|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
1-390 |
0e+00 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 770.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 1 MSANAETQTPQQPVKKSGKRKRLLLLLTLLFIIIAVAIGIYWFLVLRHFEETDDAYVAGNQIQIMSQVSGSVTKVWADNT 80
Cdd:PRK15136 1 MSANAETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 81 DFVKEGDVLVTLDPTDARQAFEKAKTALASSVRQTHQLMINSKQLQANIEVQKIALAKAQSDYNRRVPLGNANLIGREEL 160
Cdd:PRK15136 81 DFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 161 QHARDAVTSAQAQLDVAIQQYNANQAMILGTKLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQPGAQISPT 240
Cdd:PRK15136 161 QHARDAVASAQAQLDVAIQQYNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 241 TPLMAVVPATNMWVDANFKETQIANMRIGQPVTITTDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLP 320
Cdd:PRK15136 241 TPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 321 VRIELDQKQLEQYPLRIGLSTLVSVNTTNRDGQVLANKVRSTPVAVSTAREISLAPVNKLIDDIVKANAG 390
Cdd:PRK15136 321 VRIELDAKQLAQHPLRIGLSTLVTVDTANRDGQVLANQVRSTPAYESNALEIDLAPVNKLIDDIIQANAG 390
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
20-345 |
2.85e-173 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 486.22 E-value: 2.85e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 20 RKRLLLLLTLLFIIIAVAIGIYWFLVLRHFEETDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQ 99
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 100 AFEKAKTALASSVRQTHQLMINSKQLQANIEVQKIALAKAQS-------DYNRRVPLGNANLIGREELQHARDAVTSAQA 172
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAREkllqaelDLRRRVPLFKKGLISREELDHARKALLSAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 173 QLDVAIQ-QYNANQAMILGTKLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATN 251
Cdd:TIGR00998 161 ALNAAIQeQLNANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 252 MWVDANFKETQIANMRIGQPVTITTDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDQKQLE 331
Cdd:TIGR00998 241 MYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELD 320
|
330
....*....|....
gi 481022922 332 QYPLRIGLSTLVSV 345
Cdd:TIGR00998 321 EHPLRIGLSAEVEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
31-347 |
3.14e-78 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 244.19 E-value: 3.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 31 FIIIAVAIGIYWFLVLRHF---EETDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTA 107
Cdd:COG1566 12 LVLLLLALGLALWAAGRNGpdePVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 108 LASSVRQTHQLMINS------KQLQANIEVQKIALAKAQSDYNRRVPLGNANLIGREELQHARDAVTSAQAQLDVAIQQY 181
Cdd:COG1566 92 LAAAEAQLARLEAELgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 182 NANQAMILG--TKLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFK 259
Cdd:COG1566 172 AQAQAGLREeeELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 260 ETQIANMRIGQPVTITTDIYgDDVKYTGKVVGLDMGTGSAFsllPAQNATGNwikVVQRLPVRIELDQKQLEqyPLRIGL 339
Cdd:COG1566 252 ETDLGRVKPGQPVEVRVDAY-PDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDPE--PLRPGM 322
|
....*...
gi 481022922 340 STLVSVNT 347
Cdd:COG1566 323 SATVEIDT 330
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
47-347 |
1.02e-62 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 204.19 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 47 RHFEETDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALASSVRQTHQLMINSKQLQ 126
Cdd:pfam00529 6 KGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 127 ------------------------ANIEVQKIALAKAQSDYNRRVPLGNANLIGREELQHARDAVTSAQAQLDVAIQQ-- 180
Cdd:pfam00529 86 aleselaisrqdydgataqlraaqAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQld 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 181 ---------YNANQAMILGTKLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQP-GAQISPTTPLMAVVPAT 250
Cdd:pfam00529 166 qiyvqitqsAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPED 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 251 NMWVDANFKETQIANMRIGQPVTITTDIYGDDV--KYTGKVVGLDMGTGsafsllpaqnatgnwikvvqrlPVRIELDQK 328
Cdd:pfam00529 246 NLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRVVVDKA 303
|
330
....*....|....*....
gi 481022922 329 QLEQYPLRIGLSTLVSVNT 347
Cdd:pfam00529 304 QGPYYPLRIGLSAGALVRL 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
1-390 |
0e+00 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 770.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 1 MSANAETQTPQQPVKKSGKRKRLLLLLTLLFIIIAVAIGIYWFLVLRHFEETDDAYVAGNQIQIMSQVSGSVTKVWADNT 80
Cdd:PRK15136 1 MSANAETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 81 DFVKEGDVLVTLDPTDARQAFEKAKTALASSVRQTHQLMINSKQLQANIEVQKIALAKAQSDYNRRVPLGNANLIGREEL 160
Cdd:PRK15136 81 DFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 161 QHARDAVTSAQAQLDVAIQQYNANQAMILGTKLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQPGAQISPT 240
Cdd:PRK15136 161 QHARDAVASAQAQLDVAIQQYNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 241 TPLMAVVPATNMWVDANFKETQIANMRIGQPVTITTDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLP 320
Cdd:PRK15136 241 TPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 321 VRIELDQKQLEQYPLRIGLSTLVSVNTTNRDGQVLANKVRSTPVAVSTAREISLAPVNKLIDDIVKANAG 390
Cdd:PRK15136 321 VRIELDAKQLAQHPLRIGLSTLVTVDTANRDGQVLANQVRSTPAYESNALEIDLAPVNKLIDDIIQANAG 390
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
20-345 |
2.85e-173 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 486.22 E-value: 2.85e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 20 RKRLLLLLTLLFIIIAVAIGIYWFLVLRHFEETDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQ 99
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 100 AFEKAKTALASSVRQTHQLMINSKQLQANIEVQKIALAKAQS-------DYNRRVPLGNANLIGREELQHARDAVTSAQA 172
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAREkllqaelDLRRRVPLFKKGLISREELDHARKALLSAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 173 QLDVAIQ-QYNANQAMILGTKLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATN 251
Cdd:TIGR00998 161 ALNAAIQeQLNANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 252 MWVDANFKETQIANMRIGQPVTITTDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDQKQLE 331
Cdd:TIGR00998 241 MYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELD 320
|
330
....*....|....
gi 481022922 332 QYPLRIGLSTLVSV 345
Cdd:TIGR00998 321 EHPLRIGLSAEVEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
31-347 |
3.14e-78 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 244.19 E-value: 3.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 31 FIIIAVAIGIYWFLVLRHF---EETDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTA 107
Cdd:COG1566 12 LVLLLLALGLALWAAGRNGpdePVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 108 LASSVRQTHQLMINS------KQLQANIEVQKIALAKAQSDYNRRVPLGNANLIGREELQHARDAVTSAQAQLDVAIQQY 181
Cdd:COG1566 92 LAAAEAQLARLEAELgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 182 NANQAMILG--TKLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFK 259
Cdd:COG1566 172 AQAQAGLREeeELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 260 ETQIANMRIGQPVTITTDIYgDDVKYTGKVVGLDMGTGSAFsllPAQNATGNwikVVQRLPVRIELDQKQLEqyPLRIGL 339
Cdd:COG1566 252 ETDLGRVKPGQPVEVRVDAY-PDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDPE--PLRPGM 322
|
....*...
gi 481022922 340 STLVSVNT 347
Cdd:COG1566 323 SATVEIDT 330
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
47-347 |
1.02e-62 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 204.19 E-value: 1.02e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 47 RHFEETDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALASSVRQTHQLMINSKQLQ 126
Cdd:pfam00529 6 KGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 127 ------------------------ANIEVQKIALAKAQSDYNRRVPLGNANLIGREELQHARDAVTSAQAQLDVAIQQ-- 180
Cdd:pfam00529 86 aleselaisrqdydgataqlraaqAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQld 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 181 ---------YNANQAMILGTKLEDQPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQP-GAQISPTTPLMAVVPAT 250
Cdd:pfam00529 166 qiyvqitqsAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPED 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 251 NMWVDANFKETQIANMRIGQPVTITTDIYGDDV--KYTGKVVGLDMGTGsafsllpaqnatgnwikvvqrlPVRIELDQK 328
Cdd:pfam00529 246 NLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRVVVDKA 303
|
330
....*....|....*....
gi 481022922 329 QLEQYPLRIGLSTLVSVNT 347
Cdd:pfam00529 304 QGPYYPLRIGLSAGALVRL 322
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
57-355 |
2.99e-33 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 126.60 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 57 VAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAktalassvrqthqlminskqlQANIEVQKIAL 136
Cdd:COG0845 19 EARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQA---------------------QAQLAAAQAQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 137 AKAQSDYNRRVPLGNANLIGREELQHARDAVTSAQAQldvaiqqynanqamilgtkledqpaVQQAATEVRNAWLALERT 216
Cdd:COG0845 78 ELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAA-------------------------LAAAQAALEQARANLAYT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 217 RIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFKETQIANMRIGQPVTITTDIYgDDVKYTGKVVGLDmgt 296
Cdd:COG0845 133 TIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAG-PGKTFEGKVTFID--- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 481022922 297 gsafsllPAQNATgnwikvVQRLPVRIELDQKQLeqyPLRIGLSTLVSVNTTNRDGQVL 355
Cdd:COG0845 209 -------PAVDPA------TRTVRVRAELPNPDG---LLRPGMFVRVRIVLGERENALL 251
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
32-345 |
7.26e-33 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 125.91 E-value: 7.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 32 IIIAVAIGIYWFLVLRHFEETDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALASS 111
Cdd:PRK10476 19 VALAIVALVFVIWRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 112 VRQ--THQLMINSKQLQANIEVQKIALAKAQSD-----YNRRVPLGNANLIGREELQHARDAVTSAQAQLDVAIQQYNAN 184
Cdd:PRK10476 99 DAQimTTQRSVDAERSNAASANEQVERARANAKlatrtLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQALLQAQAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 185 QAMILGTK-LEDQPAVQQAATEVrnAWLALERTRIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFKETQI 263
Cdd:PRK10476 179 AAAVGGVDaLVAQRAAREAALAI--AELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 264 ANMRIGQPVTITTDIygDDVK-YTGKVVGLDMGTGSAFSL-----LPAQNATGNWIKVVQRLPVRIELDQKQLEQypLRI 337
Cdd:PRK10476 257 KNIRVGDCATVYSMI--DRGRpFEGKVDSIGWGVLPDDGGnvprgLPYVPRSINWVRVAQRFPVRIMLDKPDPEL--FRI 332
|
....*...
gi 481022922 338 GLSTLVSV 345
Cdd:PRK10476 333 GASAVVEL 340
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
20-289 |
2.70e-21 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 93.49 E-value: 2.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 20 RKRLLLLLTLLFIIIAVAIGIYWFLvlrhfEETDDA-YVAGN----QIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDP 94
Cdd:PRK03598 2 KKKVVIGLAVVVLAAAVAGGWWWYQ-----SRQDNGlTLYGNvdirTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 95 TDARQAFEKAKtALASSVRQTHQLMINS------KQLQANIEVQKIALAKAQSDYNRRVPLGNANLIGREELQHARDAVT 168
Cdd:PRK03598 77 APYENALMQAK-ANVSVAQAQLDLMLAGyrdeeiAQARAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 169 SAQAQLDVAIQQYNANQAmilGTKLED----QPAVQQAATEVRNAWLALERTRIVSPMTGYVSRRAVQPGAQISPTTPLM 244
Cdd:PRK03598 156 QAQATLKSAQDKLSQYRE---GNRPQDiaqaKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVF 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 481022922 245 AVVPATNMWVDANFKETQIANMRIGQPVTITTDIYGDDVkYTGKV 289
Cdd:PRK03598 233 TLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKP-YHGQI 276
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
57-289 |
4.74e-20 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 89.68 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 57 VAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKtalassvrqthqlminskqlqANIEVQKIAL 136
Cdd:TIGR01730 22 EAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAAL---------------------AQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 137 AKAQSDYNRRVPLgnanligreelqHARDAVTsaQAQLDVAIQQYNANQAmilgtkledqpAVQQAATEVRNAWLALERT 216
Cdd:TIGR01730 81 ELAQRSFERAERL------------VKRNAVS--QADLDDAKAAVEAAQA-----------DLEAAKASLASAQLNLRYT 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 481022922 217 RIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFKETQIANMRIGQPVTITTDIYgDDVKYTGKV 289
Cdd:TIGR01730 136 EIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDAL-PGEEFKGKL 207
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
52-334 |
1.26e-16 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 79.78 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 52 TDDAYVAGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALAssvrqTHQLMINSKQLQANiev 131
Cdd:PRK10559 38 TRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVA-----YYQVLAQEKRREAG--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 132 qkialakaqsdynRRVPLGnANLIGREELQHARDAVTSAQAQLdvaiqqynanqamilgtkledqpAVQQAATEVrnAWL 211
Cdd:PRK10559 110 -------------RRNRLG-VQAMSREEIDQANNVLQTVLHQL-----------------------AKAQATRDL--AKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 212 ALERTRIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFKETQIANMRIGQPVTITTdiYGDDVKYTGKVVG 291
Cdd:PRK10559 151 DLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITP--LGSNKVLKGTVDS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 481022922 292 LDMGTGSAFSL-----LPAQNATGNWIKVVQRLPVRIELDQKQLEQYP 334
Cdd:PRK10559 229 VAAGVTNSSSTrdskgMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYP 276
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
31-340 |
2.37e-10 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 61.56 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 31 FIIIAVAIGIYWFLVLRHFEETDDAYVA-------GNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFE- 102
Cdd:TIGR01843 6 LITWLIAGLVVIFFLWAYFAPLDVVATAtgkvvpsGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 103 -------------------------------------------KAKTALASSVRQTHQLMINS-----KQLQANIEVQKI 134
Cdd:TIGR01843 86 lesqvlrleaevarlraeadsqaaiefpddllsaedpavpeliKGQQSLFESRKSTLRAQLELilaqiKQLEAELAGLQA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 135 ALAKAQSD---YNRRV----PLGNANLIGREELQHARDAVTSAQAQLDVAIQQYNANQAMILGTKLEDQPAVQQAATEVR 207
Cdd:TIGR01843 166 QLQALRQQlevISEELearrKLKEKGLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFREEVL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 208 N------------------AWLALERTRIVSPMTGYVSRRAVQP-GAQISPTTPLMAVVPATN-MWVDANFKETQIANMR 267
Cdd:TIGR01843 246 EelteaqarlaelrerlnkARDRLQRLIIRSPVDGTVQSLKVHTvGGVVQPGETLMEIVPEDDpLEIEAKLSPKDIGFVH 325
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 481022922 268 IGQPVTITTDIYgDDVKY---TGKVVGLdmgtgSAfSLLPAQNATGNWikvvqrLPVRIELDQKQLEQYPLRIGLS 340
Cdd:TIGR01843 326 VGQPAEIKFSAF-PYRRYgilNGKVKSI-----SP-DTFTDERGGGPY------YRVRISIDQNTLGIGPKGLELS 388
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
212-289 |
3.75e-10 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 59.06 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 212 ALERTR-------IVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFKETQIANMRIGQPVTITTDIYGDDVk 284
Cdd:pfam16576 98 ELERTGkvqptvtVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKT- 176
|
....*
gi 481022922 285 YTGKV 289
Cdd:pfam16576 177 FEGKV 181
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
217-338 |
9.35e-08 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 49.67 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 217 RIVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFKETQIANMRIGQPVTITTDiYGDDVKYTGKVVgldmgt 296
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLD-PGSDYTLEGKVV------ 73
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 481022922 297 gsafSLLPAQNATGnwikvvQRLPVRIELDQkQLEQYPLRIG 338
Cdd:pfam13437 74 ----RISPTVDPDT------GVIPVRVSIEN-PKTPIPLLPG 104
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
66-289 |
1.44e-06 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 49.77 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 66 SQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALassvrqthqlminsKQLQANIEVQKIALAKAQSDYNR 145
Cdd:PRK11578 66 AQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATL--------------MELRAQRQQAEAELKLARVTLSR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 146 RVPLGNANLIGREELQHARDAVTSAQAQLDVAIQQYNANQAmilgtkledqpavqqaatEVRNAWLALERTRIVSPMTGY 225
Cdd:PRK11578 132 QQRLAKTQAVSQQDLDTAATELAVKQAQIGTIDAQIKRNQA------------------SLDTAKTNLDYTRIVAPMAGE 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 226 VSRRAVQPG-----AQISPTtpLMAVVPATNMWVDANFKETQIANMRIGQPVTITtdIYGD-DVKYTGKV 289
Cdd:PRK11578 194 VTQITTLQGqtviaAQQAPN--ILTLADMSTMLVKAQVSEADVIHLKPGQKAWFT--VLGDpLTRYEGVL 259
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
58-274 |
1.26e-05 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 47.09 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 58 AGNQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALASSvrqthqlminskqlqanievqKIALA 137
Cdd:PRK11556 84 AANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKD---------------------QATLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 138 KAQSDYNRRVPLGNANLIGREELQHARDAVTSAQAQLDVaiqqynanqamilgtkleDQPAVQqaatevrNAWLALERTR 217
Cdd:PRK11556 143 NARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKA------------------DEASVA-------SAQLQLDYSR 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 481022922 218 IVSPMTGYVSRRAVQPGAQISPTTPLMAVVPATNMWVDANFK--ETQIANM----RIGQPVTI 274
Cdd:PRK11556 198 ITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTlpESDIATVvqaqKAGKPLVV 260
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
63-238 |
1.60e-05 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 46.63 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 63 QIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALASSVRqthqlminskqlqanievqkiALAKAQSD 142
Cdd:PRK09859 63 EIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALS---------------------TASNARIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 481022922 143 YNRRVPLGNANLIGREELQHARDAVTSAQAQLDVAiqqynanqamilgtkledQPAVQQAAtevrnawLALERTRIVSPM 222
Cdd:PRK09859 122 FNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVA------------------KAAVEQAT-------INLQYANVTSPI 176
|
170
....*....|....*.
gi 481022922 223 TGYVSRRAVQPGAQIS 238
Cdd:PRK09859 177 TGVSGKSSVTVGALVT 192
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
60-109 |
1.98e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 38.58 E-value: 1.98e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 481022922 60 NQIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDARQAFEKAKTALA 109
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK08225 |
PRK08225 |
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
61-93 |
8.57e-03 |
|
acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 181304 [Multi-domain] Cd Length: 70 Bit Score: 34.76 E-value: 8.57e-03
10 20 30
....*....|....*....|....*....|...
gi 481022922 61 QIQIMSQVSGSVTKVWADNTDFVKEGDVLVTLD 93
Cdd:PRK08225 38 EIPIVAEEAGTVKKINVQEGDFVNEGDVLLEIE 70
|
|
| |
