|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
14-383 |
1.62e-159 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 453.77 E-value: 1.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 14 KRKRWLLILLAMIVLATLASVAWEFFYGRWHEDTDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDAD 93
Cdd:PRK15136 19 KRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 94 IALQRAEANLAHTVRQVRGLFSNVDGYRAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHARDALDSAKASLTSSE 173
Cdd:PRK15136 99 QAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 174 QQLNTNRALVDDTQITSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALMAVVPLDQIWIDANF 253
Cdd:PRK15136 179 QQYNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 254 KETQLKHMRIGQPVEIRSDLYGSDVRYSGTVDSLGVGTGSAFSLLPAQNATGNWIKIVQRVPVRIHIDPQELQKHPLRIG 333
Cdd:PRK15136 259 KETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIG 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15600352 334 LSMDVKVDLHDQSGPALAQQPPREALFSTDVYQQQLASADKLIERLIEAN 383
Cdd:PRK15136 339 LSTLVTVDTANRDGQVLANQVRSTPAYESNALEIDLAPVNKLIDDIIQAN 388
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
15-340 |
5.91e-127 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 369.12 E-value: 5.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 15 RKRWLLILLAMIVLATLASVAWEFFYGRWHEDTDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADI 94
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 95 ALQRAEANLAHTVRQVRGLFSNVDGYRAEVATRKVALAKA-------EADYKRRKNLADDGAISQEELAHARDALDSAKA 167
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQArekllqaELDLRRRVPLFKKGLISREELDHARKALLSAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 168 SLTSS-EQQLNTNRALVDDTQITSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALMAVVPLDQ 246
Cdd:TIGR00998 161 ALNAAiQEQLNANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 247 IWIDANFKETQLKHMRIGQPVEIRSDLYGSDVRYSGTVDSLGVGTGSAFSLLPAQNATGNWIKIVQRVPVRIHIDPQELQ 326
Cdd:TIGR00998 241 MYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELD 320
|
330
....*....|....
gi 15600352 327 KHPLRIGLSMDVKV 340
Cdd:TIGR00998 321 EHPLRIGLSAEVEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
12-343 |
1.70e-88 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 270.77 E-value: 1.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 12 NPKRKRWLLILLAMIVLatlasVAWEFFYGRWHED---TDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFD 88
Cdd:COG1566 3 ALKKRRLLALVLLLLAL-----GLALWAAGRNGPDepvTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 89 PSDADIALQRAEANLAHTVRQVRGLFSN------VDGYRAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHARDAL 162
Cdd:COG1566 78 PTDLQAALAQAEAQLAAAEAQLARLEAElgaeaeIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 163 DSAKASLTSSEQQLNTNRALVD--DTQITSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALMA 240
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLReeEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 241 VVPLDQIWIDANFKETQLKHMRIGQPVEIRSDLYGsDVRYSGTVDSLGVGTGSAFsllPAQNATGNwikIVQRVPVRIHI 320
Cdd:COG1566 238 IVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYP-DRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRL 310
|
330 340
....*....|....*....|...
gi 15600352 321 DPQELqkHPLRIGLSMDVKVDLH 343
Cdd:COG1566 311 DNPDP--EPLRPGMSATVEIDTE 331
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
40-342 |
5.44e-65 |
|
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: 209.97 E-value: 5.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 40 YGRWHEDTDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQRAEANLAHTVRQVRGLFSNVDG 119
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 120 Y------------------------RAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHARDALDSAKASLTSSEQQ 175
Cdd:pfam00529 84 LqaleselaisrqdydgataqlraaQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 176 L-----------NTNRALVDDTQITSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQV-GQRVQPGNALMAVVP 243
Cdd:pfam00529 164 LdqiyvqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 244 LDQIWIDANFKETQLKHMRIGQPVEIRSDLYGSDV--RYSGTVDSLGVGTGsafsllpaqnatgnwikivqrvPVRIHID 321
Cdd:pfam00529 244 EDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRVVVD 301
|
330 340
....*....|....*....|.
gi 15600352 322 PQELQKHPLRIGLSMDVKVDL 342
Cdd:pfam00529 302 KAQGPYYPLRIGLSAGALVRL 322
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
14-383 |
1.62e-159 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 453.77 E-value: 1.62e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 14 KRKRWLLILLAMIVLATLASVAWEFFYGRWHEDTDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDAD 93
Cdd:PRK15136 19 KRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 94 IALQRAEANLAHTVRQVRGLFSNVDGYRAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHARDALDSAKASLTSSE 173
Cdd:PRK15136 99 QAFEKAKTALANSVRQTHQLMINSKQYQANIELQKTALAQAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 174 QQLNTNRALVDDTQITSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALMAVVPLDQIWIDANF 253
Cdd:PRK15136 179 QQYNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANF 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 254 KETQLKHMRIGQPVEIRSDLYGSDVRYSGTVDSLGVGTGSAFSLLPAQNATGNWIKIVQRVPVRIHIDPQELQKHPLRIG 333
Cdd:PRK15136 259 KETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIG 338
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 15600352 334 LSMDVKVDLHDQSGPALAQQPPREALFSTDVYQQQLASADKLIERLIEAN 383
Cdd:PRK15136 339 LSTLVTVDTANRDGQVLANQVRSTPAYESNALEIDLAPVNKLIDDIIQAN 388
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
15-340 |
5.91e-127 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 369.12 E-value: 5.91e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 15 RKRWLLILLAMIVLATLASVAWEFFYGRWHEDTDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADI 94
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 95 ALQRAEANLAHTVRQVRGLFSNVDGYRAEVATRKVALAKA-------EADYKRRKNLADDGAISQEELAHARDALDSAKA 167
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQArekllqaELDLRRRVPLFKKGLISREELDHARKALLSAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 168 SLTSS-EQQLNTNRALVDDTQITSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALMAVVPLDQ 246
Cdd:TIGR00998 161 ALNAAiQEQLNANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 247 IWIDANFKETQLKHMRIGQPVEIRSDLYGSDVRYSGTVDSLGVGTGSAFSLLPAQNATGNWIKIVQRVPVRIHIDPQELQ 326
Cdd:TIGR00998 241 MYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELD 320
|
330
....*....|....
gi 15600352 327 KHPLRIGLSMDVKV 340
Cdd:TIGR00998 321 EHPLRIGLSAEVEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
12-343 |
1.70e-88 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 270.77 E-value: 1.70e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 12 NPKRKRWLLILLAMIVLatlasVAWEFFYGRWHED---TDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFD 88
Cdd:COG1566 3 ALKKRRLLALVLLLLAL-----GLALWAAGRNGPDepvTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 89 PSDADIALQRAEANLAHTVRQVRGLFSN------VDGYRAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHARDAL 162
Cdd:COG1566 78 PTDLQAALAQAEAQLAAAEAQLARLEAElgaeaeIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 163 DSAKASLTSSEQQLNTNRALVD--DTQITSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALMA 240
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLReeEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 241 VVPLDQIWIDANFKETQLKHMRIGQPVEIRSDLYGsDVRYSGTVDSLGVGTGSAFsllPAQNATGNwikIVQRVPVRIHI 320
Cdd:COG1566 238 IVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYP-DRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRL 310
|
330 340
....*....|....*....|...
gi 15600352 321 DPQELqkHPLRIGLSMDVKVDLH 343
Cdd:COG1566 311 DNPDP--EPLRPGMSATVEIDTE 331
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
40-342 |
5.44e-65 |
|
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: 209.97 E-value: 5.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 40 YGRWHEDTDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQRAEANLAHTVRQVRGLFSNVDG 119
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 120 Y------------------------RAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHARDALDSAKASLTSSEQQ 175
Cdd:pfam00529 84 LqaleselaisrqdydgataqlraaQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 176 L-----------NTNRALVDDTQITSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQV-GQRVQPGNALMAVVP 243
Cdd:pfam00529 164 LdqiyvqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 244 LDQIWIDANFKETQLKHMRIGQPVEIRSDLYGSDV--RYSGTVDSLGVGTGsafsllpaqnatgnwikivqrvPVRIHID 321
Cdd:pfam00529 244 EDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRVVVD 301
|
330 340
....*....|....*....|.
gi 15600352 322 PQELQKHPLRIGLSMDVKVDL 342
Cdd:pfam00529 302 KAQGPYYPLRIGLSAGALVRL 322
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
55-363 |
4.02e-42 |
|
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: 150.48 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 55 NVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQRAEANLAHTvrqvrglfsnvdgyraevatrKVALAKA 134
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAA---------------------QAQLELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 135 EADYKRRKNLADDGAISQEELAHARDALDSAKAsltsseqqlntnralvddtqitshpDVKAAAAQLRQAYLDDARSTIV 214
Cdd:COG0845 81 KAELERYKALLKKGAVSQQELDQAKAALDQAQA-------------------------ALAAAQAALEQARANLAYTTIR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 215 APVTGYVAKRSVQVGQRVQPGNALMAVVPLDQIWIDANFKETQLKHMRIGQPVEIRSDLYgSDVRYSGTVDSLGvgtgsa 294
Cdd:COG0845 136 APFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAG-PGKTFEGKVTFID------ 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600352 295 fsllPAQNATgnwikiVQRVPVRIHIDPQElqkHPLRIGLSMDVKVDLhDQSGPALAQqpPREALFSTD 363
Cdd:COG0845 209 ----PAVDPA------TRTVRVRAELPNPD---GLLRPGMFVRVRIVL-GERENALLV--PASAVVRDG 261
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
7-340 |
2.20e-40 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 146.33 E-value: 2.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 7 ETPAGNPKRKRWLLILLAMIVLATLASVAWEFfygRWHEDTDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVR 86
Cdd:PRK10476 2 ESTPKKSPRKKLPALAIVALAIVALVFVIWRT---DSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 87 FDP-------SDADIALQRAEANLAHTVRQVRGLFSNVDGYRAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHAR 159
Cdd:PRK10476 79 IDPrpyeltvAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 160 DALDSAKASLTSSEQQLNTNRALVDDTQiTSHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALM 239
Cdd:PRK10476 159 TAQRDAEVSLNQALLQAQAAAAAVGGVD-ALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 240 AVVPLDQIWIDANFKETQLKHMRIGQPVEIRSdLYGSDVRYSGTVDSLGVGTGSAFSL-----LPAQNATGNWIKIVQRV 314
Cdd:PRK10476 238 TLIDTDHWYAIANFRETDLKNIRVGDCATVYS-MIDRGRPFEGKVDSIGWGVLPDDGGnvprgLPYVPRSINWVRVAQRF 316
|
330 340
....*....|....*....|....*...
gi 15600352 315 PVRIHID--PQELqkhpLRIGLSMDVKV 340
Cdd:PRK10476 317 PVRIMLDkpDPEL----FRIGASAVVEL 340
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
54-287 |
4.07e-27 |
|
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: 109.71 E-value: 4.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 54 GNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQRAeanlahtvrqvrglfsnvdgyRAEVATRKVALAK 133
Cdd:TIGR01730 24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAA---------------------LAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 134 AEADYKRRKNLADDGAISQEELAHARDALDSAKAsltsseqqlntnralvddtqitshpDVKAAAAQLRQAYLDDARSTI 213
Cdd:TIGR01730 83 AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQA-------------------------DLEAAKASLASAQLNLRYTEI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600352 214 VAPVTGYVAKRSVQVGQRVQPGNALMAVVPLDQIWIDANFKETQLKHMRIGQPVEIRSDLYGSDVrYSGTVDSL 287
Cdd:TIGR01730 138 RAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEE-FKGKLRFI 210
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
21-329 |
6.63e-26 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 106.36 E-value: 6.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 21 ILLAMIVLATLASV-AWEFFYGR-WhedTDDAYINGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQR 98
Cdd:PRK10559 13 ITLVLVILAFIAIFrAWVFYTESpW---TRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 99 AEANLAHtvrqvrglfsnvdgYRAeVATRKvalaKAEAdyKRRKNLADDgAISQEELahardalDSAKASLTSSEQQLnt 178
Cdd:PRK10559 90 AEADVAY--------------YQV-LAQEK----RREA--GRRNRLGVQ-AMSREEI-------DQANNVLQTVLHQL-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 179 nralvddtqitshpdvKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALMAVVPLDQIWIDANFKETQL 258
Cdd:PRK10559 139 ----------------AKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKL 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15600352 259 KHMRIGQPVEIRSdlYGSDVRYSGTVDSLGVGTGSAFSL-----LPAQNATGNWIKIVQRVPVRIHIDPQELQKHP 329
Cdd:PRK10559 203 EGVRPGYRAEITP--LGSNKVLKGTVDSVAAGVTNSSSTrdskgMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYP 276
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
14-284 |
9.78e-26 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 106.20 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 14 KRKRWLLILLAMIVLATLASVAWeffygrWHEDTDDA-YINGNV----VQITPQIVGTVVSIGADDGDLVRKGQELVRFD 88
Cdd:PRK03598 2 KKKVVIGLAVVVLAAAVAGGWWW------YQSRQDNGlTLYGNVdirtVNLGFRVGGRLASLAVDEGDAVKAGQVLGELD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 89 PSDADIALQRAEANLAhtVRQVRgLFSNVDGYR--------AEVATRKVALAKAEADYKRRKNLADDGAISQEELAHARD 160
Cdd:PRK03598 76 AAPYENALMQAKANVS--VAQAQ-LDLMLAGYRdeeiaqarAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 161 ALDSAKASLTSSEQQLNTNRALVDDTQIT-SHPDVKAAAAQLRQAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPGNALM 239
Cdd:PRK03598 153 SRDQAQATLKSAQDKLSQYREGNRPQDIAqAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVF 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15600352 240 aVVPLDQ-IWIDANFKETQLKHMRIGQPVEIRSDlYGSDVRYSGTV 284
Cdd:PRK03598 233 -TLSLTRpVWVRAYVDERNLGQAQPGRKVLLYTD-GRPDKPYHGQI 276
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
53-343 |
3.44e-16 |
|
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: 79.67 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 53 NGNVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSD----------------ADIALQRAEAN-------------- 102
Cdd:TIGR01843 40 SGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDveadaaelesqvlrleAEVARLRAEADsqaaiefpddllsa 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 103 ----LAHTVRQVRGLF---------------SNVDGYRAEVATRKVALAKAEAD---YKRR----KNLADDGAISQEELA 156
Cdd:TIGR01843 120 edpaVPELIKGQQSLFesrkstlraqlelilAQIKQLEAELAGLQAQLQALRQQlevISEElearRKLKEKGLVSRLELL 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 157 HARDALDSAKASLTSSEQQLNTNRALVDDTQI--------------TSHPDVKAAAAQLRQAY--LDD--ARSTIVAPVT 218
Cdd:TIGR01843 200 ELERERAEAQGELGRLEAELEVLKRQIDELQLerqqieqtfreevlEELTEAQARLAELRERLnkARDrlQRLIIRSPVD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 219 GYVAKRSVQ-VGQRVQPGNALMAVVPL-DQIWIDANFKETQLKHMRIGQPVEIRSDLYGSdVRY---SGTVDSLGVgtgS 293
Cdd:TIGR01843 280 GTVQSLKVHtVGGVVQPGETLMEIVPEdDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPY-RRYgilNGKVKSISP---D 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15600352 294 AFSllpAQNATGNWIkivqrvPVRIHIDPQELQKHPLRIGLS--MDVKVDLH 343
Cdd:TIGR01843 356 TFT---DERGGGPYY------RVRISIDQNTLGIGPKGLELSpgMPVTADIK 398
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
152-285 |
6.39e-16 |
|
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: 76.01 E-value: 6.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 152 QEELAHARDALDSAKAS--LTSSEQQLntnRAL-VDDTQItshpdvkaaaAQLRQAYLDDARSTIVAPVTGYVAKRSVQV 228
Cdd:pfam16576 60 QQEYLLALRSGDALSKSelLRAARQRL---RLLgMPEAQI----------AELERTGKVQPTVTVYAPISGVVTELNVRE 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600352 229 GQRVQPGNALMAVVPLDQIWIDANFKETQLKHMRIGQPVEIRSDLYGsDVRYSGTVD 285
Cdd:pfam16576 127 GMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALP-GKTFEGKVD 182
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
75-338 |
5.12e-14 |
|
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: 72.17 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 75 GDLVRKGQELVRFDPSDADIA-LQRAEANLAHTVR---QVRG------------------LFSNVDGYRAEVATRKVALA 132
Cdd:TIGR02971 35 GDRVQAGQVLAELDSRPERTAeLDVARTQLDEAKArlaQVRAgakkgeiaaqraaraaakLFKDVAAQQATLNRLEAELE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 133 KAEADYKRRKNLADDGAISQEELAHARDALDSAKASLTS-----SEQQLNTNRALVDDTQITSHPDVKAAAAQLR----- 202
Cdd:TIGR02971 115 TAQREVDRYRSLFRDGAVSASDLDSKALKLRTAEEELEEalasrSEQIDGARAALASLAEEVRETDVDLAQAEVKsalea 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 203 --QAYLDDARSTIVAPVTGYVAKRSVQVGQRVQPgNALMAVVPLDQIWIDANFKETQLKHMRIGQPVEIRSDLYGSDVRy 280
Cdd:TIGR02971 195 vqQAEALLELTYVKAPIDGRVLKIHAREGEVIGS-EGILEMGDTSQMYAVAEVYETDINRVRVGQRATITSTALSGPLR- 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 281 sGTVDSLG--VGTGSAFSLLPAQNATGnwikivQRVPVRIHIDPQELQKHPLRIGLSMDV 338
Cdd:TIGR02971 273 -GTVRRIGslIAKNDVLSTDPAADADA------RVVEVKIRLDPASSERVGRLTNLQVDV 325
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
212-333 |
1.29e-11 |
|
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: 60.84 E-value: 1.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 212 TIVAPVTGYVAKRSVQVGQRVQPGNALMAVVPLDQIWIDANFKETQLKHMRIGQPVEIRSDlYGSDVRYSGTVDSLGvgt 291
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLD-PGSDYTLEGKVVRIS--- 76
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15600352 292 gsafsllPAQNATGnwikivQRVPVRIHIDPQELQKhPLRIG 333
Cdd:pfam13437 77 -------PTVDPDT------GVIPVRVSIENPKTPI-PLLPG 104
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
56-250 |
1.90e-09 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 58.96 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 56 VVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQRAEANLAHTVRqvrglfsnvdgyraevatrkvALAKAE 135
Cdd:PRK09859 61 VAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALS---------------------TASNAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 136 ADYKRRKNLADDGAISQEELAHARDALDSAKASLTsseqqlntnralvddtqitshpdvkAAAAQLRQAYLDDARSTIVA 215
Cdd:PRK09859 120 ITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVT-------------------------VAKAAVEQATINLQYANVTS 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600352 216 PVTGYVAKRSVQVGQRV--QPGNALMAVVPLDQIWID 250
Cdd:PRK09859 175 PITGVSGKSSVTVGALVtaNQADSLVTVQRLDPIYVD 211
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
55-248 |
4.78e-09 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 57.88 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 55 NVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQRAEANLAHTvrqvrglfsnvdgyraevatrKVALAKA 134
Cdd:PRK11556 86 NTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKD---------------------QATLANA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 135 EADYKRRKNLADDGAISQeelahardaldsakasltsseQQLNTNRALVDDTQITSHPDVKA-AAAQLRQAYlddarSTI 213
Cdd:PRK11556 145 RRDLARYQQLAKTNLVSR---------------------QELDAQQALVSETEGTIKADEASvASAQLQLDY-----SRI 198
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15600352 214 VAPVTGYVAKRSVQVGQRVQPGNALMAVV-----PLDQIW 248
Cdd:PRK11556 199 TAPISGRVGLKQVDVGNQISSGDTTGIVVitqthPIDLVF 238
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
15-265 |
5.10e-07 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 51.31 E-value: 5.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 15 RKRWLLILlamIVLATLASVAWEFFYGRWHEDTDDAYINGNVVQ---------------ITPQIVGTVVSIGADDGDLVR 79
Cdd:PRK11578 8 KKRYLIAL---VIVLAGGITLWRILNAPVPTYQTLIVRPGDLQQsvlatgkldalrkvdVGAQVSGQLKTLSVAIGDKVK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 80 KGQELVRFDPSDADIALQRAEANLAHtvrqvrglfsnvdgYRAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHAR 159
Cdd:PRK11578 85 KDQLLGVIDPEQAENQIKEVEATLME--------------LRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 160 DALDSAKASLTSSEQQLNTNRALVDDTQITshpdvkaaaaqlrqayLDDARstIVAPVTGYVAKRSVQVGQRV---QPGN 236
Cdd:PRK11578 151 TELAVKQAQIGTIDAQIKRNQASLDTAKTN----------------LDYTR--IVAPMAGEVTQITTLQGQTViaaQQAP 212
|
250 260
....*....|....*....|....*....
gi 15600352 237 ALMAVVPLDQIWIDANFKETQLKHMRIGQ 265
Cdd:PRK11578 213 NILTLADMSTMLVKAQVSEADVIHLKPGQ 241
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
55-104 |
1.03e-06 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 45.13 E-value: 1.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15600352 55 NVVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQRAEANLA 104
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
56-250 |
1.93e-05 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 46.25 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 56 VVQITPQIVGTVVSIGADDGDLVRKGQELVRFDPSDADIALQRAEANLAHTvrqvrglfsnvdgyraevatrKVALAKAE 135
Cdd:PRK15030 65 IAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKA---------------------QAAANIAQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 136 ADYKRRKNLADDGAISQEELahardaldsakasltsseqqlntNRALVDDTQITShpDVKAAAAQLRQAYLDDARSTIVA 215
Cdd:PRK15030 124 LTVNRYQKLLGTQYISKQEY-----------------------DQALADAQQANA--AVTAAKAAVETARINLAYTKVTS 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 15600352 216 PVTGYVAKRSVQVGQRVQPG--NALMAVVPLDQIWID 250
Cdd:PRK15030 179 PISGRIGKSNVTEGALVQNGqaTALATVQQLDPIYVD 215
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
92-181 |
8.45e-03 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 37.12 E-value: 8.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600352 92 ADIALQRAEANLAHTVRQVR----GLFSNVDGYRAEVATRKVALAKAEADYKRRKNLADDGAISQEELAHARDALDSAKA 167
Cdd:pfam02321 81 AKAQVEAAEAQLEQARQQLRlevaQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEARL 160
|
90
....*....|....
gi 15600352 168 SLTSSEQQLNTNRA 181
Cdd:pfam02321 161 ELLNAEADLELALA 174
|
|
|