|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
1-343 |
0e+00 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 528.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 1 MESTPKKAPRSKFPALLVVALALVALVFVIWRVDSAPSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRID 80
Cdd:PRK10476 1 MESTPKKSPRKKLPALAIVALAIVALVFVIWRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 81 PRPFEANLAKAEASLAALDKQIMLTQRSVDAQQFGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTA 160
Cdd:PRK10476 81 PRPYELTVAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 161 QRAAEADLNAVLLQAQSAASAVSGVDALVAQRAAVEADIALTKLHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLI 240
Cdd:PRK10476 161 QRDAEVSLNQALLQAQAAAAAVGGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 241 DTRHWYVIANFRETDLKNIRSGTPATIRLMSDSGKTFEGKVDSIGYGVLPDDGGLVLGGLPKVSRSINWVRVAQRFPVKI 320
Cdd:PRK10476 241 DTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIGWGVLPDDGGNVPRGLPYVPRSINWVRVAQRFPVRI 320
|
330 340
....*....|....*....|...
gi 446368493 321 MVDKPDPEMFRIGASAVANLEPQ 343
Cdd:PRK10476 321 MLDKPDPELFRIGASAVVELRPG 343
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
10-340 |
9.41e-145 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 412.27 E-value: 9.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 10 RSKFPALLVVALALVALVFVIWR---VDSAPSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEA 86
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWflvLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 87 NLAKAEASLAALDKQIMLTQRSVDAQQFGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEA 166
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAREKLLQAELDLRRRVPLFKKGLISREELDHARKALLSAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 167 DLNAVLLQAQSAASAVSGVDALVAQRAAVEADIALTK--LHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRH 244
Cdd:TIGR00998 161 ALNAAIQEQLNANQALVRGTPLKKQPAVQEAKERLKTawLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 245 WYVIANFRETDLKNIRSGTPATIRL-MSDSGKTFEGKVDSIGYGvlpddGGLVLGGLPKVSRSINWVRVAQRFPVKIMVD 323
Cdd:TIGR00998 241 MYVEANFKETQLKNVRIGQPVTIRSdLYGSDVVFEGKVTGISMG-----TGSAFSLLPAQNATGNWIKVVQRLPVRIKLD 315
|
330
....*....|....*....
gi 446368493 324 KP--DPEMFRIGASAVANL 340
Cdd:TIGR00998 316 PKelDEHPLRIGLSAEVEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
32-343 |
3.30e-76 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 237.25 E-value: 3.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 32 RVDSAPSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAALDKQIMLTQRSVDA 111
Cdd:COG1566 29 NGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 112 QQfGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLNAV---LLQAQSAASAVSGVDAL 188
Cdd:COG1566 109 EA-EIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAqaqLAQAQAGLREEEELAAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 189 VAQRAAVEADIALTKLHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIR 268
Cdd:COG1566 188 QAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVR 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446368493 269 LMSDSGKTFEGKVDSIGYGVLPDDGGLVLGGlpkvsrsinwvRVAQRFPVKIMVDKPDPEMFRIGASAVANLEPQ 343
Cdd:COG1566 268 VDAYPDRVFEGKVTSISPGAGFTSPPKNATG-----------NVVQRYPVRIRLDNPDPEPLRPGMSATVEIDTE 331
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
35-291 |
1.35e-55 |
|
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: 184.16 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 35 SAPSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAALDKQIMLTQRSVDAQQ- 113
Cdd:pfam00529 7 GVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 114 ----------------FGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLNAVLLQ--- 174
Cdd:pfam00529 87 leselaisrqdydgatAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQldq 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 175 ---------AQSAASAVSGVDALVAQRAAVEADIALTKLHLEMATVRAPFDGRVISLKTSV-GQFASAMRPIFTLIDTRH 244
Cdd:pfam00529 167 iyvqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDN 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446368493 245 WYVIANFRETDLKNIRSGTPATIRLMSDSGKT---FEGKVDSIGYGVLPD 291
Cdd:pfam00529 247 LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgrFTGVVVGISPDTGPV 296
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
49-79 |
7.97e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 34.70 E-value: 7.97e-03
10 20 30
....*....|....*....|....*....|.
gi 446368493 49 IDVVPEVSGRIVELAVTDNQAVKQGDLLFRI 79
Cdd:cd06850 37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
1-343 |
0e+00 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 528.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 1 MESTPKKAPRSKFPALLVVALALVALVFVIWRVDSAPSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRID 80
Cdd:PRK10476 1 MESTPKKSPRKKLPALAIVALAIVALVFVIWRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 81 PRPFEANLAKAEASLAALDKQIMLTQRSVDAQQFGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTA 160
Cdd:PRK10476 81 PRPYELTVAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 161 QRAAEADLNAVLLQAQSAASAVSGVDALVAQRAAVEADIALTKLHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLI 240
Cdd:PRK10476 161 QRDAEVSLNQALLQAQAAAAAVGGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 241 DTRHWYVIANFRETDLKNIRSGTPATIRLMSDSGKTFEGKVDSIGYGVLPDDGGLVLGGLPKVSRSINWVRVAQRFPVKI 320
Cdd:PRK10476 241 DTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIGWGVLPDDGGNVPRGLPYVPRSINWVRVAQRFPVRI 320
|
330 340
....*....|....*....|...
gi 446368493 321 MVDKPDPEMFRIGASAVANLEPQ 343
Cdd:PRK10476 321 MLDKPDPELFRIGASAVVELRPG 343
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
10-340 |
9.41e-145 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 412.27 E-value: 9.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 10 RSKFPALLVVALALVALVFVIWR---VDSAPSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEA 86
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWflvLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 87 NLAKAEASLAALDKQIMLTQRSVDAQQFGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEA 166
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAREKLLQAELDLRRRVPLFKKGLISREELDHARKALLSAKA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 167 DLNAVLLQAQSAASAVSGVDALVAQRAAVEADIALTK--LHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRH 244
Cdd:TIGR00998 161 ALNAAIQEQLNANQALVRGTPLKKQPAVQEAKERLKTawLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAEQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 245 WYVIANFRETDLKNIRSGTPATIRL-MSDSGKTFEGKVDSIGYGvlpddGGLVLGGLPKVSRSINWVRVAQRFPVKIMVD 323
Cdd:TIGR00998 241 MYVEANFKETQLKNVRIGQPVTIRSdLYGSDVVFEGKVTGISMG-----TGSAFSLLPAQNATGNWIKVVQRLPVRIKLD 315
|
330
....*....|....*....
gi 446368493 324 KP--DPEMFRIGASAVANL 340
Cdd:TIGR00998 316 PKelDEHPLRIGLSAEVEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
32-343 |
3.30e-76 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 237.25 E-value: 3.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 32 RVDSAPSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAALDKQIMLTQRSVDA 111
Cdd:COG1566 29 NGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARLEAELGA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 112 QQfGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLNAV---LLQAQSAASAVSGVDAL 188
Cdd:COG1566 109 EA-EIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAqaqLAQAQAGLREEEELAAA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 189 VAQRAAVEADIALTKLHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIR 268
Cdd:COG1566 188 QAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVR 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446368493 269 LMSDSGKTFEGKVDSIGYGVLPDDGGLVLGGlpkvsrsinwvRVAQRFPVKIMVDKPDPEMFRIGASAVANLEPQ 343
Cdd:COG1566 268 VDAYPDRVFEGKVTSISPGAGFTSPPKNATG-----------NVVQRYPVRIRLDNPDPEPLRPGMSATVEIDTE 331
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
35-291 |
1.35e-55 |
|
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: 184.16 E-value: 1.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 35 SAPSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAALDKQIMLTQRSVDAQQ- 113
Cdd:pfam00529 7 GVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQa 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 114 ----------------FGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLNAVLLQ--- 174
Cdd:pfam00529 87 leselaisrqdydgatAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQldq 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 175 ---------AQSAASAVSGVDALVAQRAAVEADIALTKLHLEMATVRAPFDGRVISLKTSV-GQFASAMRPIFTLIDTRH 244
Cdd:pfam00529 167 iyvqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDN 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446368493 245 WYVIANFRETDLKNIRSGTPATIRLMSDSGKT---FEGKVDSIGYGVLPD 291
Cdd:pfam00529 247 LLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgrFTGVVVGISPDTGPV 296
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
44-341 |
1.23e-45 |
|
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: 158.18 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 44 ASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAAldkqimltqrsvdaqqfgadsinatv 123
Cdd:COG0845 19 EARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAA-------------------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 124 ekARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLnavllqaqsaasavsgvdalvaqrAAVEADIALTK 203
Cdd:COG0845 73 --AQAQLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAAL------------------------AAAQAALEQAR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 204 LHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIRLMSDSGKTFEGKVDS 283
Cdd:COG0845 127 ANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTF 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446368493 284 IGYGVLPDdgglvlgglpkvsrsinwvrvAQRFPVKIMVDKPDPEmFRIGASAVANLE 341
Cdd:COG0845 207 IDPAVDPA---------------------TRTVRVRAELPNPDGL-LRPGMFVRVRIV 242
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
39-341 |
3.39e-32 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 124.04 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 39 TNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAALDKQIMltQRSVDAQQFgads 118
Cdd:PRK15136 52 TDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTH--QLMINSKQY---- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 119 iNATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLNAVLLQAQSAASAVsgVDALVAQRAAVE-- 196
Cdd:PRK15136 126 -QANIELQKTALAQAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAIQQYNANQAMI--LNTPLEDQPAVQqa 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 197 -ADIALTKLHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIrlMSD--- 272
Cdd:PRK15136 203 aTEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATI--TSDiyg 280
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446368493 273 SGKTFEGKVDSIGYGVlpddgGLVLGGLPKVSRSINWVRVAQRFPVKIMVDKPDPEM--FRIGASAVANLE 341
Cdd:PRK15136 281 DDVVYTGKVVGLDMGT-----GSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQhpLRIGLSTLVTVD 346
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
36-336 |
1.09e-31 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 121.00 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 36 APSTNDAYASADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAALdkQIMLTqrsvdaqqfg 115
Cdd:PRK10559 35 SPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYY--QVLAQ---------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 116 adsinatvEKARAAAkqatdtlRRTEplLKEGFVSAEDVDRARTAQRAAEADLnavllqaqsaasavsgvdalvaqrAAV 195
Cdd:PRK10559 103 --------EKRREAG-------RRNR--LGVQAMSREEIDQANNVLQTVLHQL------------------------AKA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 196 EADIALTKLHLEMATVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIRLMSdSGK 275
Cdd:PRK10559 142 QATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLG-SNK 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446368493 276 TFEGKVDSIGYGVLPDDGGLVLGGLPKVSRSINWVRVAQRFPVKIMVDKPDPEMFRIGASA 336
Cdd:PRK10559 221 VLKGTVDSVAAGVTNSSSTRDSKGMATIDSNLEWVRLAQRVPVRIRLDNQQGNLYPAGTTA 281
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
47-284 |
2.38e-29 |
|
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: 114.72 E-value: 2.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 47 DTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAAldkqimltqrsvdaqqfgadsinatvekA 126
Cdd:TIGR01730 25 DEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAA----------------------------A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 127 RAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLnavllqaqsaasavsgvdalvaqrAAVEADIALTKLHL 206
Cdd:TIGR01730 77 EAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADL------------------------EAAKASLASAQLNL 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446368493 207 EMATVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIRLMSDSGKTFEGKVDSI 284
Cdd:TIGR01730 133 RYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFI 210
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
55-281 |
7.09e-25 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 102.73 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 55 VSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAALDKQIMLTQRSVDAQQFGadSINATVEKARAAAKQAT 134
Cdd:PRK03598 50 VGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDLMLAGYRDEEIA--QARAAVKQAQAAYDYAQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 135 DTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLNAV---LLQAQsAASAVSGVDALVAQRAAVEADIALTKLHLEMATV 211
Cdd:PRK03598 128 NFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAqdkLSQYR-EGNRPQDIAQAKASLAQAQAALAQAELNLQDTEL 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 212 RAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIRLMSDSGKTFEGKV 281
Cdd:PRK03598 207 IAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQI 276
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
58-285 |
9.12e-15 |
|
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: 74.09 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 58 RIVELAVTDNQAVKQGDLLFRIDPRP-------------FEANLAKAEASLAALDKQIMLTQRSVDAQQFGADS--INAT 122
Cdd:TIGR02971 26 RIKKLLVAEGDRVQAGQVLAELDSRPertaeldvartqlDEAKARLAQVRAGAKKGEIAAQRAARAAAKLFKDVaaQQAT 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 123 VEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLNAVLLQAQ-----------SAASAVSGVDALVAQ 191
Cdd:TIGR02971 106 LNRLEAELETAQREVDRYRSLFRDGAVSASDLDSKALKLRTAEEELEEALASRSeqidgaraalaSLAEEVRETDVDLAQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 192 ---RAAVEAdIALTKLHLEMATVRAPFDGRVISLKTSVGQfASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIR 268
Cdd:TIGR02971 186 aevKSALEA-VQQAEALLELTYVKAPIDGRVLKIHAREGE-VIGSEGILEMGDTSQMYAVAEVYETDINRVRVGQRATIT 263
|
250
....*....|....*..
gi 446368493 269 LMSDSGkTFEGKVDSIG 285
Cdd:TIGR02971 264 STALSG-PLRGTVRRIG 279
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
28-284 |
1.41e-14 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 73.66 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 28 FVIWRVDSAPSTND---------------AYASADT---IDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLA 89
Cdd:PRK11578 23 ITLWRILNAPVPTYqtlivrpgdlqqsvlATGKLDAlrkVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 90 KAEASLAALdkqimltqrsvdaqqfgadsiNATVEKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTaqraaeadlN 169
Cdd:PRK11578 103 EVEATLMEL---------------------RAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAAT---------E 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 170 AVLLQAQsaasavsgVDALVAQRAAVEADIALTKLHLEMATVRAPFDGRVISLKTSVGQ--FASAMRP-IFTLIDTRHWY 246
Cdd:PRK11578 153 LAVKQAQ--------IGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQtvIAAQQAPnILTLADMSTML 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 446368493 247 VIANFRETDLKNIRSGTPATIRLMSDSGKTFEGKVDSI 284
Cdd:PRK11578 225 VKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDI 262
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
45-232 |
1.94e-13 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 70.59 E-value: 1.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 45 SADTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAaldkqimltqrsvdaqqfgadsinatve 124
Cdd:PRK11556 84 AANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLA---------------------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 125 KARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLNAvllqaqsaasavsgvDalvaqraavEADIALTKL 204
Cdd:PRK11556 136 KDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKA---------------D---------EASVASAQL 191
|
170 180
....*....|....*....|....*...
gi 446368493 205 HLEMATVRAPFDGRVISLKTSVGQFASA 232
Cdd:PRK11556 192 QLDYSRITAPISGRVGLKQVDVGNQISS 219
|
|
| 8a0102 |
TIGR00999 |
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, ... |
68-288 |
1.60e-12 |
|
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, Other]
Pssm-ID: 273386 [Multi-domain] Cd Length: 265 Bit Score: 66.69 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 68 QAVKQGDLLFRIDPrpfeANLAKAEASLAALDKQimltqrsvdaqqfgadsinatVEKARAaakqatdTLRRTEPLLKEG 147
Cdd:TIGR00999 2 DPVKKGQVLAVVDS----PELAKMAAELKVAQKR---------------------VELARK-------TYEREKKLFEQG 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 148 FVSAEDVDRARTAQRAAEADLNAVLLQAQSAASAVSGvdalvaqraaveadialtklhlEMATVRAPFDGRVISLKTSVG 227
Cdd:TIGR00999 50 VIPRQEFESAEYALEEAQAEVQAAKSELRSAREAKDG----------------------SYVEVRSPFDGYITQKSVTLG 107
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446368493 228 QFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIrlMSDSGKTFEGKVDSIGYGV 288
Cdd:TIGR00999 108 DYVAPQAELFRVADLGAVWVEAEVPAKDVSRIRKGSKATV--LLENGRPLPARVDYVGPEV 166
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
210-293 |
7.61e-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: 61.22 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 210 TVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIRLMSDSGKTFEGKVDSIGYGVL 289
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
....
gi 446368493 290 PDDG 293
Cdd:pfam13437 81 PDTG 84
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
47-96 |
3.88e-11 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 57.45 E-value: 3.88e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446368493 47 DTIDVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLA 96
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
50-226 |
4.75e-11 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 63.20 E-value: 4.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 50 DVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAaldkqimltqrsvdaqqfgadsinatveKARAA 129
Cdd:PRK09859 63 EIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLA----------------------------KALST 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 130 AKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLnavllqaqsaasavsgvdalvaqrAAVEADIALTKLHLEMA 209
Cdd:PRK09859 115 ASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANV------------------------TVAKAAVEQATINLQYA 170
|
170
....*....|....*..
gi 446368493 210 TVRAPFDGrvISLKTSV 226
Cdd:PRK09859 171 NVTSPITG--VSGKSSV 185
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
210-284 |
9.13e-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: 60.60 E-value: 9.13e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446368493 210 TVRAPFDGRVISLKTSVGQFASAMRPIFTLIDTRHWYVIANFRETDLKNIRSGTPATIRLMSDSGKTFEGKVDSI 284
Cdd:pfam16576 110 TVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDYI 184
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
37-218 |
2.50e-09 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 57.88 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 37 PSTNDAYASADtidVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAaldkqimltqrsvdaqqfga 116
Cdd:PRK09578 55 PGRLDAYRQAE---VRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALA-------------------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 117 dsinatveKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLnavllqaqsaasavsgvdalvaqrAAVE 196
Cdd:PRK09578 112 --------KAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAV------------------------ASAK 159
|
170 180
....*....|....*....|..
gi 446368493 197 ADIALTKLHLEMATVRAPFDGR 218
Cdd:PRK09578 160 AELARAQLQLDYATVTAPIDGR 181
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
37-219 |
8.19e-07 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 50.48 E-value: 8.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 37 PSTNDAYASADtidVVPEVSGRIVELAVTDNQAVKQGDLLFRIDPRPFEANLAKAEASLAaldkqimltqrsvdaqqfga 116
Cdd:PRK15030 57 PGRTSAYRIAE---VRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLA-------------------- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 117 dsinatveKARAAAKQATDTLRRTEPLLKEGFVSAEDVDRArtaqraaeadlnavLLQAQSAASAVsgvdalVAQRAAVE 196
Cdd:PRK15030 114 --------KAQAAANIAQLTVNRYQKLLGTQYISKQEYDQA--------------LADAQQANAAV------TAAKAAVE 165
|
170 180
....*....|....*....|...
gi 446368493 197 AdialTKLHLEMATVRAPFDGRV 219
Cdd:PRK15030 166 T----ARINLAYTKVTSPISGRI 184
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
76-178 |
5.78e-04 |
|
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: 40.20 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 76 LFRIDPRPFEANLAKAEASLAALDKQIMLTQRSVDAQQ--FGADSINATVEKARAAAKQATDTLRRTEPLLKEGFVSAED 153
Cdd:pfam02321 68 LFDGGKRRARVKAAKAQVEAAEAQLEQARQQLRLEVAQayLQLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLD 147
|
90 100
....*....|....*....|....*
gi 446368493 154 VDRARTAQRAAEADLNAVLLQAQSA 178
Cdd:pfam02321 148 VLQAEVELLEARLELLNAEADLELA 172
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
90-201 |
7.65e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 37.93 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446368493 90 KAEASLAALDKQIMLTQRSVDAQQFGADSINATVEKARAAAKqATDTLRRTEPLLKEGFVSAEDVDRARTAQRAAEADLN 169
Cdd:PRK12472 181 KAEALAAAPARAETLAREAEDAARAADEAKTAAAAAAREAAP-LKASLRKLERAKARADAELKRADKALAAAKTDEAKAR 259
|
90 100 110
....*....|....*....|....*....|..
gi 446368493 170 AVLLQAQSAASAVSGVDALVAQRAAVEADIAL 201
Cdd:PRK12472 260 AEERQQKAAQQAAEAATQLDTAKADAEAKRAA 291
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
49-79 |
7.97e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 34.70 E-value: 7.97e-03
10 20 30
....*....|....*....|....*....|.
gi 446368493 49 IDVVPEVSGRIVELAVTDNQAVKQGDLLFRI 79
Cdd:cd06850 37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
