|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
13-331 |
1.02e-55 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 184.87 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 13 ISLAGFVVLFLYFVIADLYMPVTPQARVYHPVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYD 92
Cdd:COG1566 14 LLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 93 DAKLQNQRLDSSVKAIEAQLAAAQAKLHEQTLL------FERGESLLKKRSISDQEYETINANYQSSKANVAAIEAQLSE 166
Cdd:COG1566 94 AAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLdlaqreLERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 167 AKLA---RGKIGDDNLALRHAQNQLEQAKLNLSYTTVTADTDGKTANLQVTPGTYANKGQPLMAIV-ANKADLVADFREK 242
Cdd:COG1566 174 AQAGlreEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVpLDDLWVEAYVPET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 243 SLVHVQIGSTAKVSFDALPGKVFTGKIVSFEAGVSDGQLNANGLLsatessnrwvRDAQRQRIHIQLDEHQmLAKFPSGA 322
Cdd:COG1566 254 DLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNATG----------NVVQRYPVRIRLDNPD-PEPLRPGM 322
|
....*....
gi 2544577432 323 RATVQLLPD 331
Cdd:COG1566 323 SATVEIDTE 331
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
15-333 |
5.36e-38 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 139.01 E-value: 5.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 15 LAGFVVLFLYFVI--ADLYmPVTPQARVYHPVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAE--LA 90
Cdd:PRK10476 18 IVALAIVALVFVIwrTDSA-PSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQadLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 91 YDDAKLQN-------QRLDSSVKAIEAQLAAAQAKLHEQTLlfERGESLLKKRSISDQEYEtinanyqssKANVA--AIE 161
Cdd:PRK10476 97 LADAQIMTtqrsvdaERSNAASANEQVERARANAKLATRTL--ERLEPLLAKGYVSAQQVD---------QARTAqrDAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 162 AQLSEAKL----ARGKIGDDN--LALRHA-QNQLEQAKLNLSYTTVTADTDGKTANLQVTPGTYANKGQPLMAIVANKA- 233
Cdd:PRK10476 166 VSLNQALLqaqaAAAAVGGVDalVAQRAArEAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHw 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 234 DLVADFREKSLVHVQIGSTAKVSFDALPGKVFTGKIVSFEAGV-SDGQLNANGLLSATESSNRWVRDAQRQRIHIQLDE- 311
Cdd:PRK10476 246 YAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIGWGVlPDDGGNVPRGLPYVPRSINWVRVAQRFPVRIMLDKp 325
|
330 340
....*....|....*....|..
gi 2544577432 312 HQMLAKFpsGARATVQLLPDSS 333
Cdd:PRK10476 326 DPELFRI--GASAVVELRPGAA 345
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
33-278 |
5.23e-30 |
|
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: 116.75 E-value: 5.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 33 PVTPQARVYHPVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYDDAKLQNQRLDSSVKAIEAQL 112
Cdd:pfam00529 9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 113 AAAQAKLHEQTLL------------------------FERGESLLKKRSISDQEYETINANYQSSKANVAAIEAQLSE-- 166
Cdd:pfam00529 89 SELAISRQDYDGAtaqlraaqaavkaaqaqlaqaqidLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQiy 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 167 ----------AKLARGKIGDDNLALRHAQNQLEQAKLNLSYTTVTADTDGKTANLQVTP-GTYANKGQPLMAIVANKADL 235
Cdd:pfam00529 169 vqitqsaaenQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNLL 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2544577432 236 V-ADFREKSLVHVQIGSTAKVSFDALPGKV---FTGKIVSFEAGVSD 278
Cdd:pfam00529 249 VpGMFVETQLDQVRVGQPVLIPFDAFPQTKtgrFTGVVVGISPDTGP 295
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
45-269 |
1.98e-26 |
|
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: 107.02 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 45 VQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYDDAKLQnqrldssvkaieaqlaaaqakLHEQTL 124
Cdd:TIGR01730 27 ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQ---------------------LELAQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 125 LFERGESLLKKRSISDQEYETINANYQSSKANVAAIEAqlseaklargkigddnlalrhaqnQLEQAKLNLSYTTVTADT 204
Cdd:TIGR01730 86 SFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKA------------------------SLASAQLNLRYTEIRAPF 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544577432 205 DGKTANLQVTPGTYANKGQPLMAIVAN-KADLVADFREKSLVHVQIGSTAKVSFDALPGKVFTGKI 269
Cdd:TIGR01730 142 DGTIGRRLVEVGAYVTAGQTLATIVDLdPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
13-331 |
1.02e-55 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 184.87 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 13 ISLAGFVVLFLYFVIADLYMPVTPQARVYHPVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYD 92
Cdd:COG1566 14 LLLLALGLALWAAGRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 93 DAKLQNQRLDSSVKAIEAQLAAAQAKLHEQTLL------FERGESLLKKRSISDQEYETINANYQSSKANVAAIEAQLSE 166
Cdd:COG1566 94 AAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLdlaqreLERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 167 AKLA---RGKIGDDNLALRHAQNQLEQAKLNLSYTTVTADTDGKTANLQVTPGTYANKGQPLMAIV-ANKADLVADFREK 242
Cdd:COG1566 174 AQAGlreEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVpLDDLWVEAYVPET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 243 SLVHVQIGSTAKVSFDALPGKVFTGKIVSFEAGVSDGQLNANGLLsatessnrwvRDAQRQRIHIQLDEHQmLAKFPSGA 322
Cdd:COG1566 254 DLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNATG----------NVVQRYPVRIRLDNPD-PEPLRPGM 322
|
....*....
gi 2544577432 323 RATVQLLPD 331
Cdd:COG1566 323 SATVEIDTE 331
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
15-333 |
5.36e-38 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 139.01 E-value: 5.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 15 LAGFVVLFLYFVI--ADLYmPVTPQARVYHPVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAE--LA 90
Cdd:PRK10476 18 IVALAIVALVFVIwrTDSA-PSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQadLA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 91 YDDAKLQN-------QRLDSSVKAIEAQLAAAQAKLHEQTLlfERGESLLKKRSISDQEYEtinanyqssKANVA--AIE 161
Cdd:PRK10476 97 LADAQIMTtqrsvdaERSNAASANEQVERARANAKLATRTL--ERLEPLLAKGYVSAQQVD---------QARTAqrDAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 162 AQLSEAKL----ARGKIGDDN--LALRHA-QNQLEQAKLNLSYTTVTADTDGKTANLQVTPGTYANKGQPLMAIVANKA- 233
Cdd:PRK10476 166 VSLNQALLqaqaAAAAVGGVDalVAQRAArEAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHw 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 234 DLVADFREKSLVHVQIGSTAKVSFDALPGKVFTGKIVSFEAGV-SDGQLNANGLLSATESSNRWVRDAQRQRIHIQLDE- 311
Cdd:PRK10476 246 YAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIGWGVlPDDGGNVPRGLPYVPRSINWVRVAQRFPVRIMLDKp 325
|
330 340
....*....|....*....|..
gi 2544577432 312 HQMLAKFpsGARATVQLLPDSS 333
Cdd:PRK10476 326 DPELFRI--GASAVVELRPGAA 345
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
45-279 |
3.23e-35 |
|
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: 130.83 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 45 VQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYDdaklqnqrldssvkaieaqlaAAQAKLHEQTL 124
Cdd:COG0845 24 VEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLA---------------------AAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 125 LFERGESLLKKRSISDQEYETINANYQSSKANVAAieaqlseaklargkigddnlalrhAQNQLEQAKLNLSYTTVTADT 204
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAA------------------------AQAALEQARANLAYTTIRAPF 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544577432 205 DGKTANLQVTPGTYANKGQPLMAIVA-NKADLVADFREKSLVHVQIGSTAKVSFDALPGKVFTGKIVSFEAGVSDG 279
Cdd:COG0845 139 DGVVGERNVEPGQLVSAGTPLFTIADlDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPA 214
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
33-278 |
5.23e-30 |
|
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: 116.75 E-value: 5.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 33 PVTPQARVYHPVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYDDAKLQNQRLDSSVKAIEAQL 112
Cdd:pfam00529 9 EAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 113 AAAQAKLHEQTLL------------------------FERGESLLKKRSISDQEYETINANYQSSKANVAAIEAQLSE-- 166
Cdd:pfam00529 89 SELAISRQDYDGAtaqlraaqaavkaaqaqlaqaqidLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQiy 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 167 ----------AKLARGKIGDDNLALRHAQNQLEQAKLNLSYTTVTADTDGKTANLQVTP-GTYANKGQPLMAIVANKADL 235
Cdd:pfam00529 169 vqitqsaaenQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNLL 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2544577432 236 V-ADFREKSLVHVQIGSTAKVSFDALPGKV---FTGKIVSFEAGVSD 278
Cdd:pfam00529 249 VpGMFVETQLDQVRVGQPVLIPFDAFPQTKtgrFTGVVVGISPDTGP 295
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
45-269 |
1.98e-26 |
|
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: 107.02 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 45 VQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYDDAKLQnqrldssvkaieaqlaaaqakLHEQTL 124
Cdd:TIGR01730 27 ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQ---------------------LELAQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 125 LFERGESLLKKRSISDQEYETINANYQSSKANVAAIEAqlseaklargkigddnlalrhaqnQLEQAKLNLSYTTVTADT 204
Cdd:TIGR01730 86 SFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKA------------------------SLASAQLNLRYTEIRAPF 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544577432 205 DGKTANLQVTPGTYANKGQPLMAIVAN-KADLVADFREKSLVHVQIGSTAKVSFDALPGKVFTGKI 269
Cdd:TIGR01730 142 DGTIGRRLVEVGAYVTAGQTLATIVDLdPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKL 207
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
6-326 |
8.54e-24 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 99.43 E-value: 8.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 6 KFARY---VKISLAGFVVLFLYFViadLYM--PVTPQARVYHPVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPF 80
Cdd:PRK10559 7 KISRTaitLVLVILAFIAIFRAWV---FYTesPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 81 ELAVQQAE--LAYDDAKLQNQRLDSSVKAIeaqlaaaqaklheqtllfergeslLKKRSISDQEYETINANYQSSkanva 158
Cdd:PRK10559 84 QKALAEAEadVAYYQVLAQEKRREAGRRNR------------------------LGVQAMSREEIDQANNVLQTV----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 159 aieaqlsEAKLARgkigddnlalrhAQNQLEQAKLNLSYTTVTADTDGKTANLQVTPGTYANKGQPLMAIVA-NKADLVA 237
Cdd:PRK10559 135 -------LHQLAK------------AQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKqNSFYVLA 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 238 DFREKSLVHVQIGSTAKVSfdalP---GKVFTGKIVSFEAGVSDGQLNANGLLSATESSN-RWVRDAQRQRIHIQLDeHQ 313
Cdd:PRK10559 196 YMEETKLEGVRPGYRAEIT----PlgsNKVLKGTVDSVAAGVTNSSSTRDSKGMATIDSNlEWVRLAQRVPVRIRLD-NQ 270
|
330
....*....|...
gi 2544577432 314 MLAKFPSGARATV 326
Cdd:PRK10559 271 QGNLYPAGTTATV 283
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
45-319 |
9.42e-18 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 83.59 E-value: 9.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 45 VQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYDDAKLQNQRLDSSVKAIEAQLAAAQAKLHEQTL 124
Cdd:PRK15136 62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQAQS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 125 LFERGESLLKKRSISDQEYetinanyQSSKANVAAIEAQLSEAK----LARGKIGDDNL----ALRHAQNQLEQAKLNLS 196
Cdd:PRK15136 142 DLNRRVPLGNANLIGREEL-------QHARDAVASAQAQLDVAIqqynANQAMILNTPLedqpAVQQAATEVRNAWLALQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 197 YTTVTADTDGKTANLQVTPGTYANKGQPLMAIV-ANKADLVADFREKSLVHVQIGSTAKVSFDAL-PGKVFTGKIVsfea 274
Cdd:PRK15136 215 RTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVpATNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVV---- 290
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2544577432 275 GVSDGQLNANGLLSATESSNRWVRDAQRQRIHIQLDEHQmLAKFP 319
Cdd:PRK15136 291 GLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQ-LAQHP 334
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
141-269 |
6.07e-11 |
|
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: 61.37 E-value: 6.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 141 QEYetINAnYQSSKANVAAIEAQLSEAKLArgkigddNLALRHAQ-NQLEQAKLNLSYTTVTADTDGKTANLQVTPGTYA 219
Cdd:pfam16576 61 QEY--LLA-LRSGDALSKSELLRAARQRLR-------LLGMPEAQiAELERTGKVQPTVTVYAPISGVVTELNVREGMYV 130
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2544577432 220 NKGQPLMAIvankADL-----VADFREKSLVHVQIGSTAKVSFDALPGKVFTGKI 269
Cdd:pfam16576 131 QPGDTLFTI----ADLstvwvEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKV 181
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
45-269 |
1.18e-10 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 61.90 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 45 VQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYDDAKLQNQRL-----DSSVKAIEAQLAAAQAKL 119
Cdd:PRK03598 44 VNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDLMlagyrDEEIAQARAAVKQAQAAY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 120 HEQTLLFERGESLLKKRSISDQEYETINANYQSSKANVAAIEAQLSEakLARG----KIGDDNLALRHAQNQLEQAKLNL 195
Cdd:PRK03598 124 DYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLSQ--YREGnrpqDIAQAKASLAQAQAALAQAELNL 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2544577432 196 SYTTVTADTDGKTANLQVTPGTYANKGQPLMAIVANKADLV-ADFREKSLVHVQIGSTAKVSFDALPGKVFTGKI 269
Cdd:PRK03598 202 QDTELIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVrAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQI 276
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
43-88 |
3.28e-09 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 52.06 E-value: 3.28e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2544577432 43 PVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAE 88
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAE 46
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
46-224 |
1.69e-08 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 55.57 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 46 QVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYddAKLQNQRLDSSVKAieaqlaaaqaklheqtll 125
Cdd:PRK09578 65 EVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGAL--AKAEAAHLAALDKR------------------ 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 126 fERGESLLKKRSISDQEYETINANYQSSKANVAAieaqlseaklargkigddnlalrhAQNQLEQAKLNLSYTTVTADTD 205
Cdd:PRK09578 125 -RRYDDLVRDRAVSERDYTEAVADERQAKAAVAS------------------------AKAELARAQLQLDYATVTAPID 179
|
170
....*....|....*....
gi 2544577432 206 GKTANLQVTPGTYANKGQP 224
Cdd:PRK09578 180 GRARRALVTEGALVGQDQA 198
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
45-222 |
1.20e-06 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 49.79 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 45 VQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAE--LAYDDAKLQNQRLDssvkaieaqlaaaqaklheq 122
Cdd:PRK11556 88 VTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQgqLAKDQATLANARRD-------------------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 123 tllFERGESLLKKRSISDQEYETINANYQSSKANVAAIEAQLSeaklargkigddnlalrhaqnqleQAKLNLSYTTVTA 202
Cdd:PRK11556 148 ---LARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVA------------------------SAQLQLDYSRITA 200
|
170 180
....*....|....*....|
gi 2544577432 203 DTDGKTANLQVTPGTYANKG 222
Cdd:PRK11556 201 PISGRVGLKQVDVGNQISSG 220
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
36-282 |
2.42e-06 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 48.94 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 36 PQARVYHPVVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAE--LAYDDAKLQNQRLDssvkaieaqla 113
Cdd:PRK09859 53 PGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKgsLAKALSTASNARIT----------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 114 aaqaklheqtllFERGESLLKKRSISDQEYETINANYQSSKANVAAieaqlseaklargkigddnlalrhAQNQLEQAKL 193
Cdd:PRK09859 122 ------------FNRQASLLKTNYVSRQDYDTARTQLNEAEANVTV------------------------AKAAVEQATI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 194 NLSYTTVTADTDGKTANLQVTPGTYankgqplmaIVANKADLVADFREKSLVHVQIGSTAKvSFDALPGKVFTGKIVSFE 273
Cdd:PRK09859 166 NLQYANVTSPITGVSGKSSVTVGAL---------VTANQADSLVTVQRLDPIYVDLTQSVQ-DFLRMKEEVASGQIKQVQ 235
|
....*....
gi 2544577432 274 aGVSDGQLN 282
Cdd:PRK09859 236 -GSTPVQLN 243
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
45-269 |
8.06e-06 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 47.08 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 45 VQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDEPFELAVQQAELAYDDAKLQNQRldssvkaieaqlaaAQAKLHEQTL 124
Cdd:PRK11578 62 VDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQ--------------AEAELKLARV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 125 LFERGESLLKKRSISDQEYETINANYQSSKANVAAIEAQlseaklargkigddnlaLRHAQNQLEQAKLNLSYTTVTADT 204
Cdd:PRK11578 128 TLSRQQRLAKTQAVSQQDLDTAATELAVKQAQIGTIDAQ-----------------IKRNQASLDTAKTNLDYTRIVAPM 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2544577432 205 DGKTANLQVTPG--TYANKGQPLMAIVANKADLV--ADFREKSLVHVQIGStaKVSFDAL--PGKVFTGKI 269
Cdd:PRK11578 191 AGEVTQITTLQGqtVIAAQQAPNILTLADMSTMLvkAQVSEADVIHLKPGQ--KAWFTVLgdPLTRYEGVL 259
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
44-223 |
1.69e-05 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 46.25 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 44 VVQVTPQVSGRVTDVLVTNNQAVEKQQALFKINDepfelAVQQAelAYDDAKLQNQRLDSSVKAIEaqlaaaqaklheqt 123
Cdd:PRK15030 65 IAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDP-----ATYQA--TYDSAKGDLAKAQAAANIAQ-------------- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544577432 124 LLFERGESLLKKRSISDQEYETINANYQSSKANVAAieaqlseaklargkigddnlalrhAQNQLEQAKLNLSYTTVTAD 203
Cdd:PRK15030 124 LTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTA------------------------AKAAVETARINLAYTKVTSP 179
|
170 180
....*....|....*....|
gi 2544577432 204 TDGKTANLQVTPGTYANKGQ 223
Cdd:PRK15030 180 ISGRIGKSNVTEGALVQNGQ 199
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
51-75 |
5.02e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 36.80 E-value: 5.02e-03
10 20
....*....|....*....|....*
gi 2544577432 51 VSGRVTDVLVTNNQAVEKQQALFKI 75
Cdd:COG0511 111 VSGTVVEILVENGQPVEYGQPLFVI 135
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
199-271 |
8.55e-03 |
|
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: 35.42 E-value: 8.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544577432 199 TVTADTDGKTANLQVTPGTYANKGQPLMAIVA-NKADLVADFREKSLVHVQIGSTAKVSFDALPGKVFTGKIVS 271
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPpDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVR 74
|
|
|