|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
167-474 |
3.70e-76 |
|
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: 241.77 E-value: 3.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 167 SLAQVVSLPGEIRFneDRTAHIVPRLPGIVDSVPANLGQAVKQGELLAVISSP----QLSDQRSEFAAAQRRLSLAQSTY 242
Cdd:COG0845 7 DVPETVEATGTVEA--RREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPdlqaALAQAQAQLAAAQAQLELAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 243 KREQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAALGGNPSlqggnRYELRAPFAGVLVEKHLTQGEPVDGTANV 322
Cdd:COG0845 85 ERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLA-----YTTIRAPFDGVVGERNVEPGQLVSAGTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 323 FTLSDLSSVWATFNVPAQLLGQVRVGSKVKVLAQAL-DSEVEGTVSYIGDLLGEQTRAATARVTLSNPESTWRPGLFVSV 401
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGpGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489200307 402 QVAEATRKEVLTVADGAVQNVDGEDVVFVRVADG-FVVQPVKLGISDGQRVEVLEGLRAGSQVAASGSFILKSE 474
Cdd:COG0845 240 RIVLGERENALLVPASAVVRDGGGAYVFVVDADGkVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
167-399 |
2.40e-40 |
|
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: 144.19 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 167 SLAQVVSLPGEIRFNEDRTAHIVPRLPGIVDSVPAN-LGQAVKQGELLAVISSPQLsdqrsefaaaqrrlslaqstykre 245
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPEL------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 246 qqlwkegISAEQEFLLARQGLQEAEIA--LNNARAKIAALGGNPSL--------QGGNRYELRAPFAGVLVEKHLTQGEP 315
Cdd:pfam16576 57 -------VAAQQEYLLALRSGDALSKSelLRAARQRLRLLGMPEAQiaelertgKVQPTVTVYAPISGVVTELNVREGMY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 316 VDGTANVFTLSDLSSVWATFNVPAQLLGQVRVGSKVKVLAQAL-DSEVEGTVSYIGDLLGEQTRAATARVTLSNPESTWR 394
Cdd:pfam16576 130 VQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALpGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLK 209
|
....*
gi 489200307 395 PGLFV 399
Cdd:pfam16576 210 PGMFA 214
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
158-472 |
9.96e-37 |
|
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: 137.83 E-value: 9.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 158 ITLDTARTISLAQVVSLPGEIRFNEDrtAHIVPRLPGIVDSVPANLGQAVKQGELLAVISSP----QLSDQRSEFAAAQR 233
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDE--ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDdyqlALQAALAQLAAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 234 RLSLAQSTYKREQQLWKEGI-------SAEQEFLLARQGLQEAEIALNNARAKIAalggnpslqggnRYELRAPFAGVLV 306
Cdd:TIGR01730 79 QLELAQRSFERAERLVKRNAvsqadldDAKAAVEAAQADLEAAKASLASAQLNLR------------YTEIRAPFDGTIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 307 EKHLTQGEPVDGTANVFTLSDLSSVWATFNVPAQLLGQVRVGSKVKVLAQALDS-EVEGTVSYIGDLLGEQTRAATARVT 385
Cdd:TIGR01730 147 RRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGeEFKGKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 386 LSNPESTWRPGLFVSVQVAEATRKEVLTVADGAVQNVDGEDVVFVRVADGFVV-QPVKLGISDGQRVEVLEGLRAGSQVA 464
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSkRPVEVGLRNGGYVEIESGLKAGDQIV 306
|
....*...
gi 489200307 465 ASGSFILK 472
Cdd:TIGR01730 307 TAGVVKLR 314
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
150-467 |
1.78e-13 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 71.67 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 150 AEQIEAA----GITLDTARTISLAQvvSLPGeiRFNEDRTAHIVPRLPGIVDSVPANLGQAVKQGELLAVIS----SPQL 221
Cdd:PRK09859 26 AENAAAMtpevGVVTLSPGSVNVLS--ELPG--RTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDpaplQAEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 222 SDQRSEFAAAQRRLSLAQSTYKREQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAALGGNpsLQGGNryeLRAPF 301
Cdd:PRK09859 102 NSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATIN--LQYAN---VTSPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 302 AGVLVEKHLTQGEPVdgTAN----VFTLSDLSSVWATFNVPAQ----LLGQVRVGSKVKVLAQ---ALDSE------VEG 364
Cdd:PRK09859 177 TGVSGKSSVTVGALV--TANqadsLVTVQRLDPIYVDLTQSVQdflrMKEEVASGQIKQVQGStpvQLNLEngkrysQTG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 365 TVSYIGDLLGEQTRAATARVTLSNPESTWRPGLFVSVQVAEATRKEVLTV-ADGAVQNVDGEDVVFVRVADGFVVQ-PVK 442
Cdd:PRK09859 255 TLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVpQEGVTHNAQGKATALILDKDDVVQLrEIE 334
|
330 340
....*....|....*....|....*
gi 489200307 443 LGISDGQRVEVLEGLRAGSQVAASG 467
Cdd:PRK09859 335 ASKAIGDQWVVTSGLQAGDRVIVSG 359
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
167-474 |
3.70e-76 |
|
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: 241.77 E-value: 3.70e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 167 SLAQVVSLPGEIRFneDRTAHIVPRLPGIVDSVPANLGQAVKQGELLAVISSP----QLSDQRSEFAAAQRRLSLAQSTY 242
Cdd:COG0845 7 DVPETVEATGTVEA--RREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPdlqaALAQAQAQLAAAQAQLELAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 243 KREQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAALGGNPSlqggnRYELRAPFAGVLVEKHLTQGEPVDGTANV 322
Cdd:COG0845 85 ERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLA-----YTTIRAPFDGVVGERNVEPGQLVSAGTPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 323 FTLSDLSSVWATFNVPAQLLGQVRVGSKVKVLAQAL-DSEVEGTVSYIGDLLGEQTRAATARVTLSNPESTWRPGLFVSV 401
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGpGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489200307 402 QVAEATRKEVLTVADGAVQNVDGEDVVFVRVADG-FVVQPVKLGISDGQRVEVLEGLRAGSQVAASGSFILKSE 474
Cdd:COG0845 240 RIVLGERENALLVPASAVVRDGGGAYVFVVDADGkVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
167-399 |
2.40e-40 |
|
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: 144.19 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 167 SLAQVVSLPGEIRFNEDRTAHIVPRLPGIVDSVPAN-LGQAVKQGELLAVISSPQLsdqrsefaaaqrrlslaqstykre 245
Cdd:pfam16576 1 PLSRTIRAVGRVAYDERRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPEL------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 246 qqlwkegISAEQEFLLARQGLQEAEIA--LNNARAKIAALGGNPSL--------QGGNRYELRAPFAGVLVEKHLTQGEP 315
Cdd:pfam16576 57 -------VAAQQEYLLALRSGDALSKSelLRAARQRLRLLGMPEAQiaelertgKVQPTVTVYAPISGVVTELNVREGMY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 316 VDGTANVFTLSDLSSVWATFNVPAQLLGQVRVGSKVKVLAQAL-DSEVEGTVSYIGDLLGEQTRAATARVTLSNPESTWR 394
Cdd:pfam16576 130 VQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALpGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLK 209
|
....*
gi 489200307 395 PGLFV 399
Cdd:pfam16576 210 PGMFA 214
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
158-472 |
9.96e-37 |
|
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: 137.83 E-value: 9.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 158 ITLDTARTISLAQVVSLPGEIRFNEDrtAHIVPRLPGIVDSVPANLGQAVKQGELLAVISSP----QLSDQRSEFAAAQR 233
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDE--ADLAAEVAGKITKISVREGQKVKKGQVLARLDDDdyqlALQAALAQLAAAEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 234 RLSLAQSTYKREQQLWKEGI-------SAEQEFLLARQGLQEAEIALNNARAKIAalggnpslqggnRYELRAPFAGVLV 306
Cdd:TIGR01730 79 QLELAQRSFERAERLVKRNAvsqadldDAKAAVEAAQADLEAAKASLASAQLNLR------------YTEIRAPFDGTIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 307 EKHLTQGEPVDGTANVFTLSDLSSVWATFNVPAQLLGQVRVGSKVKVLAQALDS-EVEGTVSYIGDLLGEQTRAATARVT 385
Cdd:TIGR01730 147 RRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGeEFKGKLRFIDPRVDSGTGTVRVRAT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 386 LSNPESTWRPGLFVSVQVAEATRKEVLTVADGAVQNVDGEDVVFVRVADGFVV-QPVKLGISDGQRVEVLEGLRAGSQVA 464
Cdd:TIGR01730 227 FPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSkRPVEVGLRNGGYVEIESGLKAGDQIV 306
|
....*...
gi 489200307 465 ASGSFILK 472
Cdd:TIGR01730 307 TAGVVKLR 314
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
155-403 |
4.50e-30 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 119.77 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 155 AAGITLDTARTISLAQVVSLPGEIrfnEDRTAHIVPRLPGIVDSVPANLGQAVKQGELLAVISSPQLSDQ---------- 224
Cdd:COG1566 18 ALGLALWAAGRNGPDEPVTADGRV---EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAAlaqaeaqlaa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 225 ---------------------RSEFAAAQRRLSLAQSTYKREQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAAL 283
Cdd:COG1566 95 aeaqlarleaelgaeaeiaaaEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 284 GGNPSLQGG----------------------NRYELRAPFAGVLVEKHLTQGEPVDGTANVFTLSDLSSVWATFNVPAQL 341
Cdd:COG1566 175 QAGLREEEElaaaqaqvaqaeaalaqaelnlARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETD 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489200307 342 LGQVRVGSKVKVLAQAL-DSEVEGTVSYIGDLLGEQTRAATA----------RVTLSNPES-TWRPGLFVSVQV 403
Cdd:COG1566 255 LGRVKPGQPVEVRVDAYpDRVFEGKVTSISPGAGFTSPPKNAtgnvvqrypvRIRLDNPDPePLRPGMSATVEI 328
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
168-464 |
3.47e-24 |
|
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: 102.89 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 168 LAQVVSLPGEIRFNEDRTAhIVPRLPGIVDSVPANLGQAVKQGELLAVISSPQLSDQRSE----FAAAQRRLSLAQSTYK 243
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKA-VQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSaeaqLAKAQAQVARLQAELD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 244 REQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAALGGNPslqggNRYELRAPFAGVLVEKHLTQGEPVDGTANVF 323
Cdd:pfam00529 83 RLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDL-----ARRRVLAPIGGISRESLVTAGALVAQAQANL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 324 --TLSDLSSVWATFNVPAQLLGQVRVGSKVKVLAQALDSEVE------------------GTVSYIGDLLGEQTRAATAR 383
Cdd:pfam00529 158 laTVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAElklakldlerteirapvdGTVAFLSVTVDGGTVSAGLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 384 VTLSNPE-STWRPGLFVSVQVAEA-TRKEVLTVADGAVQNVDGEDVVFVR-VADGFVVQPVKLGISDGQRVEVLEGLRAG 460
Cdd:pfam00529 238 LMFVVPEdNLLVPGMFVETQLDQVrVGQPVLIPFDAFPQTKTGRFTGVVVgISPDTGPVRVVVDKAQGPYYPLRIGLSAG 317
|
....
gi 489200307 461 SQVA 464
Cdd:pfam00529 318 ALVR 321
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
296-396 |
1.44e-15 |
|
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: 72.39 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 296 ELRAPFAGVLVEKHLTQGEPVDGTANVFTLSDLSSVWATFNVPAQLLGQVRVGSKVKV-LAQALDSEVEGTVSYIGDLLG 374
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLkLDPGSDYTLEGKVVRISPTVD 80
|
90 100
....*....|....*....|....
gi 489200307 375 EQTRAATARVTLSNP--ESTWRPG 396
Cdd:pfam13437 81 PDTGVIPVRVSIENPktPIPLLPG 104
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
150-467 |
1.78e-13 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 71.67 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 150 AEQIEAA----GITLDTARTISLAQvvSLPGeiRFNEDRTAHIVPRLPGIVDSVPANLGQAVKQGELLAVIS----SPQL 221
Cdd:PRK09859 26 AENAAAMtpevGVVTLSPGSVNVLS--ELPG--RTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDpaplQAEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 222 SDQRSEFAAAQRRLSLAQSTYKREQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAALGGNpsLQGGNryeLRAPF 301
Cdd:PRK09859 102 NSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATIN--LQYAN---VTSPI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 302 AGVLVEKHLTQGEPVdgTAN----VFTLSDLSSVWATFNVPAQ----LLGQVRVGSKVKVLAQ---ALDSE------VEG 364
Cdd:PRK09859 177 TGVSGKSSVTVGALV--TANqadsLVTVQRLDPIYVDLTQSVQdflrMKEEVASGQIKQVQGStpvQLNLEngkrysQTG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 365 TVSYIGDLLGEQTRAATARVTLSNPESTWRPGLFVSVQVAEATRKEVLTV-ADGAVQNVDGEDVVFVRVADGFVVQ-PVK 442
Cdd:PRK09859 255 TLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVpQEGVTHNAQGKATALILDKDDVVQLrEIE 334
|
330 340
....*....|....*....|....*
gi 489200307 443 LGISDGQRVEVLEGLRAGSQVAASG 467
Cdd:PRK09859 335 ASKAIGDQWVVTSGLQAGDRVIVSG 359
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
148-474 |
4.75e-13 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 70.67 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 148 LDAEQIEAAGITLDTARTISLAQVVSLPGEIRFNEDRTAHIVPRLPGIVDSV-PANLGQAVKQGELLAVISSPQLSDQRS 226
Cdd:PRK09783 86 IDPTQTQNLGVKTATVTRGPLTFAQTFPANVSYNEYQYAIVQARAAGFIDKVyPLTVGDKVQKGTPLLDLTIPDWVEAQS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 227 EFaaaqrrLSLAQSTykreqqlwkeGISAEQEFLLAR---QGLQEAEIALNNARAKIAAlggnpslqggnRYELRAPFAG 303
Cdd:PRK09783 166 EY------LLLRETG----------GTATQTEGILERlrlAGMPEADIRRLIATRKIQT-----------RFTLKAPIDG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 304 VLVEKHLTQGEPVDGTANVFTLSDLSSVWATFNVPAQLLGQVRVGSKVKVLAQALDSEvEGTVSYIGDLLG--EQTRAAT 381
Cdd:PRK09783 219 VITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDK-TFTIRKWTLLPSvdAATRTLQ 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 382 ARVTLSNPESTWRPGLFVSVQVAEATRKEVLTVADGAVQNVDGEDVVFVRVADGFVVQPVKLGISDGQRVEVLEGLRAGS 461
Cdd:PRK09783 298 LRLEVDNADEALKPGMNAWLQLNTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGE 377
|
330
....*....|...
gi 489200307 462 QVAASGSFILKSE 474
Cdd:PRK09783 378 KVVSSGLFLIDSE 390
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
150-467 |
2.91e-11 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 65.12 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 150 AEQIEAAGITldTARTISLAQVVSLPGeiRFNEDRTAHIVPRLPGIVDSVPANLGQAVKQGELLAVIS----SPQLSDQR 225
Cdd:PRK15030 34 GQQMPAVGVV--TVKTEPLQITTELPG--RTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDpatyQATYDSAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 226 SEFAAAQRRLSLAQSTYKREQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAALGGNPSLQggnryELRAPFAGVL 305
Cdd:PRK15030 110 GDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYT-----KVTSPISGRI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 306 VEKHLTQGEPV-DGTANVF-TLSDLSSVWATFNVPAQ------------LLGQVRVGSKVK-VLAQALDSEVEGTVSYIG 370
Cdd:PRK15030 185 GKSNVTEGALVqNGQATALaTVQQLDPIYVDVTQSSNdflrlkqelangTLKQENGKAKVSlITSDGIKFPQDGTLEFSD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 371 DLLGEQTRAATARVTLSNPESTWRPGLFVSVQVAEATRKEVLTV-ADGAVQNVDGEDVVFVRVADGFV-VQPVKLGISDG 448
Cdd:PRK15030 265 VTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVpQQGVTRTPRGDATVLVVGADDKVeTRPIVASQAIG 344
|
330
....*....|....*....
gi 489200307 449 QRVEVLEGLRAGSQVAASG 467
Cdd:PRK15030 345 DKWLVTEGLKAGDRVVISG 363
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
204-467 |
1.09e-08 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 57.11 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 204 GQAVKQGELLAVIS-SP---QLSDQRSEFAAAQRRLSLAQSTYKREQQLWKEGISAEQEfLLARQGL---QEAEI----- 271
Cdd:PRK11556 106 GQQVKAGDLLAEIDpRPfkvALAQAQGQLAKDQATLANARRDLARYQQLAKTNLVSRQE-LDAQQALvseTEGTIkadea 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 272 ALNNAR---------AKIAALGGNPSLQGGNrYELRAPFAGVLVekhLTQGEPVDgtaNVFTL--SDLSSVwatfnVPAQ 340
Cdd:PRK11556 185 SVASAQlqldysritAPISGRVGLKQVDVGN-QISSGDTTGIVV---ITQTHPID---LVFTLpeSDIATV-----VQAQ 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 341 LLGQvrvgskvKVLAQALDSEVEGTVSYiGDLLG--EQTRAATARVTL----SNPESTWRPGLFVSVQVAEATRKEVLTV 414
Cdd:PRK11556 253 KAGK-------PLVVEAWDRTNSKKLSE-GTLLSldNQIDATTGTIKLkarfNNQDDALFPNQFVNARMLVDTLQNAVVI 324
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 489200307 415 ADGAVQNvdGEDVVFVRVADG---FVVQPVKLGISDGQRVEVLEGLRAGSQVAASG 467
Cdd:PRK11556 325 PTAALQM--GNEGHFVWVLNDenkVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDG 378
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
202-466 |
4.82e-07 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 51.70 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 202 NLGQAVKQGELLAVISSPQLSDQRSEFAA------AQRR-----LSLAQSTYKREQQLWKEGisaeqefLLARQGLQEAE 270
Cdd:PRK11578 78 AIGDKVKKDQLLGVIDPEQAENQIKEVEAtlmelrAQRQqaeaeLKLARVTLSRQQRLAKTQ-------AVSQQDLDTAA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 271 IALNNARAKIAALGGN-----PSLQGGN---RY-ELRAPFAGVLVEKHLTQGEPVDGT---ANVFTLSDLSSVWATFNVP 338
Cdd:PRK11578 151 TELAVKQAQIGTIDAQikrnqASLDTAKtnlDYtRIVAPMAGEVTQITTLQGQTVIAAqqaPNILTLADMSTMLVKAQVS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 339 AQLLGQVRVGSKV--KVLAqALDSEVEGTvsyIGDLL--GEQTRAA---TARVTLSNPESTWRPGLFVSVQVAEATRKEV 411
Cdd:PRK11578 231 EADVIHLKPGQKAwfTVLG-DPLTRYEGV---LKDILptPEKVNDAifyYARFEVPNPNGLLRLDMTAQVHIQLTDVKNV 306
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 489200307 412 LTVADGAVQNVDGEDVVFVRVADGFVVQP--VKLGISDGQRVEVLEGLRAGSQVAAS 466
Cdd:PRK11578 307 LTIPLSALGDPVGDNRYKVKLLRNGETREreVTIGARNDTDVEIVKGLEAGDEVIIG 363
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
225-353 |
6.37e-07 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 51.12 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 225 RSEFAAAQRRLSLAQSTYKREQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAAlggnpsLQGGNRYE-------- 296
Cdd:PRK03598 113 RAAVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDKLSQ------YREGNRPQdiaqakas 186
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489200307 297 -------------------LRAPFAGVLVEKHLTQGEPVDGTANVFTLSDLSSVWATFNVPAQLLGQVRVGSKVKV 353
Cdd:PRK03598 187 laqaqaalaqaelnlqdteLIAPSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLL 262
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
185-353 |
1.51e-05 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 46.94 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 185 TAHIVPRLPGIVDSVPANLGQAVKQGELL-----------------------AVISSPQ--LSDQRSEFAA-------AQ 232
Cdd:PRK10476 48 VVHVASEVGGRIVELAVTENQAVKKGDLLfridprpyeltvaqaqadlaladAQIMTTQrsVDAERSNAASaneqverAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 233 RRLSLAQSTYKREQQLWKEGISAEQEFLLARQGLQEAEIALNNAR----AKIAALGGNPSLQGG----------NRYEL- 297
Cdd:PRK10476 128 ANAKLATRTLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQALlqaqAAAAAVGGVDALVAQraareaalaiAELHLe 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 298 ----RAPFAGVLVEKHLTQGEPVDGTANVFTLSDLSSVWATFNVPAQLLGQVRVGSKVKV 353
Cdd:PRK10476 208 dttvRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATV 267
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
143-463 |
1.83e-04 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 43.63 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 143 EGKLELDAEQIEAAGITLDTARTISLAQVVSLPGeiRFNEDRTAHIVPRLPGIVDSVPANLGQAVKQGELLAVISSPQLS 222
Cdd:PRK09578 23 CGKGDSDAAAAAPREATVVTVRPTSVPMTVELPG--RLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 223 DQRSefaAAQRRLSLAQSTY-------KREQQLWKEGISAEQEFLLARQGLQEAEIALNNARAKIAalggNPSLQGGnRY 295
Cdd:PRK09578 101 AARD---AAAGALAKAEAAHlaaldkrRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELA----RAQLQLD-YA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 296 ELRAPFAGVLVEKHLTQGEPV--DGTANVFTLSDLSSVWATFNVPA----QLLGQVRVGsKVKVLAQAlDSEV-----EG 364
Cdd:PRK09578 173 TVTAPIDGRARRALVTEGALVgqDQATPLTTVEQLDPIYVNFSQPAadveALRRAVKSG-RATGIAQQ-DVAVtlvraDG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 365 TVS------YIGDLLGEQTRAATA-RVTLSNPESTWRPGLFVSVQVAEATRKEVLTVADGAVQNVDGEDVVFVRVADGfV 437
Cdd:PRK09578 251 SEYplkgklLFSDLAVDPTTDTVAmRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNG-K 329
|
330 340
....*....|....*....|....*....
gi 489200307 438 VQPVKL---GISDGQRVeVLEGLRAGSQV 463
Cdd:PRK09578 330 VRDVEVeadQMSGRDWI-VTRGLAGGERV 357
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
102-403 |
2.31e-04 |
|
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: 43.28 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 102 LFKASGDGLVANAGIAEPHAFTARL-KLMAGKQGYDFAfTREEGKLELDAEQIEAAGITLDTARTISLAQVVSLPGEIRF 180
Cdd:TIGR02971 30 LLVAEGDRVQAGQVLAELDSRPERTaELDVARTQLDEA-KARLAQVRAGAKKGEIAAQRAARAAAKLFKDVAAQQATLNR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 181 --NEDRTAHI-VPRLPGIVdSVPANLGQAVKQGELlavisspQLSDQRSEFAAAQRRLSLAQSTYKREQQLWKEGIsAEQ 257
Cdd:TIGR02971 109 leAELETAQReVDRYRSLF-RDGAVSASDLDSKAL-------KLRTAEEELEEALASRSEQIDGARAALASLAEEV-RET 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489200307 258 EFLLARQGLQEAEIALNNARAKIaalggnpslqggNRYELRAPFAGVLVEKHLTQGEPVdGTANVFTLSDLSSVWATFNV 337
Cdd:TIGR02971 180 DVDLAQAEVKSALEAVQQAEALL------------ELTYVKAPIDGRVLKIHAREGEVI-GSEGILEMGDTSQMYAVAEV 246
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489200307 338 PAQLLGQVRVGSKVKVLAQALDSEVEGTVSYIGDLLGEQT------------RAATARVTLsNPESTWRPGLFVSVQV 403
Cdd:TIGR02971 247 YETDINRVRVGQRATITSTALSGPLRGTVRRIGSLIAKNDvlstdpaadadaRVVEVKIRL-DPASSERVGRLTNLQV 323
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
220-285 |
4.85e-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: 38.27 E-value: 4.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489200307 220 QLSDQRSEFAAAQRRLSLAQSTYKREQQLWKEG-------ISAEQEFLLARQGLQEAEIALNNARAKIAALGG 285
Cdd:pfam02321 109 QLLAAKEQLELAEQALELAEEALELAEARYEAGlislldvLQAEVELLEARLELLNAEADLELALAQLEQLLG 181
|
|
| |
