|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
43-343 |
3.00e-78 |
|
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: 242.54 E-value: 3.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 43 TVRQSLAEPSIKLVSKLAANRSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAELAEQSASVR------DEAR 116
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAaaqaqlELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 117 K-LRDMRKLVARGAVTTSELEGQEATVAQAQARVDAARYE-------LSLRTLAAPFDGTVSLIDLSEGALVNSGDVLLH 188
Cdd:COG0845 82 AeLERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAAleqaranLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 189 LDELAKLRLDLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRISSDTQNIKARVILPNTGGQLRPGMLMNVDL 268
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522012 269 SLPPQKMTL-IPAQSVEYAGEQRFVYRLEADGRVKRVPVELGDTHGEAVWVLKGLNVGDRIAVEGLVNLRDGAQVR 343
Cdd:COG0845 242 VLGERENALlVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVR 317
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
41-343 |
9.05e-65 |
|
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: 207.94 E-value: 9.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 41 AETVRQSLAEPSIKLVSKLAANRSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQ-------AELAEQSASVRD 113
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQlalqaalAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 114 EARKLRDMRKLVARGAVTTSELEGQEATVAQAQARV-------DAARYELSLRTLAAPFDGTVSLIDLSEGALVNSGDVL 186
Cdd:TIGR01730 83 AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLeaakaslASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 187 LHLDELAKLRLDLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRISSDTQNIKARVILPNTGGQLRPGMLMNV 266
Cdd:TIGR01730 163 ATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFGRV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522012 267 DLSLP-PQKMTLIPAQSVEYAGEQRFVYRLEADGRVKRVPVELGDTHGEAVWVLKGLNVGDRIAVEGLVNLRDGAQVR 343
Cdd:TIGR01730 243 TISLKvRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKVK 320
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
51-263 |
6.65e-27 |
|
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: 105.67 E-value: 6.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 51 PSIKLVSKLAAN--RSVAISPEVTGRIATIAVSS-GQQVKQGQTLIALDA---GKQQAE--LAEQSASVRDEARKLRDMR 122
Cdd:pfam16576 4 RTIRAVGRVAYDerRLAHVHARVEGWIEKLYVNAtGDPVKKGQPLAELYSpelVAAQQEylLALRSGDALSKSELLRAAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 123 -KLVARGaVTTSELEGQEATvAQAQARVdaaryelslrTLAAPFDGTVSLIDLSEGALVNSGDVLLHLDELAKLRLDLAV 201
Cdd:pfam16576 84 qRLRLLG-MPEAQIAELERT-GKVQPTV----------TVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522012 202 PERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRISSDTQNIKARVILPNTGGQLRPGML 263
Cdd:pfam16576 152 PEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMF 213
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
41-342 |
5.24e-25 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 104.49 E-value: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 41 AETVRQSLAEPSIKLVSKLAANrSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAELAE-QSASVRDEA---- 115
Cdd:PRK11556 65 ATATEQAVPRYLTGLGTVTAAN-TVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQaQGQLAKDQAtlan 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 116 --RKLRDMRKLVARGAVTTSELEGQEATVAQA-------QARVDAARYELSLRTLAAPFDGTVSLIDLSEGALVNSGDV- 185
Cdd:PRK11556 144 arRDLARYQQLAKTNLVSRQELDAQQALVSETegtikadEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTt 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 186 -LLHLDELAKLRLDLAVPE----RYLSLLRPGMAVTAtsSAWpDQSFS-----GVLETLDSRISSDTQNIKARVILPNTG 255
Cdd:PRK11556 224 gIVVITQTHPIDLVFTLPEsdiaTVVQAQKAGKPLVV--EAW-DRTNSkklseGTLLSLDNQIDATTGTIKLKARFNNQD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 256 GQLRPGMLMNVDLSLPP-QKMTLIPAQSVEYAGEQRFVYRLEADGRVKRVPVELGDTHGEAVWVLKGLNVGDRIAVEGLV 334
Cdd:PRK11556 301 DALFPNQFVNARMLVDTlQNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGID 380
|
....*...
gi 743522012 335 NLRDGAQV 342
Cdd:PRK11556 381 RLTEGAKV 388
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
43-343 |
3.00e-78 |
|
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: 242.54 E-value: 3.00e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 43 TVRQSLAEPSIKLVSKLAANRSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAELAEQSASVR------DEAR 116
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAaaqaqlELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 117 K-LRDMRKLVARGAVTTSELEGQEATVAQAQARVDAARYE-------LSLRTLAAPFDGTVSLIDLSEGALVNSGDVLLH 188
Cdd:COG0845 82 AeLERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAAleqaranLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 189 LDELAKLRLDLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRISSDTQNIKARVILPNTGGQLRPGMLMNVDL 268
Cdd:COG0845 162 IADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRI 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522012 269 SLPPQKMTL-IPAQSVEYAGEQRFVYRLEADGRVKRVPVELGDTHGEAVWVLKGLNVGDRIAVEGLVNLRDGAQVR 343
Cdd:COG0845 242 VLGERENALlVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVR 317
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
41-343 |
9.05e-65 |
|
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: 207.94 E-value: 9.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 41 AETVRQSLAEPSIKLVSKLAANRSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQ-------AELAEQSASVRD 113
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQlalqaalAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 114 EARKLRDMRKLVARGAVTTSELEGQEATVAQAQARV-------DAARYELSLRTLAAPFDGTVSLIDLSEGALVNSGDVL 186
Cdd:TIGR01730 83 AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLeaakaslASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 187 LHLDELAKLRLDLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRISSDTQNIKARVILPNTGGQLRPGMLMNV 266
Cdd:TIGR01730 163 ATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFGRV 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522012 267 DLSLP-PQKMTLIPAQSVEYAGEQRFVYRLEADGRVKRVPVELGDTHGEAVWVLKGLNVGDRIAVEGLVNLRDGAQVR 343
Cdd:TIGR01730 243 TISLKvRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKVK 320
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
63-268 |
2.88e-29 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 115.15 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 63 RSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAELAEQSASVR------------------------------ 112
Cdd:COG1566 44 RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelgaeaeiaaaeaqlaaaq 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 113 ---DEARK-LRDMRKLVARGAVTTSELE----------------------------------GQEATVAQAQARVDAARY 154
Cdd:COG1566 124 aqlDLAQReLERYQALYKKGAVSQQELDearaaldaaqaqleaaqaqlaqaqaglreeeelaAAQAQVAQAEAALAQAEL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 155 ELSLRTLAAPFDGTVSLIDLSEGALVNSGDVLLHLDELAKLRLDLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVLETL 234
Cdd:COG1566 204 NLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSI 283
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 743522012 235 DSRISS----------DTQNIKARVILPN-TGGQLRPGMLMNVDL 268
Cdd:COG1566 284 SPGAGFtsppknatgnVVQRYPVRIRLDNpDPEPLRPGMSATVEI 328
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
51-263 |
6.65e-27 |
|
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: 105.67 E-value: 6.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 51 PSIKLVSKLAAN--RSVAISPEVTGRIATIAVSS-GQQVKQGQTLIALDA---GKQQAE--LAEQSASVRDEARKLRDMR 122
Cdd:pfam16576 4 RTIRAVGRVAYDerRLAHVHARVEGWIEKLYVNAtGDPVKKGQPLAELYSpelVAAQQEylLALRSGDALSKSELLRAAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 123 -KLVARGaVTTSELEGQEATvAQAQARVdaaryelslrTLAAPFDGTVSLIDLSEGALVNSGDVLLHLDELAKLRLDLAV 201
Cdd:pfam16576 84 qRLRLLG-MPEAQIAELERT-GKVQPTV----------TVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522012 202 PERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRISSDTQNIKARVILPNTGGQLRPGML 263
Cdd:pfam16576 152 PEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMF 213
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
41-342 |
5.24e-25 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 104.49 E-value: 5.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 41 AETVRQSLAEPSIKLVSKLAANrSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAELAE-QSASVRDEA---- 115
Cdd:PRK11556 65 ATATEQAVPRYLTGLGTVTAAN-TVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQaQGQLAKDQAtlan 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 116 --RKLRDMRKLVARGAVTTSELEGQEATVAQA-------QARVDAARYELSLRTLAAPFDGTVSLIDLSEGALVNSGDV- 185
Cdd:PRK11556 144 arRDLARYQQLAKTNLVSRQELDAQQALVSETegtikadEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTt 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 186 -LLHLDELAKLRLDLAVPE----RYLSLLRPGMAVTAtsSAWpDQSFS-----GVLETLDSRISSDTQNIKARVILPNTG 255
Cdd:PRK11556 224 gIVVITQTHPIDLVFTLPEsdiaTVVQAQKAGKPLVV--EAW-DRTNSkklseGTLLSLDNQIDATTGTIKLKARFNNQD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 256 GQLRPGMLMNVDLSLPP-QKMTLIPAQSVEYAGEQRFVYRLEADGRVKRVPVELGDTHGEAVWVLKGLNVGDRIAVEGLV 334
Cdd:PRK11556 301 DALFPNQFVNARMLVDTlQNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGID 380
|
....*...
gi 743522012 335 NLRDGAQV 342
Cdd:PRK11556 381 RLTEGAKV 388
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
24-343 |
7.46e-17 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 80.91 E-value: 7.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 24 RQAEPASKPAPReinIRAETVRQSLAEPSIKLVSKLAANRSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQA- 102
Cdd:PRK15030 28 KQAQQGGQQMPA---VGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQAt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 103 ------ELAEQSASVRDEARKLRDMRKLVARGAVTTSELE-----GQEAT--VAQAQARVDAARYELSLRTLAAPFDGTV 169
Cdd:PRK15030 105 ydsakgDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDqaladAQQANaaVTAAKAAVETARINLAYTKVTSPISGRI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 170 SLIDLSEGALVNSGDV--LLHLDELAKLRLDLAVPERYLSLLRPGMA---------------VTATSSAWPDqsfSGVLE 232
Cdd:PRK15030 185 GKSNVTEGALVQNGQAtaLATVQQLDPIYVDVTQSSNDFLRLKQELAngtlkqengkakvslITSDGIKFPQ---DGTLE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 233 TLDSRISSDTQNIKARVILPNTGGQLRPGMLMNVDLS--LPPQKMtLIPAQSVEYAGE-QRFVYRLEADGRVKRVPVELG 309
Cdd:PRK15030 262 FSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEegLNPNAI-LVPQQGVTRTPRgDATVLVVGADDKVETRPIVAS 340
|
330 340 350
....*....|....*....|....*....|....
gi 743522012 310 DTHGEAVWVLKGLNVGDRIAVEGLVNLRDGAQVR 343
Cdd:PRK15030 341 QAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVK 374
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
160-333 |
7.82e-16 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 77.99 E-value: 7.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 160 TLAAPFDGTVSLIDLSEGALVNSGDVLLHLDELAKLRLDLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRIS 239
Cdd:PRK09783 211 TLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVD 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 240 SDTQNIKARVILPNTGGQLRPGMLMNVDLSLPPQKMTLIPAQSVEYAGEQRFVYRLEADGRV--KRVPVeLGDTHGEAVw 317
Cdd:PRK09783 291 AATRTLQLRLEVDNADEALKPGMNAWLQLNTASEPMLLIPSQALIDTGSEQRVITVDADGRFvpKRVAV-FQESQGVTA- 368
|
170
....*....|....*.
gi 743522012 318 VLKGLNVGDRIAVEGL 333
Cdd:PRK09783 369 IRSGLAEGEKVVSSGL 384
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
30-343 |
1.15e-14 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 74.37 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 30 SKPAPREINIRAETVRQSLAEPSIKLVSKLAAnRSVA-----ISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAEL 104
Cdd:PRK09859 23 DKSAENAAAMTPEVGVVTLSPGSVNVLSELPG-RTVPyevaeIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 105 AEQSASVRDEARKLRDMRKLVARGA--------------VTTSELEGQEATVAQAQARVDAARYELSLRTLAAPFDGTVS 170
Cdd:PRK09859 102 NSAKGSLAKALSTASNARITFNRQAsllktnyvsrqdydTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 171 LIDLSEGALV--NSGDVLLHLDELAKLRLDLAVPERYLSLLRPGMA---VTATSSAWPDQ---------SFSGVLETLDS 236
Cdd:PRK09859 182 KSSVTVGALVtaNQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVAsgqIKQVQGSTPVQlnlengkrySQTGTLKFSDP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 237 RISSDTQNIKARVILPNTGGQLRPGMLMNVDLSLPP-QKMTLIPAQSVEYAGEQRFVYR-LEADGRVKRVPVELGDTHGE 314
Cdd:PRK09859 262 TVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSrQNVLLVPQEGVTHNAQGKATALiLDKDDVVQLREIEASKAIGD 341
|
330 340
....*....|....*....|....*....
gi 743522012 315 AVWVLKGLNVGDRIAVEGLVNLRDGAQVR 343
Cdd:PRK09859 342 QWVVTSGLQAGDRVIVSGLQRIRPGIKAR 370
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
44-330 |
1.70e-14 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 73.66 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 44 VRQSLAEPSIKLVSKLAANRSVAISPEVTGRIATIAVSSGQQVKQGQ-------------------TLIALDAGKQQAE- 103
Cdd:PRK11578 41 VRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQllgvidpeqaenqikeveaTLMELRAQRQQAEa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 104 --------LAEQSASVRDEARKLRDMRKLVARGAVTTSELEGQEATVAQAQARVDAARYELSLRTLAAPFDGTVSLIDLS 175
Cdd:PRK11578 121 elklarvtLSRQQRLAKTQAVSQQDLDTAATELAVKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 176 EGALV---NSGDVLLHLDELAKLRLDLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRISSDTQNI--KARVI 250
Cdd:PRK11578 201 QGQTViaaQQAPNILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIfyYARFE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 251 LPNTGGQLRPGMLMNVDLSLPPQKMTL-IPAQSV-EYAGEQRFVYRLEADGRVKRVPVELGDTHGEAVWVLKGLNVGDRI 328
Cdd:PRK11578 281 VPNPNGLLRLDMTAQVHIQLTDVKNVLtIPLSALgDPVGDNRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEV 360
|
..
gi 743522012 329 AV 330
Cdd:PRK11578 361 II 362
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
28-343 |
4.22e-13 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 69.44 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 28 PASKPAPREINIRaeTVRQSLAEPSIKLVSKLAANRSVAISPEVTGRIATIAVSSGQQVKQGQTLIALD-----AGKQQA 102
Cdd:PRK09578 29 DAAAAAPREATVV--TVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDpaplkAARDAA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 103 E--LAEQSASVRDEARKLRDMRKLVARGAVttSELEGQEAT---------VAQAQARVDAARYELSLRTLAAPFDGTVSL 171
Cdd:PRK09578 107 AgaLAKAEAAHLAALDKRRRYDDLVRDRAV--SERDYTEAVaderqakaaVASAKAELARAQLQLDYATVTAPIDGRARR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 172 IDLSEGALV--NSGDVLLHLDELAKLRLDLAVPERYLSLLRPGM-------------AVT---ATSSAWPdqsFSGVLET 233
Cdd:PRK09578 185 ALVTEGALVgqDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVksgratgiaqqdvAVTlvrADGSEYP---LKGKLLF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 234 LDSRISSDTQNIKARVILPNTGGQLRPGMLMNVDLSLP-PQKMTLIPAQSVEYAGEQRFVYRLEADGRVKRVPVELGDTH 312
Cdd:PRK09578 262 SDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAvNPRAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMS 341
|
330 340 350
....*....|....*....|....*....|.
gi 743522012 313 GEAVWVLKGLNVGDRIAVEGLVNLRDGAQVR 343
Cdd:PRK09578 342 GRDWIVTRGLAGGERVIVDNAAQFAPGTAVK 372
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
160-261 |
1.32e-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: 63.15 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 160 TLAAPFDGTVSLIDLSEGALVNSGDVLLHLDELAKLRLDLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVLETLDSRIS 239
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
90 100
....*....|....*....|....
gi 743522012 240 SDTQNIKARVILPNTGGQ--LRPG 261
Cdd:pfam13437 81 PDTGVIPVRVSIENPKTPipLLPG 104
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
65-218 |
4.67e-10 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 59.75 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 65 VAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAELAEQSASV-----------RDEARKLRDMRKLVARGAVTTS 133
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVayyqvlaqekrREAGRRNRLGVQAMSREEIDQA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 134 --ELEGQEATVAQAQARVDAARYELSLRTLAAPFDGTVSLIDLSEGALVNSGDVLLHLDELAKLRLDLAVPERYLSLLRP 211
Cdd:PRK10559 128 nnVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRP 207
|
....*..
gi 743522012 212 GMAVTAT 218
Cdd:PRK10559 208 GYRAEIT 214
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
63-272 |
1.47e-09 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 58.43 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 63 RSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQ---------------------------------AELAEQSA 109
Cdd:PRK03598 42 RTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYEnalmqakanvsvaqaqldlmlagyrdeeiaqarAAVKQAQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 110 SVRDEARKLRDMRKLVARGAVTTSELEGQEATVAQAQARVDAARYELSL------------------------------- 158
Cdd:PRK03598 122 AYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLSQyregnrpqdiaqakaslaqaqaalaqaelnl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 159 --RTLAAPFDGTVSLIDLSEGALVNSGDVL--LHLDELAKLRldLAVPERYLSLLRPGMAVTATSSAWPDQSFSGVL--- 231
Cdd:PRK03598 202 qdTELIAPSDGTILTRAVEPGTMLNAGSTVftLSLTRPVWVR--AYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIgfv 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 743522012 232 -----------ETLDSRissdTQNI-KARVILPNTGGQLRPGMLMNVDLSLPP 272
Cdd:PRK03598 280 sptaeftpktvETPDLR----TDLVyRLRIVVTDADDALRQGMPVTVRFADEA 328
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
63-183 |
1.82e-07 |
|
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: 52.04 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 63 RSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAEL----AEQSASVRDEAR---KLRDMRKLVARGAVT---- 131
Cdd:pfam00529 19 NAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALdsaeAQLAKAQAQVARlqaELDRLQALESELAISrqdy 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 743522012 132 ---TSELEGQEATVAQAQARVDAARYELSLRTLAAPFDGTVSLIDLSEGALVNSG 183
Cdd:pfam00529 99 dgaTAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQA 153
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
63-112 |
3.71e-07 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 46.28 E-value: 3.71e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 743522012 63 RSVAISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAELAEQSASVR 112
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
65-241 |
8.91e-06 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 46.94 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 65 VAISPEVTGRIATIAVSSGQQVKQGQTLIALD-------AGKQQAEL---------------AEQS-ASVRDE------- 114
Cdd:PRK10476 49 VHVASEVGGRIVELAVTENQAVKKGDLLFRIDprpyeltVAQAQADLaladaqimttqrsvdAERSnAASANEqverara 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 115 -----ARKLRDMRKLVARGAVTT-------------------------------SELEGQEATVAQAQARVDAARYELSL 158
Cdd:PRK10476 129 naklaTRTLERLEPLLAKGYVSAqqvdqartaqrdaevslnqallqaqaaaaavGGVDALVAQRAAREAALAIAELHLED 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 159 RTLAAPFDGTVSLIDLSEGALVNSGDV---LLHLDE---LAKLRldlavpERYLSLLRPGMAVTATSSAWPDQSFSGVLE 232
Cdd:PRK10476 209 TTVRAPFDGRVVGLKVSVGEFAAPMQPiftLIDTDHwyaIANFR------ETDLKNIRVGDCATVYSMIDRGRPFEGKVD 282
|
....*....
gi 743522012 233 TLDSRISSD 241
Cdd:PRK10476 283 SIGWGVLPD 291
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
34-187 |
5.85e-05 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 45.07 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 34 PREINIRAETVrqslaepSIKLVSKLAANRSVA--ISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKqqaelaeqsasv 111
Cdd:COG1038 1051 PREVRVRDRSV-------KVTVASREKADPGNPghIGAPMPGTVVKVLVKEGDEVKKGDPLLTIEAMK------------ 1111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522012 112 rdearklrdMrklvargavttselegqEATVaqaqarvdaaryelslrtlAAPFDGTVSLIDLSEGALVNSGDVLL 187
Cdd:COG1038 1112 ---------M-----------------ETTI-------------------TAPRDGTVKEVLVKEGDQVEAGDLLI 1142
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
34-191 |
9.63e-04 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 41.28 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 34 PREINIRAETVrqslaEPSIKLVSKlaANRSVA--ISPEVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAelaeqsasv 111
Cdd:PRK12999 1051 PREVQVRDRSV-----KSTVAAREK--ADPGNPghVGAPMPGSVVTVLVKEGDEVKAGDPLAVIEAMKMET--------- 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522012 112 rdearklrdmrklvargavttselegqeatvaqaqarvdaaryelslrTLAAPFDGTVSLIDLSEGALVNSGDVLLHLDE 191
Cdd:PRK12999 1115 ------------------------------------------------TITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PRK05641 |
PRK05641 |
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated |
26-104 |
7.84e-03 |
|
putative acetyl-CoA carboxylase biotin carboxyl carrier protein subunit; Validated
Pssm-ID: 235540 [Multi-domain] Cd Length: 153 Bit Score: 36.38 E-value: 7.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743522012 26 AEPASKPAPREINIRAETVRQSLAEPSIklvsklAANRSVAISPeVTGRIATIAVSSGQQVKQGQTLIALDAGKQQAEL 104
Cdd:PRK05641 53 PTPAPAPAPAVPSAPTPVAPAAPAPAPA------SAGENVVTAP-MPGKILRILVREGQQVKVGQGLLILEAMKMENEI 124
|
|
| |
