|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
2-332 |
0e+00 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 555.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 2 MKKPVVIGLAVVVLAAVVAGGYWWYQSRQDNGLTLYGNVDIRTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYE 81
Cdd:PRK03598 1 MKKKVVIGLAVVVLAAAVAGGWWWYQSRQDNGLTLYGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 82 IALMQAKAGVSVAQAQYDLMLAGYRDEEIAQAAAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQAT 161
Cdd:PRK03598 81 NALMQAKANVSVAQAQLDLMLAGYRDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 162 LKSAQDKLRQYRSGNREQDIAQAKASLEQAQAQLAQAELNLQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPV 241
Cdd:PRK03598 161 LKSAQDKLSQYREGNRPQDIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 242 WVRAYVDERNLDQAQPGRKVLLYTDGRPNKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDADDALRQGMPV 321
Cdd:PRK03598 241 WVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDADDALRQGMPV 320
|
330
....*....|.
gi 31563262 322 TVQFGDEAGHE 332
Cdd:PRK03598 321 TVRFADEAGHE 331
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
23-325 |
4.73e-72 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 226.47 E-value: 4.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 23 YWWYQSRQDNGLTLYGNVDIRTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQYDLML 102
Cdd:COG1566 24 WAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 103 AGY-RDEEIAQAAAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLRQYRSGNREQ-D 180
Cdd:COG1566 104 AELgAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEeE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 181 IAQAKASLEQAQAQLAQAELNLQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRK 260
Cdd:COG1566 184 LAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQP 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31563262 261 VLLYTDGRPNKPYHGQIGFVSPTAEFTPkTVETPDLRTDLVYRLRIVVTDAD-DALRQGMPVTVQF 325
Cdd:COG1566 264 VEVRVDAYPDRVFEGKVTSISPGAGFTS-PPKNATGNVVQRYPVRIRLDNPDpEPLRPGMSATVEI 328
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
45-323 |
1.95e-31 |
|
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: 120.11 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 45 VNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQYDLmlagyrdeeiaqaaaavkqaqaay 124
Cdd:TIGR01730 27 ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL------------------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 125 dyAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLRQyrsgnreqdiaqakasleqaqaqlaqAELNLQD 204
Cdd:TIGR01730 83 --AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLAS--------------------------AQLNLRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 205 STLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGRPNKPYHGQIGFVSPTA 284
Cdd:TIGR01730 135 TEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRV 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 31563262 285 EFTPKTvetpdlrtdlvYRLRIVVTDADDALRQGMPVTV 323
Cdd:TIGR01730 215 DSGTGT-----------VRVRATFPNPDGRLLPGMFGRV 242
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
43-312 |
2.93e-20 |
|
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: 89.40 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 43 RTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQ---YDLMLAGYRDEEIAQAAAAVKQ 119
Cdd:pfam00529 19 NAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQvarLQAELDRLQALESELAISRQDY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 120 AQAAYDY----------------AQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQ---DKLRQYRSGN---- 176
Cdd:pfam00529 99 DGATAQLraaqaavkaaqaqlaqAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVaqlDQIYVQITQSaaen 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 177 ---REQDIAQAKASLEQAQAQLAQAELNLQDSTLVAPSDGTLLTRAVEP-GTVLNEGGTVFTVSLTRPVWVRAYVDERNL 252
Cdd:pfam00529 179 qaeVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNLLVPGMFVETQL 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 253 DQAQPGRKVLLYTDGRPNKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDAD 312
Cdd:pfam00529 259 DQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGA 318
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
2-332 |
0e+00 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 555.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 2 MKKPVVIGLAVVVLAAVVAGGYWWYQSRQDNGLTLYGNVDIRTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYE 81
Cdd:PRK03598 1 MKKKVVIGLAVVVLAAAVAGGWWWYQSRQDNGLTLYGNVDIRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 82 IALMQAKAGVSVAQAQYDLMLAGYRDEEIAQAAAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQAT 161
Cdd:PRK03598 81 NALMQAKANVSVAQAQLDLMLAGYRDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 162 LKSAQDKLRQYRSGNREQDIAQAKASLEQAQAQLAQAELNLQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPV 241
Cdd:PRK03598 161 LKSAQDKLSQYREGNRPQDIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 242 WVRAYVDERNLDQAQPGRKVLLYTDGRPNKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDADDALRQGMPV 321
Cdd:PRK03598 241 WVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDADDALRQGMPV 320
|
330
....*....|.
gi 31563262 322 TVQFGDEAGHE 332
Cdd:PRK03598 321 TVRFADEAGHE 331
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
23-325 |
4.73e-72 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 226.47 E-value: 4.73e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 23 YWWYQSRQDNGLTLYGNVDIRTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQYDLML 102
Cdd:COG1566 24 WAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 103 AGY-RDEEIAQAAAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLRQYRSGNREQ-D 180
Cdd:COG1566 104 AELgAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEeE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 181 IAQAKASLEQAQAQLAQAELNLQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRK 260
Cdd:COG1566 184 LAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQP 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31563262 261 VLLYTDGRPNKPYHGQIGFVSPTAEFTPkTVETPDLRTDLVYRLRIVVTDAD-DALRQGMPVTVQF 325
Cdd:COG1566 264 VEVRVDAYPDRVFEGKVTSISPGAGFTS-PPKNATGNVVQRYPVRIRLDNPDpEPLRPGMSATVEI 328
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
34-325 |
2.03e-52 |
|
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: 175.52 E-value: 2.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 34 LTLYGNVD-IRTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQYDLmlagyrdeeiaq 112
Cdd:COG0845 12 VEATGTVEaRREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLEL------------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 113 aaaavkqaqaaydyAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQdklrqyrsgnreqdiaqakasleqaq 192
Cdd:COG0845 80 --------------AKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQ-------------------------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 193 AQLAQAELNLQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGRPNKP 272
Cdd:COG0845 120 AALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKT 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 31563262 273 YHGQIGFVSPTAEftpktvetPDLRTdlvYRLRIVVTDADDALRQGMPVTVQF 325
Cdd:COG0845 200 FEGKVTFIDPAVD--------PATRT---VRVRAELPNPDGLLRPGMFVRVRI 241
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
45-323 |
1.95e-31 |
|
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: 120.11 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 45 VNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQYDLmlagyrdeeiaqaaaavkqaqaay 124
Cdd:TIGR01730 27 ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL------------------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 125 dyAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLRQyrsgnreqdiaqakasleqaqaqlaqAELNLQD 204
Cdd:TIGR01730 83 --AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLAS--------------------------AQLNLRY 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 205 STLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGRPNKPYHGQIGFVSPTA 284
Cdd:TIGR01730 135 TEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRV 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 31563262 285 EFTPKTvetpdlrtdlvYRLRIVVTDADDALRQGMPVTV 323
Cdd:TIGR01730 215 DSGTGT-----------VRVRATFPNPDGRLLPGMFGRV 242
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
43-312 |
2.93e-20 |
|
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: 89.40 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 43 RTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQ---YDLMLAGYRDEEIAQAAAAVKQ 119
Cdd:pfam00529 19 NAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQvarLQAELDRLQALESELAISRQDY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 120 AQAAYDY----------------AQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQ---DKLRQYRSGN---- 176
Cdd:pfam00529 99 DGATAQLraaqaavkaaqaqlaqAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVaqlDQIYVQITQSaaen 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 177 ---REQDIAQAKASLEQAQAQLAQAELNLQDSTLVAPSDGTLLTRAVEP-GTVLNEGGTVFTVSLTRPVWVRAYVDERNL 252
Cdd:pfam00529 179 qaeVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNLLVPGMFVETQL 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 253 DQAQPGRKVLLYTDGRPNKPYHGQIGFVSPTAEFTPKTVETPDLRTDLVYRLRIVVTDAD 312
Cdd:pfam00529 259 DQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGA 318
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
34-319 |
1.05e-18 |
|
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: 82.94 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 34 LTLYGNVDI---RTVNLSFRVGGRVESLAVD-EGDAIKAGQVLGELdhkpYEIALMQAkagvsvaQAQYdlmlagyrdee 109
Cdd:pfam16576 6 IRAVGRVAYderRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAEL----YSPELVAA-------QQEY----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 110 iaqaaaavkqaqaaydyaqnfynrqqglwksrtisandLENARSSRDQAQATL-KSAQDKLRQYrsGNREQDIAQAKASL 188
Cdd:pfam16576 64 --------------------------------------LLALRSGDALSKSELlRAARQRLRLL--GMPEAQIAELERTG 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 189 EQaqaqlaqaelnLQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGR 268
Cdd:pfam16576 104 KV-----------QPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPAL 172
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 31563262 269 PNKPYHGQIGFVSPTAEftPKTvetpdlRTdlvYRLRIVVTDADDALRQGM 319
Cdd:pfam16576 173 PGKTFEGKVDYIYPTLD--PKT------RT---VRVRIELPNPDGRLKPGM 212
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
40-277 |
2.67e-17 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 81.61 E-value: 2.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 40 VDIRTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAQYDL---MLAGYRdEEIAQAAAA 116
Cdd:PRK10476 44 IDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMTtqrSVDAER-SNAASANEQ 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 117 VKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLRQYRS--GNREQDIAQAKASleqaQAQ 194
Cdd:PRK10476 123 VERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQALLQAQAAAAavGGVDALVAQRAAR----EAA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 195 LAQAELNLQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGRPNKPYH 274
Cdd:PRK10476 199 LAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFE 278
|
...
gi 31563262 275 GQI 277
Cdd:PRK10476 279 GKV 281
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
206-318 |
1.90e-12 |
|
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: 62.76 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 206 TLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGRPNKPYHGQIGFVSPTae 285
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPT-- 78
|
90 100 110
....*....|....*....|....*....|...
gi 31563262 286 FTPKTVETPdlrtdlvYRLRIVVTDADDALRQG 318
Cdd:pfam13437 79 VDPDTGVIP-------VRVSIENPKTPIPLLPG 104
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
38-315 |
7.27e-12 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 65.57 E-value: 7.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 38 GNVD-IRTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKP-------YEIALMQAKAGVSVAQAQYDLmlagyrdee 109
Cdd:PRK11578 54 GKLDaLRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQaenqikeVEATLMELRAQRQQAEAELKL--------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 110 iaqaaaavkqaqaaydyAQNFYNRQQGLWKSRTISANDLenarssrDQAQATLksaqdKLRQYRSGNREQDIAQAKASle 189
Cdd:PRK11578 125 -----------------ARVTLSRQQRLAKTQAVSQQDL-------DTAATEL-----AVKQAQIGTIDAQIKRNQAS-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 190 qaqaqLAQAELNLQDSTLVAPSDGTLLT-RAVEPGTVL--NEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTD 266
Cdd:PRK11578 174 -----LDTAKTNLDYTRIVAPMAGEVTQiTTLQGQTVIaaQQAPNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVL 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 31563262 267 GRPNKPYHGQIGFVSPTAE------FTPKTVETPD----LRTDLVYRLRIVVTDADDAL 315
Cdd:PRK11578 249 GDPLTRYEGVLKDILPTPEkvndaiFYYARFEVPNpnglLRLDMTAQVHIQLTDVKNVL 307
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
54-325 |
4.67e-11 |
|
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members.
Pssm-ID: 213754 [Multi-domain] Cd Length: 327 Bit Score: 62.92 E-value: 4.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 54 RVESLAVDEGDAIKAGQVLGELDHKP---------------YEIALMQAKAGVS--VAQAQYDLMLAGYRDEEIAQAAAA 116
Cdd:TIGR02971 26 RIKKLLVAEGDRVQAGQVLAELDSRPertaeldvartqldeAKARLAQVRAGAKkgEIAAQRAARAAAKLFKDVAAQQAT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 117 VKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLRQYRSGN-----------REQDIAQAK 185
Cdd:TIGR02971 106 LNRLEAELETAQREVDRYRSLFRDGAVSASDLDSKALKLRTAEEELEEALASRSEQIDGAraalaslaeevRETDVDLAQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 186 ASLEQAQAQLAQAELNLQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVrAYVDERNLDQAQPGRKVLLYT 265
Cdd:TIGR02971 186 AEVKSALEAVQQAEALLELTYVKAPIDGRVLKIHAREGEVIGSEGILEMGDTSQMYAV-AEVYETDINRVRVGQRATITS 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31563262 266 DGRPnKPYHGQIGFVSPtaEFTPKTVETPDLRTDLVYRLRIVVT--DADDALR----QGMPVTVQF 325
Cdd:TIGR02971 265 TALS-GPLRGTVRRIGS--LIAKNDVLSTDPAADADARVVEVKIrlDPASSERvgrlTNLQVDVAI 327
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
44-166 |
3.68e-09 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 57.49 E-value: 3.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 44 TVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAqydlMLAGYRDeeiaqaaaavkqaqaa 123
Cdd:PRK11556 87 TVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQA----TLANARR---------------- 146
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 31563262 124 yDYAqnfynRQQGLWKSRTISANDLENARSSRDQAQATLKSAQ 166
Cdd:PRK11556 147 -DLA-----RYQQLAKTNLVSRQELDAQQALVSETEGTIKADE 183
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
43-92 |
1.46e-08 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 50.13 E-value: 1.46e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 31563262 43 RTVNLSFRVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVS 92
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
52-324 |
2.70e-08 |
|
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: 55.02 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 52 GGRVESLAVDEGDAIKAGQVLGELD-------HKPYEIALMQAKAGVSVAQA---------------------------- 96
Cdd:TIGR01843 51 GGIVREILVREGDRVKAGQVLVELDatdveadAAELESQVLRLEAEVARLRAeadsqaaiefpddllsaedpavpelikg 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 97 ---QYDLMLAGYRD--EEIAQAAAAVKQAQAAYDYAQNFYNRQQGLWKSRTISA-------------------------N 146
Cdd:TIGR01843 131 qqsLFESRKSTLRAqlELILAQIKQLEAELAGLQAQLQALRQQLEVISEELEARrklkekglvsrlellelereraeaqG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 147 DLENARSSRDQAQATLKSAQDKLRQYRSGNREQ---DIAQAKASLEQAQAQLAQAELNLQDSTLVAPSDGTLLTRAVEP- 222
Cdd:TIGR01843 211 ELGRLEAELEVLKRQIDELQLERQQIEQTFREEvleELTEAQARLAELRERLNKARDRLQRLIIRSPVDGTVQSLKVHTv 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 223 GTVLNEGGTVFT-VSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGRPNKPYhgqigfvsPTAEFTPKTVeTPDLRTD-- 299
Cdd:TIGR01843 291 GGVVQPGETLMEiVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRY--------GILNGKVKSI-SPDTFTDer 361
|
330 340 350
....*....|....*....|....*....|....*
gi 31563262 300 ---LVYRLRIVVTD-------ADDALRQGMPVTVQ 324
Cdd:TIGR01843 362 gggPYYRVRISIDQntlgigpKGLELSPGMPVTAD 396
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
51-277 |
2.12e-07 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 52.00 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 51 VGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGV--SVAQAqYDLMLAGyrdeeiAQAAAAVKQAQAAYDYAQ 128
Cdd:PRK15136 68 VSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALanSVRQT-HQLMINS------KQYQANIELQKTALAQAQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 129 NFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAqdkLRQYRSG-------NREQDIAQAKASLEQAQAQLAqaeln 201
Cdd:PRK15136 141 SDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVA---IQQYNANqamilntPLEDQPAVQQAATEVRNAWLA----- 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31563262 202 LQDSTLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTD--GRpNKPYHGQI 277
Cdd:PRK15136 213 LQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDiyGD-DVVYTGKV 289
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
50-322 |
1.16e-05 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 46.63 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 50 RVGGRVESLAVDEGDAIKAGQVLGELDHKPYEIALMQAKAGVSVAQAqydlmlagyrdeeiaqaaaavkqaqaAYDYAQN 129
Cdd:PRK09859 67 QVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALS--------------------------TASNARI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 130 FYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQdklrqyrsgnreQDIAQAkasleqaqaqlaqaELNLQDSTLVA 209
Cdd:PRK09859 121 TFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAK------------AAVEQA--------------TINLQYANVTS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 210 PSDGTLLTRAVEPGTVL--NEGGTVFTVSLTRPVWV------------RAYVDERNLDQAQPGRKVLLYTDGRPNKPYHG 275
Cdd:PRK09859 175 PITGVSGKSSVTVGALVtaNQADSLVTVQRLDPIYVdltqsvqdflrmKEEVASGQIKQVQGSTPVQLNLENGKRYSQTG 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 31563262 276 QIGFVSPTAEFTPKTVEtpdlrtdlvyrLRIVVTDADDALRQGMPVT 322
Cdd:PRK09859 255 TLKFSDPTVDETTGSVT-----------LRAIFPNPNGDLLPGMYVT 290
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
206-324 |
2.79e-03 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 39.08 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563262 206 TLVAPSDGTLLTRAVEPGTVLNEGGTVFTVSLTRPVWVRAYVDERNLDQAQPGRKVLLYTDGRPNKPYHGQIGFVSPTAE 285
Cdd:PRK09783 211 TLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVD 290
|
90 100 110
....*....|....*....|....*....|....*....
gi 31563262 286 FTPKTVEtpdlrtdlvyrLRIVVTDADDALRQGMPVTVQ 324
Cdd:PRK09783 291 AATRTLQ-----------LRLEVDNADEALKPGMNAWLQ 318
|
|
| |
