|
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: 758.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 1 MSENAANQTPQQSGSKKGKRKGALLLLTLLFVIVAVAYGIYWFLVLRHYEETDDAYVAGNQVQIMAQVSGSVTKVWADNT 80
Cdd:PRK15136 1 MSANAETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 81 DFVQQGDPLVTLDQTDAQQAFEKAKTQLAASVRQTRQQMINSKQLQANIDVKKTALAQAQADLNRRIPLGAANLIGREEL 160
Cdd:PRK15136 81 DFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 161 QHARDTVASAQAELDVAIQQYNANQAIVLGTKLEQQPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQPGAQIGTT 240
Cdd:PRK15136 161 QHARDAVASAQAQLDVAIQQYNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 241 TPLMAVVPATNLWVDANFKETQLAHMRIGQPATIISDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLP 320
Cdd:PRK15136 241 TPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 321 VRIEIDAKQLAQHPLRIGLSTLVEVDTSNREGEMLASQVRSSPVYESNAREIGLEPVNKLIDGIIQANAG 390
Cdd:PRK15136 321 VRIELDAKQLAQHPLRIGLSTLVTVDTANRDGQVLANQVRSTPAYESNALEIDLAPVNKLIDDIIQANAG 390
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
31-345 |
7.43e-159 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 449.63 E-value: 7.43e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 31 FVIVAVAYGIYWFLVLRHYEETDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAA 110
Cdd:TIGR00998 12 LIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAELALAKAEANLAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 111 SVRQTRQQMINSKQLQANIDVKKTALAQAQA-------DLNRRIPLGAANLIGREELQHARDTVASAQAELDVAIQ-QYN 182
Cdd:TIGR00998 92 LVRQTKQLEITVQQLQAKVESLKIKLEQAREkllqaelDLRRRVPLFKKGLISREELDHARKALLSAKAALNAAIQeQLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 183 ANQAIVLGTKLEQQPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKETQ 262
Cdd:TIGR00998 172 ANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQMYVEANFKETQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 263 LAHMRIGQPATIISDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIEIDAKQLAQHPLRIGLSTL 342
Cdd:TIGR00998 252 LKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDEHPLRIGLSAE 331
|
...
gi 695798189 343 VEV 345
Cdd:TIGR00998 332 VEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
31-347 |
9.90e-74 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 232.63 E-value: 9.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 31 FVIVAVAYGIYWFLVLRHYEE-TDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLA 109
Cdd:COG1566 14 LLLLALGLALWAAGRNGPDEPvTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 110 ASVRQTRQQMINS------KQLQANIDVKKTALAQAQADLNRRIPLGAANLIGREELQHARDTVASAQAELDVAIQQYNA 183
Cdd:COG1566 94 AAEAQLARLEAELgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 184 NQAIVLG--TKLEQQPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKET 261
Cdd:COG1566 174 AQAGLREeeELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 262 QLAHMRIGQPATIISDIYgDDVKYTGKVVGLDMGTGSAFsllPAQNATGNwikVVQRLPVRIEIDAKQLaqHPLRIGLST 341
Cdd:COG1566 254 DLGRVKPGQPVEVRVDAY-PDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDP--EPLRPGMSA 324
|
....*.
gi 695798189 342 LVEVDT 347
Cdd:COG1566 325 TVEIDT 330
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
47-347 |
3.77e-57 |
|
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: 189.56 E-value: 3.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 47 RHYEETDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAASVRQTRQQMINSKQLQ 126
Cdd:pfam00529 6 KGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 127 ------------------------ANIDVKKTALAQAQADLNRRIPLGAANLIGREELQHARDTVASAQAELDVAIQQ-- 180
Cdd:pfam00529 86 aleselaisrqdydgataqlraaqAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQld 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 181 ---------YNANQAIVLGTKLEQQPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQP-GAQIGTTTPLMAVVPAT 250
Cdd:pfam00529 166 qiyvqitqsAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPED 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 251 NLWVDANFKETQLAHMRIGQPATIISDIYGDDV--KYTGKVVGLDMGTGsafsllpaqnatgnwikvvqrlPVRIEIDAK 328
Cdd:pfam00529 246 NLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRVVVDKA 303
|
330
....*....|....*....
gi 695798189 329 QLAQHPLRIGLSTLVEVDT 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: 758.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 1 MSENAANQTPQQSGSKKGKRKGALLLLTLLFVIVAVAYGIYWFLVLRHYEETDDAYVAGNQVQIMAQVSGSVTKVWADNT 80
Cdd:PRK15136 1 MSANAETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 81 DFVQQGDPLVTLDQTDAQQAFEKAKTQLAASVRQTRQQMINSKQLQANIDVKKTALAQAQADLNRRIPLGAANLIGREEL 160
Cdd:PRK15136 81 DFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 161 QHARDTVASAQAELDVAIQQYNANQAIVLGTKLEQQPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQPGAQIGTT 240
Cdd:PRK15136 161 QHARDAVASAQAQLDVAIQQYNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 241 TPLMAVVPATNLWVDANFKETQLAHMRIGQPATIISDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLP 320
Cdd:PRK15136 241 TPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 321 VRIEIDAKQLAQHPLRIGLSTLVEVDTSNREGEMLASQVRSSPVYESNAREIGLEPVNKLIDGIIQANAG 390
Cdd:PRK15136 321 VRIELDAKQLAQHPLRIGLSTLVTVDTANRDGQVLANQVRSTPAYESNALEIDLAPVNKLIDDIIQANAG 390
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
31-345 |
7.43e-159 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 449.63 E-value: 7.43e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 31 FVIVAVAYGIYWFLVLRHYEETDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAA 110
Cdd:TIGR00998 12 LIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAELALAKAEANLAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 111 SVRQTRQQMINSKQLQANIDVKKTALAQAQA-------DLNRRIPLGAANLIGREELQHARDTVASAQAELDVAIQ-QYN 182
Cdd:TIGR00998 92 LVRQTKQLEITVQQLQAKVESLKIKLEQAREkllqaelDLRRRVPLFKKGLISREELDHARKALLSAKAALNAAIQeQLN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 183 ANQAIVLGTKLEQQPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKETQ 262
Cdd:TIGR00998 172 ANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQMYVEANFKETQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 263 LAHMRIGQPATIISDIYGDDVKYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIEIDAKQLAQHPLRIGLSTL 342
Cdd:TIGR00998 252 LKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDEHPLRIGLSAE 331
|
...
gi 695798189 343 VEV 345
Cdd:TIGR00998 332 VEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
31-347 |
9.90e-74 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 232.63 E-value: 9.90e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 31 FVIVAVAYGIYWFLVLRHYEE-TDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLA 109
Cdd:COG1566 14 LLLLALGLALWAAGRNGPDEPvTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 110 ASVRQTRQQMINS------KQLQANIDVKKTALAQAQADLNRRIPLGAANLIGREELQHARDTVASAQAELDVAIQQYNA 183
Cdd:COG1566 94 AAEAQLARLEAELgaeaeiAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 184 NQAIVLG--TKLEQQPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKET 261
Cdd:COG1566 174 AQAGLREeeELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 262 QLAHMRIGQPATIISDIYgDDVKYTGKVVGLDMGTGSAFsllPAQNATGNwikVVQRLPVRIEIDAKQLaqHPLRIGLST 341
Cdd:COG1566 254 DLGRVKPGQPVEVRVDAY-PDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDNPDP--EPLRPGMSA 324
|
....*.
gi 695798189 342 LVEVDT 347
Cdd:COG1566 325 TVEIDT 330
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
47-347 |
3.77e-57 |
|
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: 189.56 E-value: 3.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 47 RHYEETDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAASVRQTRQQMINSKQLQ 126
Cdd:pfam00529 6 KGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 127 ------------------------ANIDVKKTALAQAQADLNRRIPLGAANLIGREELQHARDTVASAQAELDVAIQQ-- 180
Cdd:pfam00529 86 aleselaisrqdydgataqlraaqAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQld 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 181 ---------YNANQAIVLGTKLEQQPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQP-GAQIGTTTPLMAVVPAT 250
Cdd:pfam00529 166 qiyvqitqsAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPED 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 251 NLWVDANFKETQLAHMRIGQPATIISDIYGDDV--KYTGKVVGLDMGTGsafsllpaqnatgnwikvvqrlPVRIEIDAK 328
Cdd:pfam00529 246 NLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRVVVDKA 303
|
330
....*....|....*....
gi 695798189 329 QLAQHPLRIGLSTLVEVDT 347
Cdd:pfam00529 304 QGPYYPLRIGLSAGALVRL 322
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
32-345 |
1.97e-35 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 132.84 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 32 VIVAVAYGIYWFLVLRHYEETDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAAS 111
Cdd:PRK10476 19 VALAIVALVFVIWRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 112 VRQ--TRQQMINSKQLQANIDVKKTALAQAQADL-----NRRIPLGAANLIGREELQHARDTVASAQAELDVAIQQYNAN 184
Cdd:PRK10476 99 DAQimTTQRSVDAERSNAASANEQVERARANAKLatrtlERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQALLQAQAA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 185 QAIVLGTK-LEQQPAVLQAATEVrnAWLALQRTQIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKETQL 263
Cdd:PRK10476 179 AAAVGGVDaLVAQRAAREAALAI--AELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 264 AHMRIGQPATIISDIygDDVK-YTGKVVGLDMGTGSAFSL-----LPAQNATGNWIKVVQRLPVRIEIDAKQlaQHPLRI 337
Cdd:PRK10476 257 KNIRVGDCATVYSMI--DRGRpFEGKVDSIGWGVLPDDGGnvprgLPYVPRSINWVRVAQRFPVRIMLDKPD--PELFRI 332
|
....*...
gi 695798189 338 GLSTLVEV 345
Cdd:PRK10476 333 GASAVVEL 340
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
57-355 |
1.65e-32 |
|
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: 124.29 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 57 VAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAASvrqtrqqminskqlqanidvkKTAL 136
Cdd:COG0845 19 EARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAA---------------------QAQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 137 AQAQADLNRRIPLGAANLIGREELQHARDTVASAQAELDvaiqqynanqaivlgtkleqqpavlQAATEVRNAWLALQRT 216
Cdd:COG0845 78 ELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALA-------------------------AAQAALEQARANLAYT 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 217 QIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKETQLAHMRIGQPATIISDIYgDDVKYTGKVVGLDmgt 296
Cdd:COG0845 133 TIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAG-PGKTFEGKVTFID--- 208
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 695798189 297 gsafsllPAQNATgnwikvVQRLPVRIEIDAkqlAQHPLRIGLSTLVEVDTSNREGEML 355
Cdd:COG0845 209 -------PAVDPA------TRTVRVRAELPN---PDGLLRPGMFVRVRIVLGERENALL 251
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
32-289 |
2.19e-18 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 85.01 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 32 VIVAVAYGIYWFLvlrhyEETDDA-YVAGN----QVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKT 106
Cdd:PRK03598 14 LAAAVAGGWWWYQ-----SRQDNGlTLYGNvdirTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 107 QLAAS-------VRQTRQQMInsKQLQANIDVKKTALAQAQADLNRRIPLGAANLIGREELQHARDTVASAQAELDVAIQ 179
Cdd:PRK03598 89 NVSVAqaqldlmLAGYRDEEI--AQARAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 180 QYNANQAivlGTKLEQ----QPAVLQAATEVRNAWLALQRTQIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVD 255
Cdd:PRK03598 167 KLSQYRE---GNRPQDiaqaKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVR 243
|
250 260 270
....*....|....*....|....*....|....
gi 695798189 256 ANFKETQLAHMRIGQPATIISDIYGDDVkYTGKV 289
Cdd:PRK03598 244 AYVDERNLGQAQPGRKVLLYTDGRPDKP-YHGQI 276
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
57-277 |
2.57e-18 |
|
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: 84.67 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 57 VAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAASvrqtrqqminskqlqanidvkKTAL 136
Cdd:TIGR01730 22 EAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAA---------------------EAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 137 AQAQADLNRRIPLGAANLIgreelqhardtvasAQAELDVAIQQYNANQAivlgtkleqqpAVLQAATEVRNAWLALQRT 216
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAV--------------SQADLDDAKAAVEAAQA-----------DLEAAKASLASAQLNLRYT 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695798189 217 QIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKETQLAHMRIGQPATIISD 277
Cdd:TIGR01730 136 EIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELD 196
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
32-334 |
4.87e-14 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 72.08 E-value: 4.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 32 VIVAVaygIYWFLVLRHYEE---TDDAYVAGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQL 108
Cdd:PRK10559 18 VILAF---IAIFRAWVFYTEspwTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 109 AasvrqTRQQMINSKQLQAnidvkktalaqaqadlNRRIPLGAAnligreelqhardtvASAQAELDvaiQQYNANQAIv 188
Cdd:PRK10559 95 A-----YYQVLAQEKRREA----------------GRRNRLGVQ---------------AMSREEID---QANNVLQTV- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 189 lgtklEQQPAVLQAATEVrnAWLALQRTQIVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKETQLAHMRI 268
Cdd:PRK10559 135 -----LHQLAKAQATRDL--AKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRP 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 695798189 269 GQPATIISdiYGDDVKYTGKVVGLDMGTGSAFSL-----LPAQNATGNWIKVVQRLPVRIEIDAKQLAQHP 334
Cdd:PRK10559 208 GYRAEITP--LGSNKVLKGTVDSVAAGVTNSSSTrdskgMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYP 276
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
168-289 |
3.04e-09 |
|
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: 56.75 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 168 ASAQAELDVAIQQYNANQAIVLGTKLEQQPAVLQAATEVRNAWLALQRTQ----IVSPISGYVSRRSVQPGAQIGTTTPL 243
Cdd:pfam16576 57 VAAQQEYLLALRSGDALSKSELLRAARQRLRLLGMPEAQIAELERTGKVQptvtVYAPISGVVTELNVREGMYVQPGDTL 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 695798189 244 MAVVPATNLWVDANFKETQLAHMRIGQPATIISDIYGDDVkYTGKV 289
Cdd:pfam16576 137 FTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKT-FEGKV 181
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
218-334 |
2.82e-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: 51.21 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 218 IVSPISGYVSRRSVQPGAQIGTTTPLMAVVPATNLWVDANFKETQLAHMRIGQPATIISDiYGDDVKYTGKVVgldmgtg 297
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLD-PGSDYTLEGKVV------- 73
|
90 100 110
....*....|....*....|....*....|....*..
gi 695798189 298 safSLLPAQNATGNWIKVVqrlpVRIEIDAKQLAQHP 334
Cdd:pfam13437 74 ---RISPTVDPDTGVIPVR----VSIENPKTPIPLLP 103
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
58-246 |
6.86e-05 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 44.78 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 58 AGNQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAASvrqtrqqminskqlqanidvkKTALA 137
Cdd:PRK11556 84 AANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKD---------------------QATLA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 138 QAQADLNRRIPLGAANLIGREELQHARDTVASAQAELdvaiqqyNANQAivlgtkleqqpavlqaatEVRNAWLALQRTQ 217
Cdd:PRK11556 143 NARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTI-------KADEA------------------SVASAQLQLDYSR 197
|
170 180 190
....*....|....*....|....*....|.
gi 695798189 218 IVSPISGYVSRRSVQPGAQI--GTTTPLMAV 246
Cdd:PRK11556 198 ITAPISGRVGLKQVDVGNQIssGDTTGIVVI 228
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
63-237 |
1.65e-04 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 43.55 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 63 QIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAASvrqtrqqminskqlqanidvkKTALAQAQAD 142
Cdd:PRK09859 63 EIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKA---------------------LSTASNARIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 143 LNRRIPLGAANLIGREELQHARDTVASAQAELDVAiqqynanqaivlgtkleqQPAVLQAAtevrnawLALQRTQIVSPI 222
Cdd:PRK09859 122 FNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVA------------------KAAVEQAT-------INLQYANVTSPI 176
|
170
....*....|....*
gi 695798189 223 SGYVSRRSVQPGAQI 237
Cdd:PRK09859 177 TGVSGKSSVTVGALV 191
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
60-109 |
3.27e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 38.19 E-value: 3.27e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 695798189 60 NQVQIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLA 109
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
63-255 |
1.92e-03 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 40.08 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 63 QIMAQVSGSVTKVWADNTDFVQQGDPLVTLDQTDAQQAFEKAKTQLAASvrqtrqqminskQLQANIdvkktalaqAQAD 142
Cdd:PRK15030 67 EVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKA------------QAAANI---------AQLT 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 695798189 143 LNRRIPLGAANLIGREELQHArdtVASAQaeldvaiqQYNAnqaivlgtkleqqpAVLQAATEVRNAWLALQRTQIVSPI 222
Cdd:PRK15030 126 VNRYQKLLGTQYISKQEYDQA---LADAQ--------QANA--------------AVTAAKAAVETARINLAYTKVTSPI 180
|
170 180 190
....*....|....*....|....*....|....*
gi 695798189 223 SGYVSRRSVQPGA--QIGTTTPLMAVVPATNLWVD 255
Cdd:PRK15030 181 SGRIGKSNVTEGAlvQNGQATALATVQQLDPIYVD 215
|
|
|