|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
47-383 |
2.80e-94 |
|
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: 285.30 E-value: 2.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 47 VVVKSISQWDSFNGRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARS 126
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 127 EANRTDKLINTNLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGDsasVL 206
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT---PL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 207 TTLVSQKTVYVYFDVDESTYLHYqnlaRSGQgassnhtalPVEIGLAGEEGYPHQGKVDFLDNQLAPSTGTIRMRALLDN 286
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARL----KVGQ---------PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 287 AQRQFTPGLFARVRLPGSAEFQATLIDDKAVLTDQDRKYVYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVIVDG 366
Cdd:COG0845 227 PDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSG 306
|
330
....*....|....*..
gi 1418658188 367 LQKVfMPGMPVNAKTVA 383
Cdd:COG0845 307 LQRL-RDGAKVRVVEAA 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
47-377 |
3.94e-74 |
|
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: 233.36 E-value: 3.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 47 VVVKSISQWDSFNGRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARS 126
Cdd:TIGR01730 6 VESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 127 EANRTDKLINTNLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGdsaSVL 206
Cdd:TIGR01730 86 SFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG---QTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 207 TTLVSQKTVYVYFDVDEstylHYQNLARSGQgassnhtalPVEIGLAGEEGYPHQGKVDFLDNQLAPSTGTIRMRALLDN 286
Cdd:TIGR01730 163 ATIVDLDPLEADFSVPE----RDLPQLRRGQ---------TLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 287 AQRQFTPGLFARVRLPGSAEFQATLIDDKAVLTDQDRKYVYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVIVDG 366
Cdd:TIGR01730 230 PDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAG 309
|
330
....*....|.
gi 1418658188 367 LQKVfMPGMPV 377
Cdd:TIGR01730 310 VVKL-RDGAKV 319
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
60-379 |
1.93e-53 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 181.92 E-value: 1.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 60 GRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARSEANRTDKLINTNL 139
Cdd:PRK09578 56 GRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 140 VSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVtAGDSASVLTTLVSQKTVYVYF 219
Cdd:PRK09578 136 VSERDYTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPIDGRARRALVTEGALV-GQDQATPLTTVEQLDPIYVNF 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 220 DVDESTYLHYQNLARSGQGASSNHTALPVEIGLAGEEGYPHQGKVDFLDNQLAPSTGTIRMRALLDNAQRQFTPGLFARV 299
Cdd:PRK09578 215 SQPAADVEALRRAVKSGRATGIAQQDVAVTLVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 300 RLPGSAEFQATLIDDKAVLTDQDRKYVYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVIVDGLQKvFMPGMPVNA 379
Cdd:PRK09578 295 ALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQ-FAPGTAVKA 373
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
53-364 |
1.23e-41 |
|
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: 149.11 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 53 SQWDSFNGRIEAV-ESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARSEANRT 131
Cdd:pfam00529 5 TKGVEAPGRVVVSgNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 132 DKLINTNLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGdSASVLTTLVS 211
Cdd:pfam00529 85 QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQA-QANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 212 QKTVYVYFDVDESTYLHYQNLARSGQGASSNhtALPVEIGLAGEEG------YPHQGKVDFLDNQLAPSTGTIRMRALLD 285
Cdd:pfam00529 164 LDQIYVQITQSAAENQAEVRSELSGAQLQIA--EAEAELKLAKLDLerteirAPVDGTVAFLSVTVDGGTVSAGLRLMFV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 286 NAQRQFT-PGLFARVRLPGSAEFQATLIDDKAVLTDQDRKY-VYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVI 363
Cdd:pfam00529 242 VPEDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVR 321
|
.
gi 1418658188 364 V 364
Cdd:pfam00529 322 L 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
47-383 |
2.80e-94 |
|
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: 285.30 E-value: 2.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 47 VVVKSISQWDSFNGRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARS 126
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 127 EANRTDKLINTNLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGDsasVL 206
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGT---PL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 207 TTLVSQKTVYVYFDVDESTYLHYqnlaRSGQgassnhtalPVEIGLAGEEGYPHQGKVDFLDNQLAPSTGTIRMRALLDN 286
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARL----KVGQ---------PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 287 AQRQFTPGLFARVRLPGSAEFQATLIDDKAVLTDQDRKYVYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVIVDG 366
Cdd:COG0845 227 PDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSG 306
|
330
....*....|....*..
gi 1418658188 367 LQKVfMPGMPVNAKTVA 383
Cdd:COG0845 307 LQRL-RDGAKVRVVEAA 322
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
47-377 |
3.94e-74 |
|
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: 233.36 E-value: 3.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 47 VVVKSISQWDSFNGRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARS 126
Cdd:TIGR01730 6 VESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 127 EANRTDKLINTNLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGdsaSVL 206
Cdd:TIGR01730 86 SFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG---QTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 207 TTLVSQKTVYVYFDVDEstylHYQNLARSGQgassnhtalPVEIGLAGEEGYPHQGKVDFLDNQLAPSTGTIRMRALLDN 286
Cdd:TIGR01730 163 ATIVDLDPLEADFSVPE----RDLPQLRRGQ---------TLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 287 AQRQFTPGLFARVRLPGSAEFQATLIDDKAVLTDQDRKYVYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVIVDG 366
Cdd:TIGR01730 230 PDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAG 309
|
330
....*....|.
gi 1418658188 367 LQKVfMPGMPV 377
Cdd:TIGR01730 310 VVKL-RDGAKV 319
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
60-379 |
1.93e-53 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 181.92 E-value: 1.93e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 60 GRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARSEANRTDKLINTNL 139
Cdd:PRK09578 56 GRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 140 VSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVtAGDSASVLTTLVSQKTVYVYF 219
Cdd:PRK09578 136 VSERDYTEAVADERQAKAAVASAKAELARAQLQLDYATVTAPIDGRARRALVTEGALV-GQDQATPLTTVEQLDPIYVNF 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 220 DVDESTYLHYQNLARSGQGASSNHTALPVEIGLAGEEGYPHQGKVDFLDNQLAPSTGTIRMRALLDNAQRQFTPGLFARV 299
Cdd:PRK09578 215 SQPAADVEALRRAVKSGRATGIAQQDVAVTLVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRI 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 300 RLPGSAEFQATLIDDKAVLTDQDRKYVYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVIVDGLQKvFMPGMPVNA 379
Cdd:PRK09578 295 ALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQ-FAPGTAVKA 373
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
3-382 |
4.43e-48 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 167.97 E-value: 4.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 3 LQKTWGNDPLHALGAILLSLLLVGCDNSVAQNAAPPAPAVNAADVVVKSISQWDSFNGRIEAVESVQLRPRVSGYIDKVN 82
Cdd:PRK15030 1 MNKNRGFTPLAVVLMLSGSLALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 83 FTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARSEANRTDKLINTNLVSREEWEQRRAAAIQAQADIRAA 162
Cdd:PRK15030 81 FKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 163 QAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGDSASVLTTlvsQKTVYVYFDVDEST--YLHYQNLARSGQGAS 240
Cdd:PRK15030 161 KAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATV---QQLDPIYVDVTQSSndFLRLKQELANGTLKQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 241 SNHTAlPVEIGLAGEEGYPHQGKVDFLDNQLAPSTGTIRMRALLDNAQRQFTPGLFARVRLPGSAEFQATLIDDKAVL-T 319
Cdd:PRK15030 238 ENGKA-KVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTrT 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418658188 320 DQDRKYVYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVIVDGLQKVfMPGMPVNAKTV 382
Cdd:PRK15030 317 PRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKV-RPGVQVKAQEV 378
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
26-391 |
1.14e-44 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 158.72 E-value: 1.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 26 GCDNSVAQNAAPPAPAVNAADVVVKSISQWDSFNGRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRA 105
Cdd:PRK09859 20 ACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 106 ALEQAQATLERAKTQASLARSEANRTDKLINTNLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGR 185
Cdd:PRK09859 100 ELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 186 ASRALITSGNLVTAGDSASVLTTlvsQKTVYVYFDVDEST--YLHYQNLARSGQgASSNHTALPVEIGLAGEEGYPHQGK 263
Cdd:PRK09859 180 SGKSSVTVGALVTANQADSLVTV---QRLDPIYVDLTQSVqdFLRMKEEVASGQ-IKQVQGSTPVQLNLENGKRYSQTGT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 264 VDFLDNQLAPSTGTIRMRALLDNAQRQFTPGLFARVRLPGSAEFQATLIDDKAVLTD-QDRKYVYIVDKEGKAQRRDITP 342
Cdd:PRK09859 256 LKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNaQGKATALILDKDDVVQLREIEA 335
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1418658188 343 GRLADGLRIVQQGLKPGDKVIVDGLQKVfMPGmpVNAKTVAMTVSTALN 391
Cdd:PRK09859 336 SKAIGDQWVVTSGLQAGDRVIVSGLQRI-RPG--IKARAISSSQENAST 381
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
60-369 |
3.65e-43 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 155.33 E-value: 3.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 60 GRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLerAKTQASL--ARSEANRTDKLINT 137
Cdd:PRK11556 80 GTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQL--AKDQATLanARRDLARYQQLAKT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 138 NLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGDSASVLtTLVSQKTVYV 217
Cdd:PRK11556 158 NLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIV-VITQTHPIDL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 218 YFDVDEStylhyqNLARSGQGASSNHTaLPVEIGLAGEEGYPHQGKVDFLDNQLAPSTGTIRMRALLDNAQRQFTPGLFA 297
Cdd:PRK11556 237 VFTLPES------DIATVVQAQKAGKP-LVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFV 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1418658188 298 RVRLPGSAEFQATLIDDKAVLTDQDRKYVYIVDKEGKAQRRDITPGrLADGLRIV-QQGLKPGDKVIVDGLQK 369
Cdd:PRK11556 310 NARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPG-IQDSQKVViSAGLSAGDRVVTDGIDR 381
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
53-364 |
1.23e-41 |
|
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: 149.11 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 53 SQWDSFNGRIEAV-ESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARSEANRT 131
Cdd:pfam00529 5 TKGVEAPGRVVVSgNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 132 DKLINTNLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGdSASVLTTLVS 211
Cdd:pfam00529 85 QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQA-QANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 212 QKTVYVYFDVDESTYLHYQNLARSGQGASSNhtALPVEIGLAGEEG------YPHQGKVDFLDNQLAPSTGTIRMRALLD 285
Cdd:pfam00529 164 LDQIYVQITQSAAENQAEVRSELSGAQLQIA--EAEAELKLAKLDLerteirAPVDGTVAFLSVTVDGGTVSAGLRLMFV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 286 NAQRQFT-PGLFARVRLPGSAEFQATLIDDKAVLTDQDRKY-VYIVDKEGKAQRRDITPGRLADGLRIVQQGLKPGDKVI 363
Cdd:pfam00529 242 VPEDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVR 321
|
.
gi 1418658188 364 V 364
Cdd:pfam00529 322 L 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
59-301 |
1.60e-27 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 110.91 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 59 NGRIEAvESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQA-------------------------- 112
Cdd:COG1566 38 DGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAqlaaaeaqlarleaelgaeaeiaaae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 113 -TLERAKTQASLARSEANRTDKLINTNLVSREEWE---------------------------QRRAAAIQAQADIRAAQA 164
Cdd:COG1566 117 aQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDearaaldaaqaqleaaqaqlaqaqaglREEEELAAAQAQVAQAEA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 165 AVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGDSasvLTTLVSQKTVYVYFDVDEsTYLHYqnlARSGQgassnht 244
Cdd:COG1566 197 ALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP---LLTIVPLDDLWVEAYVPE-TDLGR---VKPGQ------- 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1418658188 245 alPVEIGLAGEEGYPHQGKVDFL----------DNQLAPSTGTIRMRALLDNAQ-RQFTPGLFARVRL 301
Cdd:COG1566 263 --PVEVRVDAYPDRVFEGKVTSIspgagftsppKNATGNVVQRYPVRIRLDNPDpEPLRPGMSATVEI 328
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
68-217 |
1.10e-16 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 79.78 E-value: 1.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 68 VQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQASLARSEANRTDKLiNTNLVSREEWEQ 147
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRL-GVQAMSREEIDQ 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 148 RRAAAIQAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGDSAsvlTTLVSQKTVYV 217
Cdd:PRK10559 127 ANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTA---VALVKQNSFYV 193
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
60-297 |
6.93e-14 |
|
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: 70.23 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 60 GRIEAVES--VQLRPRVSGYIDK--VNFTdGQEVKKGEVLFTIddrtYRAALEQAQATLERAKT------QASLARSEAN 129
Cdd:pfam16576 10 GRVAYDERrlAHVHARVEGWIEKlyVNAT-GDPVKKGQPLAEL----YSPELVAAQQEYLLALRsgdalsKSELLRAARQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 130 R------TDKLINTNLVSREeweqrraaaiqaqadIRAAqaavdaaqlnldFTkVTAPIDGRASRALITSGNLVTAGDsa 203
Cdd:pfam16576 85 RlrllgmPEAQIAELERTGK---------------VQPT------------VT-VYAPISGVVTELNVREGMYVQPGD-- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 204 sVLTTLVSQKTVYVYFDVDEstylHYQNLARSGQGASSNHTALPveiglageeGYPHQGKVDFLDNQLAPSTGTIRMRAL 283
Cdd:pfam16576 135 -TLFTIADLSTVWVEADVPE----QDLALVKVGQPAEVTLPALP---------GKTFEGKVDYIYPTLDPKTRTVRVRIE 200
|
250
....*....|....
gi 1418658188 284 LDNAQRQFTPGLFA 297
Cdd:pfam16576 201 LPNPDGRLKPGMFA 214
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
66-115 |
4.40e-12 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 60.53 E-value: 4.40e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1418658188 66 ESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLE 115
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
60-364 |
8.94e-12 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 65.95 E-value: 8.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 60 GRIEAVESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDD-------RTYRAALEQAQATLERAKTQASLARSEANRTD 132
Cdd:PRK11578 54 GKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPeqaenqiKEVEATLMELRAQRQQAEAELKLARVTLSRQQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 133 KLINTNLVSREEWEQRRAAAI-------QAQADIRAAQAAVDAAQLNLDFTKVTAPIDGRASRALITSGNLVTAGDSASV 205
Cdd:PRK11578 134 RLAKTQAVSQQDLDTAATELAvkqaqigTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPN 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 206 LTTLVSQKTVYVYFDVDESTYLHYqnlaRSGQGASsnHTALpveiglaGEEGYPHQGKV-DFLdnqlaPSTGTIRmRALL 284
Cdd:PRK11578 214 ILTLADMSTMLVKAQVSEADVIHL----KPGQKAW--FTVL-------GDPLTRYEGVLkDIL-----PTPEKVN-DAIF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 285 DNAqRQFTPGLFARVRLPGSAEFQATLIDDKAVLT-------DQ--DRKYVYIVDKEGKAQRRDITPGRLADGLRIVQQG 355
Cdd:PRK11578 275 YYA-RFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTiplsalgDPvgDNRYKVKLLRNGETREREVTIGARNDTDVEIVKG 353
|
....*....
gi 1418658188 356 LKPGDKVIV 364
Cdd:PRK11578 354 LEAGDEVII 362
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
66-217 |
1.26e-09 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 59.27 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 66 ESVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATL----------------------------ERA 117
Cdd:PRK10476 47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLaladaqimttqrsvdaersnaasaneqvERA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 118 KTQASLARSEANRTDKLINTNLVSREEWEQRRAAAIQAQADIRAAQAAVDAAQ------------------------LNL 173
Cdd:PRK10476 127 RANAKLATRTLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQALLQAQAAAaavggvdalvaqraareaalaiaeLHL 206
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1418658188 174 DFTKVTAPIDGRASRALITSGNLVTAGDSasvLTTLVSQKTVYV 217
Cdd:PRK10476 207 EDTTVRAPFDGRVVGLKVSVGEFAAPMQP---IFTLIDTDHWYA 247
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
68-144 |
3.49e-07 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 51.62 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 68 VQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQA---------------------QATLERAKTQASLARS 126
Cdd:PRK15136 62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAktalansvrqthqlminskqyQANIELQKTALAQAQS 141
|
90
....*....|....*...
gi 1418658188 127 EANRTDKLINTNLVSREE 144
Cdd:PRK15136 142 DLNRRVPLGNANLIGREE 159
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
273-367 |
4.67e-06 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 48.33 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 273 PSTGTIRMRALLDNAQRQFTPGLFARVRLPGSAEfQATLIDDKAVLTDQDRKYVYIVDKEGKAQRRDITPGRLADGLRIV 352
Cdd:PRK09783 291 AATRTLQLRLEVDNADEALKPGMNAWLQLNTASE-PMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAI 369
|
90
....*....|....*
gi 1418658188 353 QQGLKPGDKVIVDGL 367
Cdd:PRK09783 370 RSGLAEGEKVVSSGL 384
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
177-294 |
7.74e-05 |
|
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: 41.58 E-value: 7.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 177 KVTAPIDGRASRALITSGNLVTAGDsasVLTTLVSQKTVYVYFDVDEstylhyQNLARSGQGAssnhtalPVEIGLAGEE 256
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGD---PLATIVPPDRLLVEAFVPA------ADLGSLKKGQ-------KVTLKLDPGS 64
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1418658188 257 GYPHQGKVDFLDNQLAPSTGTIRMRALLDN--AQRQFTPG 294
Cdd:pfam13437 65 DYTLEGKVVRISPTVDPDTGVIPVRVSIENpkTPIPLLPG 104
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
67-266 |
2.39e-03 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 39.56 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 67 SVQLRPRVSGYIDKVNFTDGQEVKKGEVLFTIDDRTYRAALEQAQATLERAKTQ-----------------ASLARSEA- 128
Cdd:PRK03598 43 TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQldlmlagyrdeeiaqarAAVKQAQAa 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 129 --------NRTDKLINTNLVSREEWEQRRAAAIQAQADIRAAQA--------------------------AVDAAQLNLD 174
Cdd:PRK03598 123 ydyaqnfyNRQQGLWKSRTISANDLENARSSRDQAQATLKSAQDklsqyregnrpqdiaqakaslaqaqaALAQAELNLQ 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1418658188 175 FTKVTAPIDGRA-SRAlITSGNLVTAGDSASVLTTlvsQKTVYVYFDVDEStylhyqNLARSgqgassnHTALPVEIGLA 253
Cdd:PRK03598 203 DTELIAPSDGTIlTRA-VEPGTMLNAGSTVFTLSL---TRPVWVRAYVDER------NLGQA-------QPGRKVLLYTD 265
|
250
....*....|...
gi 1418658188 254 GEEGYPHQGKVDF 266
Cdd:PRK03598 266 GRPDKPYHGQIGF 278
|
|
| |
