161 TEADVVVVGLIGERGREVKEFIEDIlgEEGLA--RSVVVAATADESPLMRLRAAFYATAIAEYFRDQGKDVLLLMDSLTR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 259 WIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGN--NDKGSITSFYAILhyA---NHPDIFTDYVKSLLDGHFFLS 333
Cdd:TIGR03496 239 FAMAQREIALAIGEPPATKGYPPSVFAKLPQLVERAGNgeEGKGSITAFYTVL--VegdDQQDPIADAARAILDGHIVLS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 334 PQEKSFSS-PPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQ 412
Cdd:TIGR03496 317 RELAEQGHyPAIDILASISRVMPDVVSPEHRQAARRFKQLLSRYQENRDLISIGAYQAGSDPELDQAIALYPRIEAFLQQ 396
|
410
....*....|....*
gi 497559136 413 PYSHYSAIHETIEQL 427
Cdd:TIGR03496 397 GMRERASFEESLEAL 411
|
|
| FliI_clade2 |
TIGR03497 |
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of ... |
21-431 |
3.20e-126 |
|
flagellar protein export ATPase FliI; Members of this protein family are the FliI protein of bacterial flagellum systems. This protein acts to drive protein export for flagellar biosynthesis. The most closely related family is the YscN family of bacterial type III secretion systems. This model represents one (of three) segment of the FliI family tree. These have been modeled separately in order to exclude the type III secretion ATPases more effectively. [Cellular processes, Chemotaxis and motility]
Pssm-ID: 274608 [Multi-domain] Cd Length: 413 Bit Score: 371.64 E-value: 3.20e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 21 GILSRISGSLLEAQGLSACLGELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLLG 100
Cdd:TIGR03497 1 GKVTRVIGLTIESKGPKASIGELCSILTKGGKPVLAEVVGFKEENVLLMPLGEVEGIGPGSLVIATGRPLAIKVGKGLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 101 RVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKG 180
Cdd:TIGR03497 81 RVLDGLGRPLDGEGPIIGEEPYPLDNPPPNPLKRPRIRDPLETGIKAIDGLLTIGKGQRVGIFAGSGVGKSTLLGMIARN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 181 SQQTINVIALIGERGREVRDYVNQH--KEGLAaqRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSR 258
Cdd:TIGR03497 161 AKADINVIALIGERGREVRDFIEKDlgEEGLK--RSVVVVATSDQPALMRLKAAFTATAIAEYFRDQGKDVLLMMDSVTR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 259 WIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYA---NHPdiFTDYVKSLLDGHFFLSPQ 335
Cdd:TIGR03497 239 FAMAQREIGLAVGEPPTTRGYTPSVFSLLPKLLERSGNSQKGSITGFYTVLVDGddmNEP--IADAVRGILDGHIVLSRE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 336 --EKSfSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQP 413
Cdd:TIGR03497 317 laAKN-HYPAIDVLASVSRVMNEIVSEEHKELAGKLRELLAVYKEAEDLINIGAYKRGSNPKIDEAIRYIEKINSFLKQG 395
|
410
....*....|....*...
gi 497559136 414 YSHYSAIHETIEQLCQLL 431
Cdd:TIGR03497 396 IDEKFTFEETVQLLKELL 413
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
11-434 |
3.51e-109 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 328.99 E-value: 3.51e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 11 IHQWRPYRECGILSRISGSLLEAQGLSACLGELCQISLS--RSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRR 88
Cdd:PRK07721 10 IETLDPYKRYGKVSRVIGLMIESKGPESSIGDVCYIHTKggGDKAIKAEVVGFKDEHVLLMPYTEVAEIAPGCLVEATGK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 89 PASLPLSNHLLGRVLDGFGNPLDGgSQLPKTnLSPLFSSPS--SPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEP 166
Cdd:PRK07721 90 PLEVKVGSGLIGQVLDALGEPLDG-SALPKG-LAPVSTDQDppNPLKRPPIREPMEVGVRAIDSLLTVGKGQRVGIFAGS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 167 GGGKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQH--KEGLAaqRTVIIASTAYETAASKVIAGRAAITIAEYFRD 244
Cdd:PRK07721 168 GVGKSTLMGMIARNTSADLNVIALIGERGREVREFIERDlgPEGLK--RSIVVVATSDQPALMRIKGAYTATAIAEYFRD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 245 QGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAIL---HYANHPdiFTDY 321
Cdd:PRK07721 246 QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLvdgDDMNEP--IADT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 322 VKSLLDGHFFLSPQ--EKSfSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRA 399
Cdd:PRK07721 324 VRGILDGHFVLDRQlaNKG-QYPAINVLKSVSRVMNHIVSPEHKEAANRFRELLSTYQNSEDLINIGAYKRGSSREIDEA 402
|
410 420 430
....*....|....*....|....*....|....*
gi 497559136 400 IRLLPSVKQFLSQPYSHYSAIHETIEQLCQLLKHE 434
Cdd:PRK07721 403 IQFYPQIISFLKQGTDEKATFEESIQALLSLFGKG 437
|
|
| fliI_yscN |
TIGR01026 |
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP ... |
15-431 |
3.69e-109 |
|
ATPase, FliI/YscN family; This family of ATPases demonstrates extensive homology with ATP synthase F1, beta subunit. It is a mixture of members with two different protein functions. The first group is exemplified by Salmonella typhimurium FliI protein. It is needed for flagellar assembly, its ATPase activity is required for flagellation, and it may be involved in a specialized protein export pathway that proceeds without signal peptide cleavage. The second group of proteins function in the export of virulence proteins; exemplified by Yersinia sp. YscN protein an ATPase involved in the type III secretory pathway for the antihost Yops proteins. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 273401 [Multi-domain] Cd Length: 440 Bit Score: 328.95 E-value: 3.69e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 15 RPYRECGILSRISGSLLEAQGLSACLGELCQISLSRSDP-ILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLP 93
Cdd:TIGR01026 19 RLVKRVGRVTKVKGLLIEAVGPQASVGDLCLIERRGSEGrLVAEVVGFNGEFVFLMPYEEVEGVRPGSKVLATGEGLSIK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 94 LSNHLLGRVLDGFGNPLDG-GSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSS 172
Cdd:TIGR01026 99 VGDGLLGRVLDGLGKPIDGkGKFLDNVETEGLITAPINPLKRAPIREILSTGVRSIDGLLTVGKGQRIGIFAGSGVGKST 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 173 LLSTIAKGSQQTINVIALIGERGREVRDYV--NQHKEGLAaqRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVL 250
Cdd:TIGR01026 179 LLGMIARNTEADVNVIALIGERGREVREFIehDLGEEGLK--RSVVVVATSDQSPLLRLKGAYVATAIAEYFRDQGKDVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 251 FTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYA---NHPdiFTDYVKSLLD 327
Cdd:TIGR01026 257 LLMDSVTRFAMAQREIGLAAGEPPATKGYTPSVFSTLPRLLERAGASGKGSITAFYTVLVEGddmNEP--IADSVRGILD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 328 GHFFLS---PQEKSFssPPINVLTSLSRSSRQLALPHHYAAA---QELLSLLKAYHeaiDIIQLGAYVSGQDAHLDRAIR 401
Cdd:TIGR01026 335 GHIVLSralAQRGHY--PAIDVLASISRLMTAIVSEEHRRAArkfRELLSKYKDNE---DLIRIGAYQRGSDRELDFAIA 409
|
410 420 430
....*....|....*....|....*....|
gi 497559136 402 LLPSVKQFLSQPYSHYSAIHETIEQLCQLL 431
Cdd:TIGR01026 410 KYPKLERFLKQGINEKVNFEESLQQLEEIF 439
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
91-353 |
8.04e-108 |
|
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: 319.12 E-value: 8.04e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 91 SLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGK 170
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLDGKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 171 SSLLSTIAKGSQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVL 250
Cdd:cd01136 81 STLLGMIARNTDADVNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRDQGKKVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 251 FTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYANHP-DIFTDYVKSLLDGH 329
Cdd:cd01136 161 LLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFnDPIADEVRSILDGH 240
|
250 260
....*....|....*....|....*.
gi 497559136 330 FFLSPQ--EKSfSSPPINVLTSLSRS 353
Cdd:cd01136 241 IVLSRRlaERG-HYPAIDVLASISRV 265
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
21-431 |
4.34e-103 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 313.29 E-value: 4.34e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 21 GILSRISGSLLEAQGLSACLGELCQISLSRsdpILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLLG 100
Cdd:PRK06820 31 GPIVEIGPTLLRASLPGVAQGELCRIEPQG---MLAEVVSIEQEMALLSPFASSDGLRCGQWVTPLGHMHQVQVGADLAG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 101 RVLDGFGNPLDGGSQLpKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKG 180
Cdd:PRK06820 108 RILDGLGAPIDGGPPL-TGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGMLCAD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 181 SQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRWI 260
Cdd:PRK06820 187 SAADVMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRDRGKKVLLMADSLTRYA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 261 ESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAIL---HYANHPdiFTDYVKSLLDGHFFLSPQ-E 336
Cdd:PRK06820 267 RAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLvegDDMNEP--VADEVRSLLDGHIVLSRRlA 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 337 KSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQPYSH 416
Cdd:PRK06820 345 GAGHYPAIDIAASVSRIMPQIVSAGQLAMAQKLRRMLACYQEIELLVRVGEYQAGEDLQADEALQRYPAICAFLQQDHSE 424
|
410
....*....|....*
gi 497559136 417 YSAIHETIEQLCQLL 431
Cdd:PRK06820 425 TAHLETTLEHLAQVV 439
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
17-431 |
1.33e-99 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 304.18 E-value: 1.33e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 17 YRECGILSRISGSLLEAQGLSACLGELCQIslsRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSN 96
Cdd:PRK07594 19 YCRWGRIQDVSATLLNAWLPGVFMGELCCI---KPGEELAEVVGINGSKALLSPFTSTIGLHCGQQVMALRRRHQVPVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 97 HLLGRVLDGFGNPLDGgSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLST 176
Cdd:PRK07594 96 ALLGRVIDGFGRPLDG-RELPDVCWKDYDAMPPPAMVRQPITQPLMTGIRAIDSVATCGEGQRVGIFSAPGVGKSTLLAM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 177 IAKGSQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSL 256
Cdd:PRK07594 175 LCNAPDADSNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPALERVRALFVATTIAEFFRDNGKRVVLLADSL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 257 SRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYA---NHPdiFTDYVKSLLDGHFFLS 333
Cdd:PRK07594 255 TRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITAFYTVLVEGddmNEP--LADEVRSLLDGHIVLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 334 PQ-EKSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQ 412
Cdd:PRK07594 333 RRlAERGHYPAIDVLATLSRVFPVVTSHEHRQLAAILRRCLALYQEVELLIRIGEYQRGVDTDTDKAIDTYPDICTFLRQ 412
|
410
....*....|....*....
gi 497559136 413 PYSHYSAIHETIEQLCQLL 431
Cdd:PRK07594 413 SKDEVCGPELLIEKLHQIL 431
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
18-430 |
5.36e-98 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 300.53 E-value: 5.36e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 18 RECGILSRISGSLLEAQGLSACLGELCQIsLSRSDPIL--AEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLS 95
Cdd:PRK09099 23 RRTGKVVEVIGTLLRVSGLDVTLGELCEL-RQRDGTLLqrAEVVGFSRDVALLSPFGELGGLSRGTRVIGLGRPLSVPVG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 96 NHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLS 175
Cdd:PRK09099 102 PALLGRVIDGLGEPIDGGGPLDCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDGLMTLGEGQRMGIFAPAGVGKSTLMG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 176 TIAKGSQQTINVIALIGERGREVRDYVNQ--HKEGLAaqRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTM 253
Cdd:PRK09099 182 MFARGTQCDVNVIALIGERGREVREFIELilGEDGMA--RSVVVCATSDRSSIERAKAAYVATAIAEYFRDRGLRVLLMM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 254 DSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYANH-PDIFTDYVKSLLDGHFFL 332
Cdd:PRK09099 260 DSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALYTVLAEDESgSDPIAEEVRGILDGHMIL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 333 SPQEKSFSS-PPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLS 411
Cdd:PRK09099 340 SREIAARNQyPAIDVLGSLSRVMPQVVPREHVQAAGRLRQLLAKHREVETLLQVGEYRAGSDPVADEAIAKIDAIRDFLS 419
|
410
....*....|....*....
gi 497559136 412 QPYSHYSAIHETIEQLCQL 430
Cdd:PRK09099 420 QRTDEYSDPDATLAALAEL 438
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
1-430 |
2.63e-95 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 293.20 E-value: 2.63e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 1 MTHLQEEtlLIHQWRPYRECGILSRISGSLLEAQGLSACLGELCQISLSRSD-PILAEVIGIHNRTTLLLALTPIYYLAI 79
Cdd:PRK06936 7 IPHHLRH--AIVGSRLIQIRGRVTQVTGTILKAVVPGVRIGELCYLRNPDNSlSLQAEVIGFAQHQALLTPLGEMYGISS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 80 GAEVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQR 159
Cdd:PRK06936 85 NTEVSPTGTMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWYPVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 160 VGIFSEPGGGKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQH--KEGLaaQRTVIIASTAYETAASKVIAGRAAIT 237
Cdd:PRK06936 165 MGIFAAAGGGKSTLLASLIRSAEVDVTVLALIGERGREVREFIESDlgEEGL--RKAVLVVATSDRPSMERAKAGFVATS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 238 IAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAILHYA---NH 314
Cdd:PRK06936 243 IAEYFRDQGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGddmTE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 315 PdiFTDYVKSLLDGHFFLSPQ-EKSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQD 393
Cdd:PRK06936 323 P--VADETRSILDGHIILSRKlAAANHYPAIDVLRSASRVMNQIVSKEHKTWAGRLRELLAKYEEVELLLQIGEYQKGQD 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 497559136 394 AHLDRAIRLLPSVKQFLSQPYSHYSAIHETIEQLCQL 430
Cdd:PRK06936 401 KEADQAIERIGAIRGFLRQGTHELSHFNETLNLLETL 437
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
21-432 |
1.01e-90 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 282.00 E-value: 1.01e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 21 GILSRISGSLLEAQGLSACLGELCQISLSRS---DPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNH 97
Cdd:PRK05688 29 GRLLRMVGLTLEAEGLRAAVGSRCLVINDDSyhpVQVEAEVMGFSGDKVFLMPVGSVAGIAPGARVVPLADTGRLPMGMS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 98 LLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTI 177
Cdd:PRK05688 109 MLGRVLDGAGRALDGKGPMKAEDWVPMDGPTINPLNRHPISEPLDVGIRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMM 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 178 AKGSQQTINVIALIGERGREVRDYVNQ--HKEGLAaqRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDS 255
Cdd:PRK05688 189 TRFTEADIIVVGLIGERGREVKEFIEHilGEEGLK--RSVVVASPADDAPLMRLRAAMYCTRIAEYFRDKGKNVLLLMDS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 256 LSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDK--GSITSFYAILHYA-NHPDIFTDYVKSLLDGHFFL 332
Cdd:PRK05688 267 LTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPggGSITAFYTVLSEGdDQQDPIADSARGVLDGHIVL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 333 S---PQEKSFssPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQF 409
Cdd:PRK05688 347 SrrlAEEGHY--PAIDIEASISRVMPQVVDPEHLRRAQRFKQLWSRYQQSRDLISVGAYVAGGDPETDLAIARFPHLVQF 424
|
410 420
....*....|....*....|...
gi 497559136 410 LSQPYSHYSAIHETIEQLCQLLK 432
Cdd:PRK05688 425 LRQGLRENVSLAQSREQLAAIFA 447
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
2-432 |
3.12e-90 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 280.43 E-value: 3.12e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 2 THLQEETLLIHQWRPYREcGILSRISGSLLEAQGLSACLGELCQISLSRSDpILAEVIGIHNRTTLLLALTPIYYLAIGA 81
Cdd:PRK08972 9 NRLKQYKVKVPPFRAVAS-GKLVRVVGLTLEATGCRAPVGSLCSIETMAGE-LEAEVVGFDGDLLYLMPIEELRGVLPGA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 82 EVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVG 161
Cdd:PRK08972 87 RVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRASRHSPPINPLSRRPITEPLDVGVRAINAMLTVGKGQRMG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 162 IFSEPGGGKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQ--HKEGLaaQRTVIIASTAYETAASKVIAGRAAITIA 239
Cdd:PRK08972 167 LFAGSGVGKSVLLGMMTRGTTADVIVVGLVGERGREVKEFIEEilGEEGR--ARSVVVAAPADTSPLMRLKGCETATTIA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 240 EYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGN--NDKGSITSFYAILHYANH-PD 316
Cdd:PRK08972 245 EYFRDQGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAGNggPGQGSITAFYTVLTEGDDlQD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 317 IFTDYVKSLLDGHFFLSPQ-EKSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAH 395
Cdd:PRK08972 325 PIADASRAILDGHIVLSRElADSGHYPAIDIEASISRVMPMVISEEHLEAMRRVKQVYSLYQQNRDLISIGAYKQGSDPR 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 497559136 396 LDRAIRLLPSVKQFLSQPYSHYSAIHETIEQLCQLLK 432
Cdd:PRK08972 405 IDNAIRLQPAMNAFLQQTMKEAVPYDMSVNMLKQLAA 441
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
24-427 |
1.26e-86 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 270.71 E-value: 1.26e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 24 SRISGSLLEAQGLSACLGELCQI--SLSRSDPI-LAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLLG 100
Cdd:PRK08149 11 LRIQGPIIEAELPDVAIGEICEIraGWHSNEVIaRAQVVGFQRERTILSLIGNAQGLSRQVVLKPTGKPLSVWVGEALLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 101 RVLDGFGNPLDGGSQ----LPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLST 176
Cdd:PRK08149 91 AVLDPTGKIVERFDApptvGPISEERVIDVAPPSYAERRPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 177 IAKGSQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSL 256
Cdd:PRK08149 171 LIEHSEADVFVIGLIGERGREVTEFVESLRASSRREKCVLVYATSDFSSVDRCNAALVATTVAEYFRDQGKRVVLFIDSM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 257 SRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAIL-HYANHPDIFTDYVKSLLDGHFFLSPQ 335
Cdd:PRK08149 251 TRYARALRDVALAAGELPARRGYPASVFDSLPRLLERPGATLAGSITAFYTVLlESEEEPDPIGDEIRSILDGHIYLSRK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 336 -EKSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQPY 414
Cdd:PRK08149 331 lAAKGHYPAIDVLKSVSRVFGQVTDPKHRQLAAAFRKLLTRLEELQLFIDLGEYRRGENADNDRAMDKRPALEAFLKQDV 410
|
410
....*....|...
gi 497559136 415 SHYSAIHETIEQL 427
Cdd:PRK08149 411 AEKSSFSDTLERL 423
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
21-432 |
5.24e-85 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 266.55 E-value: 5.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 21 GILSRISGSLLEAQGLSACLGELCQI-SLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLL 99
Cdd:PRK08472 20 GSITKISPTIIEADGLNPSVGDIVKIeSSDNGKECLGMVVVIEKEQFGISPFSFIEGFKIGDKVFISKEGLNIPVGRNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 100 GRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAK 179
Cdd:PRK08472 100 GRVVDPLGRPIDGKGAIDYERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLMGMIVK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 180 GSQQTINVIALIGERGREVRDYVnQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRW 259
Cdd:PRK08472 180 GCLAPIKVVALIGERGREIPEFI-EKNLGGDLENTVIVVATSDDSPLMRKYGAFCAMSVAEYFKNQGLDVLFIMDSVTRF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 260 IESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNND-KGSITSFYAILHYANH-PDIFTDYVKSLLDGHFFLSPQEK 337
Cdd:PRK08472 259 AMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDmSDPIADQSRSILDGHIVLSRELT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 338 SFS-SPPINVLTSLSRSSRQLALPHHYAAAQE---LLSLLKayhEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQP 413
Cdd:PRK08472 339 DFGiYPPINILNSASRVMNDIISPEHKLAARKfkrLYSLLK---ENEVLIRIGAYQKGNDKELDEAISKKEFMEQFLKQN 415
|
410
....*....|....*....
gi 497559136 414 YSHYSAIHETIEQLCQLLK 432
Cdd:PRK08472 416 PNELFPFEQTFEQLEEILR 434
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
11-431 |
8.87e-84 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 264.34 E-value: 8.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 11 IHQWRPYRECGILSRISGSLLEAQGLSACLGELCQISL---SRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEV---- 83
Cdd:PRK07960 19 MAQLPAVRRYGRLTRATGLVLEATGLQLPLGATCVIERqngSETHEVESEVVGFNGQRLFLMPLEEVEGILPGARVyarn 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 84 VPLRRPAS---LPLSNHLLGRVLDGFGNPLDGgsqLPKTNLSPLFSSPSSP---MSRTPIQEVFPTGIRAIDALLTIGEG 157
Cdd:PRK07960 99 ISGEGLQSgkqLPLGPALLGRVLDGSGKPLDG---LPAPDTGETGALITPPfnpLQRTPIEHVLDTGVRAINALLTVGRG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 158 QRVGIFSEPGGGKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQ--HKEGLAaqRTVIIASTAYETAASKVIAGRAA 235
Cdd:PRK07960 176 QRMGLFAGSGVGKSVLLGMMARYTQADVIVVGLIGERGREVKDFIENilGAEGRA--RSVVIAAPADVSPLLRMQGAAYA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 236 ITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGN--NDKGSITSFYAILHYA- 312
Cdd:PRK07960 254 TRIAEDFRDRGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYTVLTEGd 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 313 NHPDIFTDYVKSLLDGHFFLSPQ-EKSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSG 391
Cdd:PRK07960 334 DQQDPIADSARAILDGHIVLSRRlAEAGHYPAIDIEASISRAMTALIDEQHYARVRQFKQLLSSFQRNRDLVSVGAYAKG 413
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 497559136 392 QDAHLDRAIRLLPSVKQFLSQPYSHYSAIHETIEQLCQLL 431
Cdd:PRK07960 414 SDPMLDKAIALWPQLEAFLQQGIFERADWEDSLQALERIF 453
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
144-351 |
1.68e-83 |
|
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: 254.97 E-value: 1.68e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 144 GIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYE 223
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASADVVVYALIGERGREVREFIEELLGSGALKRTVVVVATSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 224 TAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGN--NDKGS 301
Cdd:pfam00006 81 PPLARYRAPYTALTIAEYFRDQGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRvkGKGGS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497559136 302 ITSFYAILHYA-NHPDIFTDYVKSLLDGHFFLSPqeKSFSS---PPINVLTSLS 351
Cdd:pfam00006 161 ITALPTVLVPGdDITDPIPDNTRSILDGQIVLSR--DLAEKghyPAIDVLASVS 212
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
26-431 |
1.32e-79 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 252.98 E-value: 1.32e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 26 ISGSLLEAQGLSACL--GELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLLGRVL 103
Cdd:PRK08927 24 VRGLLVEVAGPIHALsvGARIVVETRGGRPVPCEVVGFRGDRALLMPFGPLEGVRRGCRAVIANAAAAVRPSRAWLGRVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 104 DGFGNPLDGGSQLPKTNLSPLFSSPS-SPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKGSQ 182
Cdd:PRK08927 104 NALGEPIDGKGPLPQGPVPYPLRAPPpPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGVGKSVLLSMLARNAD 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 183 QTINVIALIGERGREVRDYVNQH--KEGLAaqRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRWI 260
Cdd:PRK08927 184 ADVSVIGLIGERGREVQEFLQDDlgPEGLA--RSVVVVATSDEPALMRRQAAYLTLAIAEYFRDQGKDVLCLMDSVTRFA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 261 ESLQEVAIARGETLSTHHYAASVFHHVAEFLERA--GNNDKGSITSFYAIL-----HyaNHPdiFTDYVKSLLDGHFFLs 333
Cdd:PRK08927 262 MAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLvdgddH--NEP--VADAVRGILDGHIVM- 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 334 pqEKSFSS----PPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQF 409
Cdd:PRK08927 337 --ERAIAErgryPAINVLKSVSRTMPGCNDPEENPLVRRARQLMATYADMEELIRLGAYRAGSDPEVDEAIRLNPALEAF 414
|
410 420
....*....|....*....|..
gi 497559136 410 LSQPYSHYSAIHETIEQLCQLL 431
Cdd:PRK08927 415 LRQGKDEATSLAEGYARLAQIL 436
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
18-431 |
1.50e-75 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 242.10 E-value: 1.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 18 RECGILSRISGSLLEAQGLSACLGELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNH 97
Cdd:PRK07196 16 RVAGRLVRVTGLLLESVGCRLAIGQRCRIESVDETFIEAQVVGFDRDITYLMPFKHPGGVLGGARVFPSEQDGELLIGDS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 98 LLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTI 177
Cdd:PRK07196 96 WLGRVINGLGEPLDGKGQLGGSTPLQQQLPQIHPLQRRAVDTPLDVGVNAINGLLTIGKGQRVGLMAGSGVGKSVLLGMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 178 AKGSQQTINVIALIGERGREVRDYVNQ--HKEGLAaqRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDS 255
Cdd:PRK07196 176 TRYTQADVVVVGLIGERGREVKEFIEHslQAAGMA--KSVVVAAPADESPLMRIKATELCHAIATYYRDKGHDVLLLVDS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 256 LSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNND-KGSITSFYAILHYA-NHPDIFTDYVKSLLDGHFFLS 333
Cdd:PRK07196 254 LTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAGNSSgNGTMTAIYTVLAEGdDQQDPIVDCARAVLDGHIVLS 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 334 PQ-EKSFSSPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQ 412
Cdd:PRK07196 334 RKlAEAGHYPAIDISQSISRCMSQVIGSQQAKAASLLKQCYADYMAIKPLIPLGGYVAGADPMADQAVHYYPAITQFLRQ 413
|
410
....*....|....*....
gi 497559136 413 PYSHYSAIHETIEQLCQLL 431
Cdd:PRK07196 414 EVGHPALFSASVEQLTGMF 432
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
21-412 |
1.41e-69 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 227.19 E-value: 1.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 21 GILSRISGSLLEAQGLS--ACLGELCQISlSRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVV---PLR-RPAslpl 94
Cdd:PRK06002 28 GTVSEVTASHYRVRGLSrfVRLGDFVAIR-ADGGTHLGEVVRVDPDGVTVKPFEPRIEIGLGDAVFrkgPLRiRPD---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 95 sNHLLGRVLDGFGNPLDGGSQLPK-TNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSL 173
Cdd:PRK06002 103 -PSWKGRVINALGEPIDGLGPLAPgTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 174 LSTIAKGSQQTINVIALIGERGREVRDYVnqhKEGLAA--QRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLF 251
Cdd:PRK06002 182 LAMLARADAFDTVVIALVGERGREVREFL---EDTLADnlKKAVAVVATSDESPMMRRLAPLTATAIAEYFRDRGENVLL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 252 TMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAG--NNDKGSITSFYAIL-HYANHPDIFTDYVKSLLDG 328
Cdd:PRK06002 259 IVDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAGpgAEGGGSITGIFSVLvDGDDHNDPVADSIRGTLDG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 329 HFFLS---PQEKSFssPPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPS 405
Cdd:PRK06002 339 HIVLDraiAEQGRY--PAVDPLASISRLARHAWTPEQRKLVSRLKSMIARFEETRDLRLIGGYRAGSDPDLDQAVDLVPR 416
|
....*..
gi 497559136 406 VKQFLSQ 412
Cdd:PRK06002 417 IYEALRQ 423
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
16-427 |
3.98e-66 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 217.54 E-value: 3.98e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 16 PYRECGILSRISGSLLEAQGLSACLGELCQISlsrSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLS 95
Cdd:PRK06793 18 FYTKVGKVHSVQEQFFVAKGPKAKIGDVCFVG---EHNVLCEVIAIEKENNMLLPFEQTEKVCYGDSVTLIAEDVVIPRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 96 NHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLS 175
Cdd:PRK06793 95 NHLLGKVLSANGEVLNEEAENIPLQKIKLDAPPIHAFEREEITDVFETGIKSIDSMLTIGIGQKIGIFAGSGVGKSTLLG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 176 TIAKGSQQTINVIALIGERGREVRDYVNQH--KEGLaaQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTM 253
Cdd:PRK06793 175 MIAKNAKADINVISLVGERGREVKDFIRKElgEEGM--RKSVVVVATSDESHLMQLRAAKLATSIAEYFRDQGNNVLLMM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 254 DSLSRWIESLQEVAIA------RGETLSTHHYaasvfhhVAEFLERAGNNDKGSITSFYAIL---HYANHPdiFTDYVKS 324
Cdd:PRK06793 253 DSVTRFADARRSVDIAvkelpiGGKTLLMESY-------MKKLLERSGKTQKGSITGIYTVLvdgDDLNGP--VPDLARG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 325 LLDGHFFLSPQEKSFSS-PPINVLTSLSRSSRQLALPHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQD-AHLDRAIRL 402
Cdd:PRK06793 324 ILDGHIVLKRELATLSHyPAISVLDSVSRIMEEIVSPNHWQLANEMRKILSIYKENELYFKLGTIQENAEnAYIFECKNK 403
|
410 420
....*....|....*....|....*
gi 497559136 403 LPSVKQFLSQPYSHYSAIHETIEQL 427
Cdd:PRK06793 404 VEGINTFLKQGRSDSFQFDDIVEAM 428
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
91-352 |
9.29e-63 |
|
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: 203.84 E-value: 9.29e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 91 SLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGK 170
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRRPIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 171 SSLLSTIAKGSQQT---INVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGA 247
Cdd:cd19476 81 TVLAMQLARNQAKAhagVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRDNGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 248 RVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAG--NNDKGSITSFYAILHYAnhpDIFTDYV--- 322
Cdd:cd19476 161 HVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGkvKDGGGSITAIPAVSTPG---DDLTDPIpdn 237
|
250 260 270
....*....|....*....|....*....|...
gi 497559136 323 -KSLLDGHFFLSPQ--EKSFsSPPINVLTSLSR 352
Cdd:cd19476 238 tFAILDGQIVLSRElaRKGI-YPAINVLDSTSR 269
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
69-434 |
4.50e-32 |
|
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: 126.76 E-value: 4.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 69 LALTPIYYLAIGAEVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAI 148
Cdd:TIGR01039 55 IAMGSTDGLVRGLEVIDTGAPISVPVGKETLGRIFNVLGEPIDEKGPIPAKERWPIHRKAPSFEEQSTKVEILETGIKVI 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 149 DALLTIGEGQRVGIFSEPGGGKS----SLLSTIAKgSQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYET 224
Cdd:TIGR01039 135 DLLAPYAKGGKIGLFGGAGVGKTvliqELINNIAK-EHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 225 AASKVIAGRAAITIAEYFRD-QGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSIT 303
Cdd:TIGR01039 214 PGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSIT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 304 SFYAILHYAnhpDIFTDYVKSL----LDGHFFLSPQEKSFS-SPPINVLTSlsrSSRQLAlP-----HHYAAAQELLSLL 373
Cdd:TIGR01039 294 SVQAVYVPA---DDLTDPAPATtfahLDATTVLSRKIAELGiYPAVDPLDS---TSRLLD-PsvvgeEHYDVARGVQQIL 366
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497559136 374 KAYHEAIDIIQ-LGA-YVSGQD-AHLDRAIRllpsVKQFLSQPY----------SHYSAIHETIEQLCQLLKHE 434
Cdd:TIGR01039 367 QRYKELQDIIAiLGMdELSEEDkLTVERARR----IQRFLSQPFfvaevftgqpGKYVPLKDTIRGFKEILEGK 436
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
89-352 |
2.50e-31 |
|
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: 121.18 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 89 PASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGG 168
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDINGPPINPVARIYPEEMIQTGISAIDVMNTLVRGQKLPIFSGSGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 169 GKSSLLSTIA------KGSQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYF 242
Cdd:cd01135 81 PHNELAAQIArqagvvGSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERIITPRMALTTAEYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 243 R-DQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGN--NDKGSITSFyAILHYAN----H- 314
Cdd:cd01135 161 AyEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERAGRveGRKGSITQI-PILTMPNdditHp 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 497559136 315 -PDIfTDYVKsllDGHFFLSPQ-EKSFSSPPINVLTSLSR 352
Cdd:cd01135 240 iPDL-TGYIT---EGQIYLDRDlHNKGIYPPIDVLPSLSR 275
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
90-352 |
1.60e-28 |
|
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: 113.04 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 90 ASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGG 169
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKERRRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQTG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 170 KSSL-LSTI--AKGsQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFRDQG 246
Cdd:cd01132 82 KTAIaIDTIinQKG-KKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRDNG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 247 ARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAG--NNDK--GSITSFYAILHYANhpDIfTDY- 321
Cdd:cd01132 161 KHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAklSDELggGSLTALPIIETQAG--DV-SAYi 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 497559136 322 ---VKSLLDGHFFLSPqeKSFSS---PPINVLTSLSR 352
Cdd:cd01132 238 ptnVISITDGQIFLES--ELFNKgirPAINVGLSVSR 272
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
18-432 |
2.48e-27 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 113.38 E-value: 2.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 18 RECGILSRISGSLLEAQGLS-ACLGELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAI-GAEVVPLRRPASLPLS 95
Cdd:PRK04196 2 KEYRTVSEIKGPLLFVEGVEgVAYGEIVEIELPNGEKRRGQVLEVSEDKAVVQVFEGTTGLDLkDTKVRFTGEPLKLPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 96 NHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLS 175
Cdd:PRK04196 82 EDMLGRIFDGLGRPIDGGPEIIPEKRLDINGAPINPVAREYPEEFIQTGISAIDGLNTLVRGQKLPIFSGSGLPHNELAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 176 TIAK-----GSQQTINVI-ALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFR-DQGAR 248
Cdd:PRK04196 162 QIARqakvlGEEENFAVVfAAMGITFEEANFFMEDFEETGALERSVVFLNLADDPAIERILTPRMALTAAEYLAfEKGMH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 249 VLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAG--NNDKGSITSFyAILHYAN----HP--DIfTD 320
Cdd:PRK04196 242 VLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERAGriKGKKGSITQI-PILTMPDdditHPipDL-TG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 321 YVKsllDGHFFLSpqeKSFSS----PPINVLTSLSR---------SSRQLalpHHYAAAQellsLLKAYHEAIDIIQLGA 387
Cdd:PRK04196 320 YIT---EGQIVLS---RELHRkgiyPPIDVLPSLSRlmkdgigegKTRED---HKDVANQ----LYAAYARGKDLRELAA 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 497559136 388 YVsGQDAHLDRAIRLLPSVKQF----LSQPYSHYSAIHETIEQLCQLLK 432
Cdd:PRK04196 387 IV-GEEALSERDRKYLKFADAFerefVNQGFDENRSIEETLDLGWELLS 434
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
77-352 |
3.75e-27 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 113.47 E-value: 3.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 77 LAIGAEVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGE 156
Cdd:PRK13343 82 ILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARRPLERPAPAIIERDFVTEPLQTGIKVVDALIPIGR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 157 GQRVGIFSEPGGGKSSL-LSTIAkgSQQTINVI---ALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAG 232
Cdd:PRK13343 162 GQRELIIGDRQTGKTAIaIDAII--NQKDSDVIcvyVAIGQKASAVARVIETLREHGALEYTTVVVAEASDPPGLQYLAP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 233 RAAITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGN-NDK---GSITSFyai 308
Cdd:PRK13343 240 FAGCAIAEYFRDQGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRLLERAAKlSPElggGSLTAL--- 316
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 497559136 309 lhyanhPDIFTD------Y----VKSLLDGHFFLSPQekSFSS---PPINVLTSLSR 352
Cdd:PRK13343 317 ------PIIETLagelsaYiptnLISITDGQIYLDSD--LFAAgqrPAVDVGLSVSR 365
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
143-303 |
2.21e-25 |
|
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: 104.96 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 143 TGIRAIDALLTIGEGqrvGIFSEPGG---GKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQ-------HKEGLAAQ 212
Cdd:cd01134 62 TGQRVLDTLFPVAKG---GTAAIPGPfgcGKTVISQSLSKWSNSDVVIYVGCGERGNEMAEVLEEfpelkdpITGESLME 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 213 RTVIIASTAyetaaSKVIAGRAA-----ITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHV 287
Cdd:cd01134 139 RTVLIANTS-----NMPVAAREAsiytgITIAEYFRDMGYNVSLMADSTSRWAEALREISGRLEEMPAEEGYPAYLGARL 213
|
170 180
....*....|....*....|...
gi 497559136 288 AEFLERAG-------NNDKGSIT 303
Cdd:cd01134 214 AEFYERAGrvrclgsPGREGSVT 236
|
|
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
69-414 |
2.73e-23 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 101.70 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 69 LALTPIYYLAIGAEVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAI 148
Cdd:COG0055 58 IAMDSTDGLVRGMEVIDTGAPISVPVGEATLGRIFNVLGEPIDGKGPIEAKERRPIHRPAPPFEEQSTKTEILETGIKVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 149 DALLTIGEGQRVGIFSEPGGGKSSLLS----TIAKGsQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYET 224
Cdd:COG0055 138 DLLAPYAKGGKIGLFGGAGVGKTVLIMelihNIAKE-HGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 225 AASKVIAGRAAITIAEYFRD-QGARVLFTMDSLSRWIESLQEVAIARGE---------TLSThhyaasvfhHVAEFLERA 294
Cdd:COG0055 217 PGARLRVALTALTMAEYFRDeEGQDVLLFIDNIFRFTQAGSEVSALLGRmpsavgyqpTLAT---------EMGALQERI 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 295 GNNDKGSITSFYAIlhYAnhP-DIFTD----YVKSLLDGHFFLSpqeKSFSS----PPINVLTSlsrSSRQLAlPH---- 361
Cdd:COG0055 288 TSTKKGSITSVQAV--YV--PaDDLTDpapaTTFAHLDATTVLS---RKIAElgiyPAVDPLDS---TSRILD-PLivge 356
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497559136 362 -HYAAAQELLSLLKAYHEAIDII------QLgayvSGQDAHL-DRAIRLlpsvKQFLSQPY 414
Cdd:COG0055 357 eHYRVAREVQRILQRYKELQDIIailgmdEL----SEEDKLTvARARKI----QRFLSQPF 409
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
23-303 |
4.25e-23 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 100.88 E-value: 4.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 23 LSRISGSLLEAQGLSACLGELCQISLSRSDpILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLLGRV 102
Cdd:PRK02118 8 ITDITGNVITVEAEGVGYGELATVERKDGS-SLAQVIRLDGDKVTLQVFGGTRGISTGDEVVFLGRPMQVTYSESLLGRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 103 LDGFGNPLDGGSQLpKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAkgSQ 182
Cdd:PRK02118 87 FNGSGKPIDGGPEL-EGEPIEIGGPSVNPVKRIVPREMIRTGIPMIDVFNTLVESQKIPIFSVSGEPYNALLARIA--LQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 183 QTINVIaLIGERGREVRDY---VNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAITIAEYFR-DQGARVLFTMDSLSR 258
Cdd:PRK02118 164 AEADII-ILGGMGLTFDDYlffKDTFENAGALDRTVMFIHTASDPPVECLLVPDMALAVAEKFAlEGKKKVLVLLTDMTN 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 497559136 259 WIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGN-NDKGSIT 303
Cdd:PRK02118 243 FADALKEISITMDQIPSNRGYPGSLYSDLASRYEKAVDfEDGGSIT 288
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
91-308 |
5.41e-23 |
|
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: 98.06 E-value: 5.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 91 SLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGK 170
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKERWPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 171 S----SLLSTIAKgSQQTINVIALIGERGREVRDYVNQHKEG-----LAAQRTVIIASTAYETAASKVIAGRAAITIAEY 241
Cdd:cd01133 81 TvlimELINNIAK-AHGGYSVFAGVGERTREGNDLYHEMKESgvinlDGLSKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497559136 242 FRDQ-GARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGNNDKGSITSFYAI 308
Cdd:cd01133 160 FRDEeGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAV 227
|
|
| ATP-synt_flagellum-secretory_path_III_N |
cd18117 |
Flagellum-specific ATP synthase, N-terminal domain; The N-terminal domain of the ... |
20-88 |
1.24e-22 |
|
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: 90.66 E-value: 1.24e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497559136 20 CGILSRISGSLLEAQGLSACLGELCQISLSRSDPILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRR 88
Cdd:cd18117 2 YGRVVRVVGLLLEAVGPQAPIGELCLIETADGLSILAEVVGFSGEKVLLMPLGELSGLSPGARVVPLGR 70
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
143-303 |
2.09e-21 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 96.77 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 143 TGIRAIDALLTIGEGqrvGIFSEPGG---GKSSLLSTIAKGSQQTINVIALIGERGREVRDYVNQHKE-------GLAAQ 212
Cdd:PRK04192 213 TGQRVIDTFFPVAKG---GTAAIPGPfgsGKTVTQHQLAKWADADIVIYVGCGERGNEMTEVLEEFPElidpktgRPLME 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 213 RTVIIASTAyetaaSKVIAGRAA-----ITIAEYFRDQGARVLFTMDSLSRWIESLQEVAiARGETLSTHH----YAASV 283
Cdd:PRK04192 290 RTVLIANTS-----NMPVAAREAsiytgITIAEYYRDMGYDVLLMADSTSRWAEALREIS-GRLEEMPGEEgypaYLASR 363
|
170 180
....*....|....*....|....*
gi 497559136 284 fhhVAEFLERAG-----NNDKGSIT 303
Cdd:PRK04192 364 ---LAEFYERAGrvktlGGEEGSVT 385
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
80-352 |
2.83e-21 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 95.80 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 80 GAEVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQR 159
Cdd:CHL00059 64 GSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISASESRLIESPAPGIISRRSVYEPLQTGLIAIDSMIPIGRGQR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 160 VGIFSEPGGGKSSL-LSTIAkgSQQTINVIAL---IGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAA 235
Cdd:CHL00059 144 ELIIGDRQTGKTAVaTDTIL--NQKGQNVICVyvaIGQKASSVAQVVTTLQERGAMEYTIVVAETADSPATLQYLAPYTG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 236 ITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAGN-NDK---GSITSFYAILHY 311
Cdd:CHL00059 222 AALAEYFMYRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKlSSQlgeGSMTALPIVETQ 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 497559136 312 ANhpD----IFTDyVKSLLDGHFFLSpqEKSFSS---PPINVLTSLSR 352
Cdd:CHL00059 302 AG--DvsayIPTN-VISITDGQIFLS--ADLFNAgirPAINVGISVSR 344
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
92-352 |
3.09e-18 |
|
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: 86.70 E-value: 3.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 92 LPLSNHLLGRVLDGFGNPLDGGSQLPKTNLSPLFSSPSSPMSRTPIQEVFPTGIRAIDALLTIGEGQRVGIFSEPGGGKS 171
Cdd:TIGR01040 76 TPVSEDMLGRVFNGSGKPIDKGPPVLAEDYLDINGQPINPYARIYPEEMIQTGISAIDVMNSIARGQKIPIFSAAGLPHN 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 172 SLLSTIAK--------------GSQQTIN-VIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIAGRAAI 236
Cdd:TIGR01040 156 EIAAQICRqaglvklptkdvhdGHEDNFAiVFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 237 TIAEYFRDQ-GARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAG--NNDKGSITSFyAILHYAN 313
Cdd:TIGR01040 236 TTAEYLAYQcEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGrvEGRNGSITQI-PILTMPN 314
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 497559136 314 ----HPdiFTDYVKSLLDGHFFLSPQ-EKSFSSPPINVLTSLSR 352
Cdd:TIGR01040 315 dditHP--IPDLTGYITEGQIYVDRQlHNRQIYPPINVLPSLSR 356
|
|
| T3SS_ATPase_C |
pfam18269 |
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family ... |
360-427 |
1.18e-17 |
|
T3SS EscN ATPase C-terminal domain; This is the C-terminal domain of the EscN protein family of ATPases that form part of the Type III secretion system (T3SS) present in Escherichia coli. T3SS is a macromolecular complex that creates a syringe-like apparatus extending from the bacterial cytosol across three membranes to the eukaryotic cytosol. This process is essential for pathogenicity. EscN is a functionally unique ATPase that provides an inner-membrane recognition gate for the T3SS chaperone-virulence effector complexes as well as a potential source of energy for their subsequent secretion.The C-terminal domain of T3SS ATPases mediates binding with multiple contact points along the chaperone.
Pssm-ID: 465691 [Multi-domain] Cd Length: 70 Bit Score: 76.70 E-value: 1.18e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497559136 360 PHHYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQPYSHYSAIHETIEQL 427
Cdd:pfam18269 3 PEHLQAARRLRELLATYQENEDLIRIGAYQAGSDPEIDEAIAKRPAINAFLRQGVDEPVSFEETLAQL 70
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
88-352 |
5.95e-17 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 82.81 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 88 RPASLPLSNHLLGRVLDGFGNPLDGGSQLPKTnlsplfsspsspmSRTPIQEVFP-------------TGIRAIDALLTI 154
Cdd:PRK09281 93 RILEVPVGEALLGRVVNPLGQPIDGKGPIEAT-------------ETRPVERKAPgvidrksvheplqTGIKAIDAMIPI 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 155 GEGQRVGIFSEPGGGKSSL-LSTI--AKGsQQTINVIALIGERGREVRDYVNQHKEGLAAQRTVIIASTAYETAASKVIA 231
Cdd:PRK09281 160 GRGQRELIIGDRQTGKTAIaIDTIinQKG-KDVICIYVAIGQKASTVAQVVRKLEEHGAMEYTIVVAATASDPAPLQYLA 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 232 GRAAITIAEYFRDQGARVLFTMDSLSRwieslQEVAIaRgeTLS--------THHYAASVFHHVAEFLERAG--NNDK-- 299
Cdd:PRK09281 239 PYAGCAMGEYFMDNGKDALIVYDDLSK-----QAVAY-R--QLSlllrrppgREAYPGDVFYLHSRLLERAAklSDELgg 310
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 300 GSITSFYAILHYANhpDIfTDY----VKSLLDGHFFLSPQekSFSS---PPINVLTSLSR 352
Cdd:PRK09281 311 GSLTALPIIETQAG--DV-SAYiptnVISITDGQIFLESD--LFNAgirPAINVGISVSR 365
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
80-425 |
1.83e-16 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 81.24 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 80 GAEVVPLRRPASLPLSNHLLGRVLDGFGNPLDG------GSQLP-----------KTNLsplfsspsspmsrtpiqEVFP 142
Cdd:CHL00060 84 GMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNlgpvdtRTTSPihrsapafiqlDTKL-----------------SIFE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 143 TGIRAIDALLTIGEGQRVGIFSEPGGGKS----SLLSTIAKgSQQTINVIALIGERGREVRDYVNQHKEG-------LAA 211
Cdd:CHL00060 147 TGIKVVDLLAPYRRGGKIGLFGGAGVGKTvlimELINNIAK-AHGGVSVFGGVGERTREGNDLYMEMKESgvineqnIAE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 212 QRTVIIASTAYETAASKVIAGRAAITIAEYFRDQGAR-VLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEF 290
Cdd:CHL00060 226 SKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQdVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSL 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 291 LERAGNNDKGSITSFYAILHYAnhpDIFTDYVK----SLLDGHFFLSpqeKSFSS----PPINVLTSLSRSSR-QLALPH 361
Cdd:CHL00060 306 QERITSTKEGSITSIQAVYVPA---DDLTDPAPattfAHLDATTVLS---RGLAAkgiyPAVDPLDSTSTMLQpRIVGEE 379
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497559136 362 HYAAAQELLSLLKAYHEAIDIIQ-LGAYVSGQDAHL--DRAIRllpsVKQFLSQPY----------SHYSAIHETIE 425
Cdd:CHL00060 380 HYETAQRVKQTLQRYKELQDIIAiLGLDELSEEDRLtvARARK----IERFLSQPFfvaevftgspGKYVGLAETIR 452
|
|
| ATP-synt_flagellum-secretory_path_III_C |
cd18114 |
Flagellum-specific ATP synthase, C-terminal domain; The C-terminal domain of the ... |
362-431 |
3.35e-16 |
|
Flagellum-specific ATP synthase, C-terminal domain; The C-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 flagellum-specific ATPase FliI is the soluble export component that drives flagellar protein export, and it shows extensive similarity to the alpha and beta subunits of FoF1-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: 349749 [Multi-domain] Cd Length: 71 Bit Score: 72.64 E-value: 3.35e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 362 HYAAAQELLSLLKAYHEAIDIIQLGAYVSGQDAHLDRAIRLLPSVKQFLSQPYSHYSAIHETIEQLCQLL 431
Cdd:cd18114 1 HYLAARKFRELMSTYQENEDLIRIGAYKKGSDPEVDEAIRLKPQIEAFLKQGLNEKAPLEESLQQLEEIF 70
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
154-295 |
2.20e-14 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 75.44 E-value: 2.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 154 IGEGQRV-GIFSEP----GGGKSSLLST------IAKGSQQTINVIALIGERGREVRDYVNQH------KEGLA-AQRTV 215
Cdd:PRK14698 642 ISEGQEVyDITTEThnfiGGNMPTLLHNtvtqhqLAKWSDAQVVIYIGCGERGNEMTDVLEEFpklkdpKTGKPlMERTV 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 216 IIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLERAG 295
Cdd:PRK14698 722 LIANTSNMPVAAREASIYTGITIAEYFRDMGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAG 801
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
143-378 |
1.52e-11 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 66.22 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 143 TGIRAIDALLTIGEGQRVGIFSEPGGGKSSL-LSTI---AKGSQQ------TINVIALIGERGREVRDYVNQHKEGLAAQ 212
Cdd:PTZ00185 175 TGFKAVDTMIPIGRGQRELIVGDRQTGKTSIaVSTIinqVRINQQilsknaVISIYVSIGQRCSNVARIHRLLRSYGALR 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 213 RTVIIASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSTHHYAASVFHHVAEFLE 292
Cdd:PTZ00185 255 YTTVMAATAAEPAGLQYLAPYSGVTMGEYFMNRGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVFYLHSRLLE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 293 RAG----NNDKGSITSFYAILHYANHPDIF-TDYVKSLLDGHFFLSpqEKSFSS---PPINVLTSLSRSSRQLALPHHYA 364
Cdd:PTZ00185 335 RAAmlspGKGGGSVTALPIVETLSNDVTAYiVTNVISITDGQIYLD--TKLFTGgqrPAVNIGLSVSRVGSSAQNVAMKA 412
|
250
....*....|....
gi 497559136 365 AAQELLSLLKAYHE 378
Cdd:PTZ00185 413 VAGKLKGILAEYRK 426
|
|
| PRK07165 |
PRK07165 |
ATP F0F1 synthase subunit alpha; |
45-418 |
2.71e-11 |
|
ATP F0F1 synthase subunit alpha;
Pssm-ID: 235951 [Multi-domain] Cd Length: 507 Bit Score: 65.38 E-value: 2.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 45 QISLSRSDP-ILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPLRRPASLPLSNHLLGRVLDGFGNPLDGGSQLPkTNLSP 123
Cdd:PRK07165 25 QFFTLKNNPnVKAFVISATEDKAYLLINNEKGKIKINDELIELNNTNKVKTSKEYFGKIIDIDGNIIYPEAQNP-LSKKF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 124 LFSSPSSPMSRTPIQEVFP------TGIRAIDALLTIGEGQRVGIFSEPGGGKSSL-LSTIAKGSQQTINVIAL-IGERG 195
Cdd:PRK07165 104 LPNTSSIFNLAHGLMTVKTlneqlyTGIIAIDLLIPIGKGQRELIIGDRQTGKTHIaLNTIINQKNTNVKCIYVaIGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 196 REVRDYVNQHKEGLAAQRTVII---ASTAYEtaasKVIAGRAAITIAE---YFRDqgarVLFTMDSLSRWIESLQEVAIA 269
Cdd:PRK07165 184 ENLSRIYETLKEHDALKNTIIIdapSTSPYE----QYLAPYVAMAHAEnisYNDD----VLIVFDDLTKHANIYREIALL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 270 RGETLSTHHYAASVFHHVAEFLERAGN-NDKGSITSFyAILHYANHpDI---FTDYVKSLLDGHFFLSpqEKSFSS---P 342
Cdd:PRK07165 256 TNKPVGKEAFPGDMFFAHSKLLERAGKfKNRKTITAL-PILQTVDN-DItslISSNIISITDGQIVTS--SDLFASgklP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 343 PINVLTSLSR--SSRQLALPHHYAAaqELLSLLKAYHEAIDIIQLgayvsgqDAHLDRAIRLLPS----VKQFLSQP-YS 415
Cdd:PRK07165 332 AIDIDLSVSRtgSSVQSKTITKVAG--EISKIYRAYKRQLKLSML-------DYDLNKETSDLLFkgkmIEKMFNQKgFS 402
|
...
gi 497559136 416 HYS 418
Cdd:PRK07165 403 LYS 405
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
146-275 |
9.74e-09 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 55.67 E-value: 9.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 146 RAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKG----SQQTINVIALIGERGREVRDYvnqhkeglaaQRTV---IIA 218
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAiaknHPEVELIVLLIDERPEEVTDM----------RRSVkgeVVA 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 497559136 219 STAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLS 275
Cdd:cd01128 75 STFDEPPERHVQVAEMVIEKAKRLVEHGKDVVILLDSITRLARAYNTVVPSSGKTLS 131
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
146-275 |
2.52e-08 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 55.48 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 146 RAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKGSqqTIN------VIALIGERGREVRDYvnqhkeglaaQRTV---I 216
Cdd:PRK12608 122 RVVDLVAPIGKGQRGLIVAPPRAGKTVLLQQIAAAV--AANhpevhlMVLLIDERPEEVTDM----------RRSVkgeV 189
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 497559136 217 IASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLS 275
Cdd:PRK12608 190 YASTFDRPPDEHIRVAELVLERAKRLVEQGKDVVILLDSLTRLARAYNNEVESSGRTLS 248
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
146-303 |
3.25e-08 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 55.46 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 146 RAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKGSqqTIN------VIALIGERGREVRDyvnqhkeglaAQRTV---I 216
Cdd:TIGR00767 157 RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQAI--TRNhpevelIVLLIDERPEEVTD----------MQRSVkgeV 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 217 IASTAYETAASKVIAGRAAITIAEYFRDQGARVLFTMDSLSRWIESLQEVAIARGETLSThHYAASVFHHVAEFLERAGN 296
Cdd:TIGR00767 225 VASTFDEPASRHVQVAEMVIEKAKRLVEHKKDVVILLDSITRLARAYNTVTPASGKVLSG-GVDANALHRPKRFFGAARN 303
|
....*...
gi 497559136 297 -NDKGSIT 303
Cdd:TIGR00767 304 iEEGGSLT 311
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
362-432 |
8.50e-06 |
|
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: 43.20 E-value: 8.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497559136 362 HYAAAQELLSLLKAYHEAIDIIQLGAYVSgQDAHLDRAIRLLPSVKQFLSQPYSHYSAIHETIEQLCQLLK 432
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDA-LSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
146-220 |
1.21e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.51 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 146 RAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAkgsqqtiNVIA-----------LIGERGREVRDYvnqhkeglaaQRT 214
Cdd:PRK12678 405 RVIDLIMPIGKGQRGLIVSPPKAGKTTILQNIA-------NAITtnnpechlmvvLVDERPEEVTDM----------QRS 467
|
....*....
gi 497559136 215 V---IIAST 220
Cdd:PRK12678 468 VkgeVIAST 476
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
24-86 |
1.69e-04 |
|
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: 39.45 E-value: 1.69e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497559136 24 SRISGSLLEAQGLSACL-GELCQISLSRSDP---ILAEVIGIHNRTTLLLALTPIYYLAIGAEVVPL 86
Cdd:pfam02874 2 VQVIGPVVDVEFGIGRLpGLLNALEVELVEFgslVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRT 68
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
146-258 |
2.23e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 43.21 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 146 RAIDALLTIGEGQRVGIFSEPGGGKSSLLSTIAKGSqqTIN------VIALIGERGREVRDYvnqhkeglaaQRTV---I 216
Cdd:PRK09376 158 RIIDLIAPIGKGQRGLIVAPPKAGKTVLLQNIANSI--TTNhpevhlIVLLIDERPEEVTDM----------QRSVkgeV 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 497559136 217 IASTAYETA------ASKVI--AGRaaitIAEYFRDqgarVLFTMDSLSR 258
Cdd:PRK09376 226 VASTFDEPAerhvqvAEMVIekAKR----LVEHGKD----VVILLDSITR 267
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
20-85 |
5.50e-04 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 38.45 E-value: 5.50e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 20 CGILSRISGSLLEAQGL-SACLGELCQISLSRSDPIL---AEVIGIHNRTTLLLALTPIYYLAIGAEVVP 85
Cdd:cd01426 1 KGRVIRVNGPLVEAELEgEVAIGEVCEIERGDGNNETvlkAEVIGFRGDRAILQLFESTRGLSRGALVEP 70
|
|
| archRadB |
cd01394 |
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional ... |
142-230 |
5.94e-03 |
|
archaeal RadB; The archaeal protein RadB shares similarity RadA, the archaeal functional homologue to the bacterial RecA. The precise function of RadB is unclear.
Pssm-ID: 410882 [Multi-domain] Cd Length: 216 Bit Score: 38.06 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497559136 142 PTGIRAIDALLTIGEGQRV--GIFSEPGGGKSSLLSTIAKGS-QQTINVIaligergrevrdYVNqhKEGLAAQRTVIIA 218
Cdd:cd01394 2 STGSKSLDSLLGGGVERGTitQIYGPPGSGKTNICLQLAVEAaKQGKKVV------------YID--TEGLSPERFQQIA 67
|
90
....*....|..
gi 497559136 219 STAYETAASKVI 230
Cdd:cd01394 68 GERFESIASNII 79
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
152-178 |
6.86e-03 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 36.86 E-value: 6.86e-03
10 20
....*....|....*....|....*..
gi 497559136 152 LTIGEGQRVGIFSEPGGGKSSLLSTIA 178
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIA 32
|
|
| |
