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Conserved domains on  [gi|516296625|ref|WP_017699932|]
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MULTISPECIES: efflux RND transporter periplasmic adaptor subunit [Pseudomonas syringae group]

Protein Classification

efflux RND transporter periplasmic adaptor subunit( domain architecture ID 11436533)

efflux RND (resistance-nodulation-division) transporter periplasmic adaptor subunit, similar to Bacillus subtilis YknX, which is part of an unusual four-component transporter with a role in protection against sporulation-delaying-protein-induced killing

CATH:  2.40.50.100|2.40.420.20|2.40.30.170|1.10.287.470
Gene Ontology:  GO:0016020|GO:0055085|GO:0022857|GO:0042802
PubMed:  32073314
TCDB:  2.A.6

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 43-369 8.29e-89

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: 271.82  E-value: 8.29e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  43 KVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVASRSD 122
Cdd:COG0845    2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 123 SEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVTADvTALT 202
Cdd:COG0845   82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG-TPLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 203 SVVSTDKVYAYFDADERVFLKYtelaRKGQrgqttPVYLGLSNETGNPHLGQMNFVDNQVNPRTGTIRGRAVFDNADGSF 282
Cdd:COG0845  161 TIADLDPLEVEFDVPESDLARL----KVGQ-----PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 283 TPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMDKDNKPAYRAVELGPKIEGLRIVRNGLAKDDTIVVKGLQRVR 362
Cdd:COG0845  232 RPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLR 311


                 ....*..
gi 516296625 363 PGQPVDP 369
Cdd:COG0845  312 DGAKVRV 318
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 43-369 8.29e-89

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: 271.82  E-value: 8.29e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  43 KVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVASRSD 122
Cdd:COG0845    2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 123 SEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVTADvTALT 202
Cdd:COG0845   82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG-TPLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 203 SVVSTDKVYAYFDADERVFLKYtelaRKGQrgqttPVYLGLSNETGNPHLGQMNFVDNQVNPRTGTIRGRAVFDNADGSF 282
Cdd:COG0845  161 TIADLDPLEVEFDVPESDLARL----KVGQ-----PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 283 TPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMDKDNKPAYRAVELGPKIEGLRIVRNGLAKDDTIVVKGLQRVR 362
Cdd:COG0845  232 RPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLR 311


                 ....*..
gi 516296625 363 PGQPVDP 369
Cdd:COG0845  312 DGAKVRV 318
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 39-367 1.64e-71

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: 227.58  E-value: 1.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625   39 VTVAKVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVA 118
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  119 SRSDSEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVTADV 198
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  199 TALTsVVSTDKVYAYFDADERvflkYTELARKGQrgqttPVYLGLSNETGNPHLGQMNFVDNQVNPRTGTIRGRAVFDNA 278
Cdd:TIGR01730 161 TLAT-IVDLDPLEADFSVPER----DLPQLRRGQ-----TLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  279 DGSFTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMDKDNKPAYRAVELGPKIEGLRIVRNGLAKDDTIVVKGL 358
Cdd:TIGR01730 231 DGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGV 310


                  ....*....
gi 516296625  359 QRVRPGQPV 367
Cdd:TIGR01730 311 VKLRDGAKV 319
PRK09859 PRK09859
multidrug transporter subunit MdtE;
19-364 7.15e-49

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 170.28  E-value: 7.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  19 VISACGGGAQQAANApGAAKVTVAKVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPR 98
Cdd:PRK09859  17 MLTACDDKSAENAAA-MTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  99 PFQSEVRRLEAQLQQARAVASRSDSEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAP 178
Cdd:PRK09859  96 PLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 179 IAGRVSRAEITAGNIVTADVT-ALTSVVSTDKVYAYFDADERVFLKYTELARKGQRGQ---TTPVYLGLSNETGNPHLGQ 254
Cdd:PRK09859 176 ITGVSGKSSVTVGALVTANQAdSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQvqgSTPVQLNLENGKRYSQTGT 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 255 MNFVDNQVNPRTGTIRGRAVFDNADGSFTPGLYARLKLVGSGTYSAVLINDEAVGTDL-GKKFVLVMDKDNKPAYRAVEL 333
Cdd:PRK09859 256 LKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAqGKATALILDKDDVVQLREIEA 335

                        330       340       350
                 ....*....|....*....|....*....|.
gi 516296625 334 GPKIEGLRIVRNGLAKDDTIVVKGLQRVRPG 364
Cdd:PRK09859 336 SKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 46-355 1.74e-47

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: 164.90  E-value: 1.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625   46 EQPVNEWDEFTGRLEA-PETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVASRSDSE 124
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  125 AQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVT-ADVTALTS 203
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAqAQANLLAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  204 VVSTDKVYAYFDADERVFLKY----------------TELARKGQRGQTTPVYlglsnetgNPHLGQMNFVDNQVNPRTG 267
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEvrselsgaqlqiaeaeAELKLAKLDLERTEIR--------APVDGTVAFLSVTVDGGTV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  268 TIRGRAVFDNADGSFT-PGLYARLKLVGSGTYSAVLINDEAVGTDLGKKF-VLVMDKDNKPAYRAVELGPKIEGLRIVRN 345
Cdd:pfam00529 233 SAGLRLMFVVPEDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRI 312

                         330
                  ....*....|
gi 516296625  346 GLAKDDTIVV 355
Cdd:pfam00529 313 GLSAGALVRL 322
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 43-369 8.29e-89

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: 271.82  E-value: 8.29e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  43 KVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVASRSD 122
Cdd:COG0845    2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 123 SEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVTADvTALT 202
Cdd:COG0845   82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG-TPLF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 203 SVVSTDKVYAYFDADERVFLKYtelaRKGQrgqttPVYLGLSNETGNPHLGQMNFVDNQVNPRTGTIRGRAVFDNADGSF 282
Cdd:COG0845  161 TIADLDPLEVEFDVPESDLARL----KVGQ-----PVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 283 TPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMDKDNKPAYRAVELGPKIEGLRIVRNGLAKDDTIVVKGLQRVR 362
Cdd:COG0845  232 RPGMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLR 311


                 ....*..
gi 516296625 363 PGQPVDP 369
Cdd:COG0845  312 DGAKVRV 318
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 39-367 1.64e-71

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: 227.58  E-value: 1.64e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625   39 VTVAKVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVA 118
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  119 SRSDSEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVTADV 198
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  199 TALTsVVSTDKVYAYFDADERvflkYTELARKGQrgqttPVYLGLSNETGNPHLGQMNFVDNQVNPRTGTIRGRAVFDNA 278
Cdd:TIGR01730 161 TLAT-IVDLDPLEADFSVPER----DLPQLRRGQ-----TLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  279 DGSFTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMDKDNKPAYRAVELGPKIEGLRIVRNGLAKDDTIVVKGL 358
Cdd:TIGR01730 231 DGRLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGV 310


                  ....*....
gi 516296625  359 QRVRPGQPV 367
Cdd:TIGR01730 311 VKLRDGAKV 319
PRK09859 PRK09859
multidrug transporter subunit MdtE;
19-364 7.15e-49

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 170.28  E-value: 7.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  19 VISACGGGAQQAANApGAAKVTVAKVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPR 98
Cdd:PRK09859  17 MLTACDDKSAENAAA-MTPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  99 PFQSEVRRLEAQLQQARAVASRSDSEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAP 178
Cdd:PRK09859  96 PLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 179 IAGRVSRAEITAGNIVTADVT-ALTSVVSTDKVYAYFDADERVFLKYTELARKGQRGQ---TTPVYLGLSNETGNPHLGQ 254
Cdd:PRK09859 176 ITGVSGKSSVTVGALVTANQAdSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGQIKQvqgSTPVQLNLENGKRYSQTGT 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 255 MNFVDNQVNPRTGTIRGRAVFDNADGSFTPGLYARLKLVGSGTYSAVLINDEAVGTDL-GKKFVLVMDKDNKPAYRAVEL 333
Cdd:PRK09859 256 LKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHNAqGKATALILDKDDVVQLREIEA 335

                        330       340       350
                 ....*....|....*....|....*....|.
gi 516296625 334 GPKIEGLRIVRNGLAKDDTIVVKGLQRVRPG 364
Cdd:PRK09859 336 SKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 46-355 1.74e-47

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: 164.90  E-value: 1.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625   46 EQPVNEWDEFTGRLEA-PETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVASRSDSE 124
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  125 AQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVT-ADVTALTS 203
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAqAQANLLAT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  204 VVSTDKVYAYFDADERVFLKY----------------TELARKGQRGQTTPVYlglsnetgNPHLGQMNFVDNQVNPRTG 267
Cdd:pfam00529 161 VAQLDQIYVQITQSAAENQAEvrselsgaqlqiaeaeAELKLAKLDLERTEIR--------APVDGTVAFLSVTVDGGTV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  268 TIRGRAVFDNADGSFT-PGLYARLKLVGSGTYSAVLINDEAVGTDLGKKF-VLVMDKDNKPAYRAVELGPKIEGLRIVRN 345
Cdd:pfam00529 233 SAGLRLMFVVPEDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRI 312

                         330
                  ....*....|
gi 516296625  346 GLAKDDTIVV 355
Cdd:pfam00529 313 GLSAGALVRL 322
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
38-367 4.71e-47

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 166.04  E-value: 4.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  38 KVTVAKVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAV 117
Cdd:PRK15030  39 AVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAA 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 118 ASRSDSEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIV-TA 196
Cdd:PRK15030 119 ANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVqNG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 197 DVTALTSVVSTDKVYAYFDADERVFLKYTELARKG---QRGQTTPVYLGLSNETGNPHLGQMNFVDNQVNPRTGTIRGRA 273
Cdd:PRK15030 199 QATALATVQQLDPIYVDVTQSSNDFLRLKQELANGtlkQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRA 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 274 VFDNADGSFTPGLYARLKLVGSGTYSAVLINDEAVG-TDLGKKFVLVMDKDNKPAYRAVELGPKIEGLRIVRNGLAKDDT 352
Cdd:PRK15030 279 IFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTrTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDR 358

                        330
                 ....*....|....*
gi 516296625 353 IVVKGLQRVRPGQPV 367
Cdd:PRK15030 359 VVISGLQKVRPGVQV 373
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
21-389 4.25e-43

MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 155.72  E-value: 4.25e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  21 SACGGGAQQAANAPGA----------AKVTVAKVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGD 90
Cdd:PRK11556  34 SAAPGAAKQAQQSPAGgrrgmrsgplAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGD 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  91 LLFQIDPRPFQSEVRRLEAQLQQARAVASRSDSEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNL 170
Cdd:PRK11556 114 LLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQL 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 171 SFTRVTAPIAGRVSRAEITAGNIVTA-DVTALTSVVSTDKVYAYF---DADERVFLKytelARKgqRGQTTPVYLGLSNE 246
Cdd:PRK11556 194 DYSRITAPISGRVGLKQVDVGNQISSgDTTGIVVITQTHPIDLVFtlpESDIATVVQ----AQK--AGKPLVVEAWDRTN 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 247 TGNPHLGQMNFVDNQVNPRTGTIRGRAVFDNADGSFTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMDKDNKP 326
Cdd:PRK11556 268 SKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDENKV 347

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516296625 327 AYRAVELGPKIEGLRIVRNGLAKDDTIVVKGLQRVRPGQPVDPeVTPMASADTLAALQKQRQA 389
Cdd:PRK11556 348 SKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEV-VEPQSATTPEEKATSREYA 409
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
8-393 2.56e-42

MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 153.03  E-value: 2.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625   8 LRYPLTALALLVISACGGGAQQAANAPGAAKVTVAKVLEQPVNEWDEFTGRLEAPETVEVRPRVSGQIDQVAFTDGSVVK 87
Cdd:PRK09578   7 RRLLLAALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVK 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  88 KGDLLFQIDPRPFQSEVRRLEAQLQQARAVASRSDSEAQRGERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQLDLAR 167
Cdd:PRK09578  87 QGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQ 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 168 LNLSFTRVTAPIAGRVSRAEITAGNIVTAD-VTALTSVVSTDKVYAYFD---ADERVFLKYTELAR-KGQRGQTTPVYLG 242
Cdd:PRK09578 167 LQLDYATVTAPIDGRARRALVTEGALVGQDqATPLTTVEQLDPIYVNFSqpaADVEALRRAVKSGRaTGIAQQDVAVTLV 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 243 LSNETGNPHLGQMNFVDNQVNPRTGTIRGRAVFDNADGSFTPGLYARLKLVGSGTYSAVLINDEAVGTDLGKKFVLVMDK 322
Cdd:PRK09578 247 RADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQ 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516296625 323 DNkpayravelgpKIEGLRIVRNGLAKDDTIVVKGLQrvrPGQPVDPE-VTPMASADTLAALQKQRQALDAS 393
Cdd:PRK09578 327 NG-----------KVRDVEVEADQMSGRDWIVTRGLA---GGERVIVDnAAQFAPGTAVKAVERAPAAKPAP 384
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
56-219 9.78e-24

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 100.89  E-value: 9.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  56 TGRLEApETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQL------------------------ 111
Cdd:COG1566   38 DGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLaaaeaqlarleaelgaeaeiaaae 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 112 ---QQARAVASRSDSEAQRGERLRSNNAISAELADSRSTSAQEAKAG---------------------------VAAIQA 161
Cdd:COG1566  117 aqlAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQleaaqaqlaqaqaglreeeelaaaqaqVAQAEA 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516296625 162 QLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVTADvTALTSVVSTDKVYAYFDADER 219
Cdd:COG1566  197 ALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAG-QPLLTIVPLDDLWVEAYVPET 253
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 56-196 1.93e-18

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 85.98  E-value: 1.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  56 TGRLEAPETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLE-------AQLQQARAVASRSDSEAQRG 128
Cdd:PRK11578  53 TGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEatlmelrAQRQQAEAELKLARVTLSRQ 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516296625 129 ERLRSNNAISAELADSRSTSAQEAKAGVAAIQAQ-------LDLARLNLSFTRVTAPIAGRVSRAEITAGNIVTA 196
Cdd:PRK11578 133 QRLAKTQAVSQQDLDTAATELAVKQAQIGTIDAQikrnqasLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIA 207
PRK10476 PRK10476
multidrug transporter subunit MdtN;
63-212 8.96e-17

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 80.84  E-value: 8.96e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  63 ETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQ----------------------------QA 114
Cdd:PRK10476  47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLAladaqimttqrsvdaersnaasaneqveRA 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 115 RAVASRSDSEAQRGERLRSNNAISAELADSRSTSAQEAK------------------------AGVAAIQAQLDLARLNL 170
Cdd:PRK10476 127 RANAKLATRTLERLEPLLAKGYVSAQQVDQARTAQRDAEvslnqallqaqaaaaavggvdalvAQRAAREAALAIAELHL 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 516296625 171 SFTRVTAPIAGRVSRAEITAGNIVTADVTALTsVVSTDKVYA 212
Cdd:PRK10476 207 EDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFT-LIDTDHWYA 247
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
65-238 2.50e-16

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 79.01  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  65 VEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVASRSDSEAQRGERLrSNNAISAELADS 144
Cdd:PRK10559  48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRL-GVQAMSREEIDQ 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 145 RSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRVSRAEITAGNIVTADVTALtSVVSTDKVY--AYfdadervfL 222
Cdd:PRK10559 127 ANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAV-ALVKQNSFYvlAY--------M 197

                        170
                 ....*....|....*...
gi 516296625 223 KYTELA--RKGQRGQTTP 238
Cdd:PRK10559 198 EETKLEgvRPGYRAEITP 215
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
 64-215 2.66e-13

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 70.38  E-value: 2.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  64 TVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQ--------------------------QARAV 117
Cdd:PRK03598  43 TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSvaqaqldlmlagyrdeeiaqaraavkQAQAA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 118 ASRSDSEAQRGERLRSNNAISA-ELADSRSTSAQ-------------------------EAKAGVAAIQAQLDLARLNLS 171
Cdd:PRK03598 123 YDYAQNFYNRQQGLWKSRTISAnDLENARSSRDQaqatlksaqdklsqyregnrpqdiaQAKASLAQAQAALAQAELNLQ 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 516296625 172 FTRVTAPIAGRV-SRAeITAGNIVTADVTALTsvVSTDK---VYAYFD 215
Cdd:PRK03598 203 DTELIAPSDGTIlTRA-VEPGTMLNAGSTVFT--LSLTRpvwVRAYVD 247
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
63-112 8.77e-10

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 53.99  E-value: 8.77e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 516296625   63 ETVEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQ 112
Cdd:pfam13533   1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 56-288 8.68e-09

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: 55.21  E-value: 8.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625   56 TGRLEAPET--VEVRPRVSGQIDQV-AFTDGSVVKKGDLLFQIDPRPFQSEVRRLEAQLQQARAVASRSDSEAQRgERLR 132
Cdd:pfam16576   9 VGRVAYDERrlAHVHARVEGWIEKLyVNATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKSELLRAAR-QRLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  133 ----SNNAIsAELADSRSTSAqeakagvaaiqaqldlarlnlSFTrVTAPIAGRVSRAEITAGNIVTADvTALTSVVSTD 208
Cdd:pfam16576  88 llgmPEAQI-AELERTGKVQP---------------------TVT-VYAPISGVVTELNVREGMYVQPG-DTLFTIADLS 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  209 KVYAYFDaderVFLKYTELARKGQRGQTTPVYLGlsNETGNphlGQMNFVDNQVNPRTGTIRGRAVFDNADGSFTPGLYA 288
Cdd:pfam16576 144 TVWVEAD----VPEQDLALVKVGQPAEVTLPALP--GKTFE---GKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
65-232 2.28e-06

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 49.31  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  65 VEVRPRVSGQIDQVAFTDGSVVKKGDLLFQIDPRPFQ-----------SEVR----------RLEAQLQQARAVASRSDS 123
Cdd:PRK15136  62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEqafekaktalaNSVRqthqlminskQYQANIELQKTALAQAQS 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 124 EAQRGERLRSNNAISAEladsrstSAQEAKAGVAAIQAQLDLAR--------------------------------LNLS 171
Cdd:PRK15136 142 DLNRRVPLGNANLIGRE-------ELQHARDAVASAQAQLDVAIqqynanqamilntpledqpavqqaatevrnawLALQ 214

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 516296625 172 FTRVTAPIAGRVSRAEITAGNIVTADvTALTSVVSTDKVYAyfDADervfLKYTELA--RKGQ 232
Cdd:PRK15136 215 RTKIVSPMTGYVSRRSVQVGAQISPT-TPLMAVVPATNLWV--DAN----FKETQLAnmRIGQ 270
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 262-358 9.01e-05

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 44.47  E-value: 9.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625 262 VNPRTGTIRGRAVFDNADGSFTPGLYARLKLvGSGTYSAVLINDEAVgTDLGK-KFVLVMDKDNKPAYRAVELGPKIEGL 340
Cdd:PRK09783 289 VDAATRTLQLRLEVDNADEALKPGMNAWLQL-NTASEPMLLIPSQAL-IDTGSeQRVITVDADGRFVPKRVAVFQESQGV 366

                         90
                 ....*....|....*...
gi 516296625 341 RIVRNGLAKDDTIVVKGL 358
Cdd:PRK09783 367 TAIRSGLAEGEKVVSSGL 384
heterocyst_DevB TIGR02971
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ...
 104-212 2.00e-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: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516296625  104 VRRLEAQLQQARAvasrSDSEAQRGERlrsnNAISAELADSRSTSAQEAKAGVAAIQAQLDLARLNLSFTRVTAPIAGRV 183
Cdd:TIGR02971 144 LRTAEEELEEALA----SRSEQIDGAR----AALASLAEEVRETDVDLAQAEVKSALEAVQQAEALLELTYVKAPIDGRV 215

                          90       100
                  ....*....|....*....|....*....
gi 516296625  184 SRAEITAGNIVtaDVTALTSVVSTDKVYA 212
Cdd:TIGR02971 216 LKIHAREGEVI--GSEGILEMGDTSQMYA 242
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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