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Conserved domains on  [gi|516616581|ref|WP_017991424|]
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MULTISPECIES: efflux RND transporter periplasmic adaptor subunit [Rhizobium]

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

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 ...
38-357 1.02e-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: 239.07  E-value: 1.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  38 AKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQL 117
Cdd:COG0845    3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 118 AYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQVVFTL 197
Cdd:COG0845   83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 198 AHDGDRDAVFEVVESAFLRPIDGDG-TVALLSNPSQKIAAKVREISPTIDSSTGTIKVKVAI-SSDAAIPLGAPVVGRFN 275
Cdd:COG0845  163 ADLDPLEVEFDVPESDLARLKVGQPvTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELpNPDGLLRPGMFVRVRIV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 276 Y-VSQDVIQLPWSAMTSKDGKPAVWIVDpASSAVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPGEIVSYVKE 354
Cdd:COG0845  243 LgERENALLVPASAVVRDGGGAYVFVVD-ADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVEA 321

                 ...
gi 516616581 355 ASK 357
Cdd:COG0845  322 AAP 324
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
38-357 1.02e-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: 239.07  E-value: 1.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  38 AKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQL 117
Cdd:COG0845    3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 118 AYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQVVFTL 197
Cdd:COG0845   83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 198 AHDGDRDAVFEVVESAFLRPIDGDG-TVALLSNPSQKIAAKVREISPTIDSSTGTIKVKVAI-SSDAAIPLGAPVVGRFN 275
Cdd:COG0845  163 ADLDPLEVEFDVPESDLARLKVGQPvTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELpNPDGLLRPGMFVRVRIV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 276 Y-VSQDVIQLPWSAMTSKDGKPAVWIVDpASSAVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPGEIVSYVKE 354
Cdd:COG0845  243 LgERENALLVPASAVVRDGGGAYVFVVD-ADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVEA 321

                 ...
gi 516616581 355 ASK 357
Cdd:COG0845  322 AAP 324
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
33-350 9.22e-61

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: 197.92  E-value: 9.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   33 VGVVVAKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQ 112
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  113 TQAQLAYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQ 192
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  193 VVFTLAHDGDRDAVFEVVESAFLRPIDGDG-TVALLSNPSQKIAAKVREISPTIDSSTGTIKVKVAISS-DAAIPLGAPV 270
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTlTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNpDGRLLPGMFG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  271 VGRFNYVSQ-DVIQLPWSAMTSKDGKPAVWIVDPASSaVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPGEIV 349
Cdd:TIGR01730 241 RVTISLKVRsSAIVVPTQAVIEDLNGKYVYVVKNDGK-VSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKV 319

                  .
gi 516616581  350 S 350
Cdd:TIGR01730 320 K 320
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
40-192 1.91e-22

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: 95.95  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   40 PEPLVQGGAVTGEVRA-RVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQLA 118
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516616581  119 YDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQ 192
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQ 154
PRK09859 PRK09859
multidrug transporter subunit MdtE;
2-346 1.32e-21

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 94.78  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   2 RTILVATAIVCAVGLGSCSDErgPTEPTAR---QVGVVVAKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQ 78
Cdd:PRK09859   4 RRKLLIPLLFCGAMLTACDDK--SAENAAAmtpEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  79 SVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLE 158
Cdd:PRK09859  82 KVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 159 TAQDTLSYTELKADADGMITARNAEVGQVAQAAQVVfTLAHDGDRDAVF--------------EVVESAFLRPIDGDGTV 224
Cdd:PRK09859 162 QATINLQYANVTSPITGVSGKSSVTVGALVTANQAD-SLVTVQRLDPIYvdltqsvqdflrmkEEVASGQIKQVQGSTPV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 225 AL-LSNPSQKIAAKVREIS-PTIDSSTGTIKVKVAI-SSDAAIPLGAPVVGRFNYVS-QDVIQLPWSAMT-SKDGKPAVW 299
Cdd:PRK09859 241 QLnLENGKRYSQTGTLKFSdPTVDETTGSVTLRAIFpNPNGDLLPGMYVTALVDEGSrQNVLLVPQEGVThNAQGKATAL 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 516616581 300 IVDpASSAVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPG 346
Cdd:PRK09859 321 ILD-KDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
38-357 1.02e-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: 239.07  E-value: 1.02e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  38 AKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQL 117
Cdd:COG0845    3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 118 AYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQVVFTL 197
Cdd:COG0845   83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 198 AHDGDRDAVFEVVESAFLRPIDGDG-TVALLSNPSQKIAAKVREISPTIDSSTGTIKVKVAI-SSDAAIPLGAPVVGRFN 275
Cdd:COG0845  163 ADLDPLEVEFDVPESDLARLKVGQPvTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELpNPDGLLRPGMFVRVRIV 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 276 Y-VSQDVIQLPWSAMTSKDGKPAVWIVDpASSAVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPGEIVSYVKE 354
Cdd:COG0845  243 LgERENALLVPASAVVRDGGGAYVFVVD-ADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVEA 321

                 ...
gi 516616581 355 ASK 357
Cdd:COG0845  322 AAP 324
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
33-350 9.22e-61

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: 197.92  E-value: 9.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   33 VGVVVAKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQ 112
Cdd:TIGR01730   1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  113 TQAQLAYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQ 192
Cdd:TIGR01730  81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  193 VVFTLAHDGDRDAVFEVVESAFLRPIDGDG-TVALLSNPSQKIAAKVREISPTIDSSTGTIKVKVAISS-DAAIPLGAPV 270
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTlTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNpDGRLLPGMFG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  271 VGRFNYVSQ-DVIQLPWSAMTSKDGKPAVWIVDPASSaVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPGEIV 349
Cdd:TIGR01730 241 RVTISLKVRsSAIVVPTQAVIEDLNGKYVYVVKNDGK-VSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKV 319

                  .
gi 516616581  350 S 350
Cdd:TIGR01730 320 K 320
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
49-275 8.86e-33

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 124.78  E-value: 8.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  49 VTGEVRARVQTdLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQ---------------QT 113
Cdd:COG1566   37 ADGRVEARVVT-VAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQlarleaelgaeaeiaAA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 114 QAQLA------------YDRQQSLFRTQVTTRAALDQAQEALLTAQAS---------------------------TKSAQ 154
Cdd:COG1566  116 EAQLAaaqaqldlaqreLERYQALYKKGAVSQQELDEARAALDAAQAQleaaqaqlaqaqaglreeeelaaaqaqVAQAE 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 155 ALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQVVFTLAHDGDRDAVFEVVES--AFLRPidGD-GTVALLSNPS 231
Cdd:COG1566  196 AALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETdlGRVKP--GQpVEVRVDAYPD 273
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 516616581 232 QKIAAKVREISPTIDSSTG----------TIKVKVAISSDAAIPL--GAPVVGRFN 275
Cdd:COG1566  274 RVFEGKVTSISPGAGFTSPpknatgnvvqRYPVRIRLDNPDPEPLrpGMSATVEID 329
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
40-192 1.91e-22

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: 95.95  E-value: 1.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   40 PEPLVQGGAVTGEVRA-RVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQLA 118
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516616581  119 YDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQ 192
Cdd:pfam00529  81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQ 154
PRK09859 PRK09859
multidrug transporter subunit MdtE;
2-346 1.32e-21

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 94.78  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   2 RTILVATAIVCAVGLGSCSDErgPTEPTAR---QVGVVVAKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQ 78
Cdd:PRK09859   4 RRKLLIPLLFCGAMLTACDDK--SAENAAAmtpEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  79 SVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLE 158
Cdd:PRK09859  82 KVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 159 TAQDTLSYTELKADADGMITARNAEVGQVAQAAQVVfTLAHDGDRDAVF--------------EVVESAFLRPIDGDGTV 224
Cdd:PRK09859 162 QATINLQYANVTSPITGVSGKSSVTVGALVTANQAD-SLVTVQRLDPIYvdltqsvqdflrmkEEVASGQIKQVQGSTPV 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 225 AL-LSNPSQKIAAKVREIS-PTIDSSTGTIKVKVAI-SSDAAIPLGAPVVGRFNYVS-QDVIQLPWSAMT-SKDGKPAVW 299
Cdd:PRK09859 241 QLnLENGKRYSQTGTLKFSdPTVDETTGSVTLRAIFpNPNGDLLPGMYVTALVDEGSrQNVLLVPQEGVThNAQGKATAL 320
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 516616581 300 IVDpASSAVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPG 346
Cdd:PRK09859 321 ILD-KDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
2-244 9.57e-21

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 92.14  E-value: 9.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   2 RTILVATAIVCAVGLGSCSDERGPtEPTARQVGVVvakPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVK 81
Cdd:PRK11578   9 KRYLIALVIVLAGGITLWRILNAP-VPTYQTLIVR---PGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  82 AGQLLARIDPE-------EQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLFRTQVTTRAALDQAQEALL-------TAQ 147
Cdd:PRK11578  85 KDQLLGVIDPEqaenqikEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAvkqaqigTID 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 148 ASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQV---AQAAQVVFTLAHDGDRDAVFEVVES--AFLRPiDGDG 222
Cdd:PRK11578 165 AQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTviaAQQAPNILTLADMSTMLVKAQVSEAdvIHLKP-GQKA 243
                        250       260
                 ....*....|....*....|..
gi 516616581 223 TVALLSNPSQKIAAKVREISPT 244
Cdd:PRK11578 244 WFTVLGDPLTRYEGVLKDILPT 265
PRK03598 PRK03598
putative efflux pump membrane fusion protein; Provisional
58-198 8.01e-20

putative efflux pump membrane fusion protein; Provisional


Pssm-ID: 235136 [Multi-domain]  Cd Length: 331  Bit Score: 88.87  E-value: 8.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  58 QTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPE-------EQKAELDVAAANLQ-------------------SAEAQ 111
Cdd:PRK03598  43 TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAApyenalmQAKANVSVAQAQLDlmlagyrdeeiaqaraavkQAQAA 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 112 QTQAQLAYDRQQSLFRTQVTTRAALDQ--------------AQEAL------------LTAQASTKSAQALLETAQDTLS 165
Cdd:PRK03598 123 YDYAQNFYNRQQGLWKSRTISANDLENarssrdqaqatlksAQDKLsqyregnrpqdiAQAKASLAQAQAALAQAELNLQ 202
                        170       180       190
                 ....*....|....*....|....*....|...
gi 516616581 166 YTELKADADGMITARNAEVGQVAQAAQVVFTLA 198
Cdd:PRK03598 203 DTELIAPSDGTILTRAVEPGTMLNAGSTVFTLS 235
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
32-346 8.67e-20

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 89.77  E-value: 8.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  32 QVGVVVAKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQ 111
Cdd:PRK15030  39 AVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 112 QTQAQLAYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAA 191
Cdd:PRK15030 119 ANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNG 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 192 QVVfTLAHDGDRDAVF-EVVESA--FLR-----------PIDGDGTVALLSNPSQKI-AAKVREISP-TIDSSTGTIKVK 255
Cdd:PRK15030 199 QAT-ALATVQQLDPIYvDVTQSSndFLRlkqelangtlkQENGKAKVSLITSDGIKFpQDGTLEFSDvTVDQTTGSITLR 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 256 VAI-SSDAAIPLGAPVVGRFNY-VSQDVIQLPWSAMTSKDGKPAVWIVDPASSAVSARAVDVSGYETGSFIVKSGVSEGE 333
Cdd:PRK15030 278 AIFpNPDHTLLPGMFVRARLEEgLNPNAILVPQQGVTRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGD 357
                        330
                 ....*....|...
gi 516616581 334 VVVADGTKFLRPG 346
Cdd:PRK15030 358 RVVISGLQKVRPG 370
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
5-356 1.33e-18

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 86.00  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   5 LVATAIVCAVGLGSCSDERGPTEPTA-RQVGVVVAKPEPLVQGGAVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVKAG 83
Cdd:PRK09578   9 LLLAALVALFVLAGCGKGDSDAAAAApREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  84 QLLARIDPEEQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDT 163
Cdd:PRK09578  89 AVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQLQ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 164 LSYTELKADADGMitARNAEVGQ---VAQAAQVVFTLAHD------------GDRDAVFEVVESAFLRPI-DGDGTVALL 227
Cdd:PRK09578 169 LDYATVTAPIDGR--ARRALVTEgalVGQDQATPLTTVEQldpiyvnfsqpaADVEALRRAVKSGRATGIaQQDVAVTLV 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 228 SNPSQKIAAKVREI--SPTIDSSTGTIKVKVAISS-DAAIPLGAPVVGRFNY-VSQDVIQLPWSAMTSKDGKPAVWIVDP 303
Cdd:PRK09578 247 RADGSEYPLKGKLLfsDLAVDPTTDTVAMRALFPNpERELLPGAYVRIALDRaVNPRAILVPRDALLRTADSASVKVVGQ 326
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 516616581 304 ASSaVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPGEIVSYVKEAS 356
Cdd:PRK09578 327 NGK-VRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAVERAP 378
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
51-352 3.69e-18

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 84.84  E-value: 3.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  51 GEVRARVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLFRTQV 130
Cdd:PRK11556  80 GTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 131 TTRAALDqAQEALLT-AQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQVAQAAQ----VVFTLAHdgDRDA 205
Cdd:PRK11556 160 VSRQELD-AQQALVSeTEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDttgiVVITQTH--PIDL 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 206 VFEVVESAFLRPIDGDGTVALLS------NPSQKIAA-KVREISPTIDSSTGTIKVKVAISS--DAAIPlgAPVVGRFNY 276
Cdd:PRK11556 237 VFTLPESDIATVVQAQKAGKPLVveawdrTNSKKLSEgTLLSLDNQIDATTGTIKLKARFNNqdDALFP--NQFVNARML 314
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516616581 277 VS--QDVIQLPWSAMTSKDGKPAVWIVDpASSAVSARAVDVSGYETGSFIVKSGVSEGEVVVADGTKFLRPGEIVSYV 352
Cdd:PRK11556 315 VDtlQNAVVIPTAALQMGNEGHFVWVLN-DENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVV 391
PRK10476 PRK10476
multidrug transporter subunit MdtN;
65-273 8.24e-13

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 68.51  E-value: 8.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  65 VSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQ-------------------------QTQAQLA- 118
Cdd:PRK10476  55 VGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQimttqrsvdaersnaasaneqveraRANAKLAt 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 119 -------------YDRQQSLFRTQVTTRAALDQAQEALLTAQAST-------------KSAQALLETAQDTLSYTELKAD 172
Cdd:PRK10476 135 rtlerlepllakgYVSAQQVDQARTAQRDAEVSLNQALLQAQAAAaavggvdalvaqrAAREAALAIAELHLEDTTVRAP 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 173 ADGMITARNAEVGQVAQAAQVVFTLAHDGDRDAVfevvesAFLRPID------GD-GTVALLSNPSQKIAAKVREISPTI 245
Cdd:PRK10476 215 FDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAI------ANFRETDlknirvGDcATVYSMIDRGRPFEGKVDSIGWGV 288
                        250       260
                 ....*....|....*....|....*...
gi 516616581 246 DSSTGTIkvkvaissdaaIPLGAPVVGR 273
Cdd:PRK10476 289 LPDDGGN-----------VPRGLPYVPR 305
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
55-259 4.12e-11

Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.


Pssm-ID: 435440 [Multi-domain]  Cd Length: 214  Bit Score: 61.75  E-value: 4.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   55 ARVQTdlsfRVSGKIvERL--VEVGQSVKAGQLLARID-PEEQKAELD-VAAANLQSAEAQQTQAQLAYDRQQSLfrtqv 130
Cdd:pfam16576  20 AHVHA----RVEGWI-EKLyvNATGDPVKKGQPLAELYsPELVAAQQEyLLALRSGDALSKSELLRAARQRLRLL----- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  131 ttraaldQAQEALLTAQASTKSAQalletaqdtlSYTELKADADGMITARNAEVGQVAQAAQVVFTLAhdgDRDAV---F 207
Cdd:pfam16576  90 -------GMPEAQIAELERTGKVQ----------PTVTVYAPISGVVTELNVREGMYVQPGDTLFTIA---DLSTVwveA 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 516616581  208 EVVES--AFLRPidGD-GTVALLSNPSQKIAAKVREISPTIDSSTGTIKVKVAIS 259
Cdd:pfam16576 150 DVPEQdlALVKV--GQpAEVTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELP 202
PRK10559 PRK10559
p-hydroxybenzoic acid efflux pump subunit AaeA;
65-186 7.44e-09

p-hydroxybenzoic acid efflux pump subunit AaeA;


Pssm-ID: 182548 [Multi-domain]  Cd Length: 310  Bit Score: 56.29  E-value: 7.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  65 VSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLfRTQVTTRAALDQAQEALL 144
Cdd:PRK10559  54 VSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRL-GVQAMSREEIDQANNVLQ 132
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 516616581 145 TAQASTKSAQALLETAQDTLSYTELKADADGMITARNAEVGQ 186
Cdd:PRK10559 133 TVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGE 174
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
168-269 1.67e-08

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: 51.59  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  168 ELKADADGMITARNAEVGQVAQAAQVVFTLAHDGDRDAVFEV--VESAFLRPiDGDGTVALLSNPSQKIAAKVREISPTI 245
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVpaADLGSLKK-GQKVTLKLDPGSDYTLEGKVVRISPTV 79
                          90       100
                  ....*....|....*....|....
gi 516616581  246 DSSTGTIKVKVAISSDAAIPLGAP 269
Cdd:pfam13437  80 DPDTGVIPVRVSIENPKTPIPLLP 103
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
61-106 8.97e-08

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 48.21  E-value: 8.97e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 516616581   61 LSFRVSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQ 106
Cdd:pfam13533   5 IASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
92-174 6.31e-06

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 47.41  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   92 EEQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLFRTQVTTRA-----ALDQAQEALLTAQASTKSAQALLETAQDTLSy 166
Cdd:TIGR04320 264 ATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELAnaqaqALQTAQNNLATAQAALANAEARLAKAKEALA- 342

                  ....*...
gi 516616581  167 tELKADAD 174
Cdd:TIGR04320 343 -NLNADLA 349
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
92-192 7.40e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 7.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  92 EEQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLFRTQVTTRAALDQAQEALLTAQASTKSAQALLETAQDTLsyTELKA 171
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL--LERLE 417
                         90       100
                 ....*....|....*....|.
gi 516616581 172 DADGMITARNAEVGQVAQAAQ 192
Cdd:COG1196  418 RLEEELEELEEALAELEEEEE 438
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
71-203 2.24e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581   71 ERLVEVG-QSVKAGQLLARIDP-EEQKAELDVAAANLQSAEAQQTQAQLAYDRQQSLFRTQVTTRAALDQAQEALLTAQa 148
Cdd:COG4913   651 QRLAEYSwDEIDVASAEREIAElEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL- 729
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 516616581  149 stKSAQALLETAQDtLSYTELKADADgmitARNAEVGQVAQAAQVVFTLAHDGDR 203
Cdd:COG4913   730 --DELQDRLEAAED-LARLELRALLE----ERFAAALGDAVERELRENLEERIDA 777
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
169-339 2.31e-03

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 39.47  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 169 LKADADGMITARNAEVGQVAQAAQVVftlAHDGDRDAVF---EVVES-AFLRPIDGDGTVALLSNPSQKIAAKVREISPT 244
Cdd:PRK09783 212 LKAPIDGVITAFDLRAGMNIAKDNVV---AKIQGMDPVWvtaAIPESiAWLVKDASQFTLTVPARPDKTFTIRKWTLLPS 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581 245 IDSSTGTIKVKVAISS-DAAIPLGAPVVGRFNYVSQDVIQLPWSAMTSKDGKPAVWIVDPASSAVSARaVDVSGYETGSF 323
Cdd:PRK09783 289 VDAATRTLQLRLEVDNaDEALKPGMNAWLQLNTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKR-VAVFQESQGVT 367
                        170
                 ....*....|....*.
gi 516616581 324 IVKSGVSEGEVVVADG 339
Cdd:PRK09783 368 AIRSGLAEGEKVVSSG 383
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
94-165 2.47e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 39.32  E-value: 2.47e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516616581   94 QKAELDVAAANLQSAEAQQTQAQLAYDRQQslfrtqvttrAALDQAQEALLTAQASTKSAQALLETAQDTLS 165
Cdd:TIGR04320 245 DKTPIPNPPNSLAALQAKLATAQADLAAAQ----------TALNTAQAALTSAQTAYAAAQAALATAQKELA 306
PRK09282 PRK09282
pyruvate carboxylase subunit B; Validated
15-102 3.99e-03

pyruvate carboxylase subunit B; Validated


Pssm-ID: 236449 [Multi-domain]  Cd Length: 592  Bit Score: 39.06  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  15 GLGSCSDERGPTEPTARQVGVVVAKPEPLVqggaVTGEVRARVQTDLSFRVSGKIVERLVEVGQSVKAGQLLARIdpEEQ 94
Cdd:PRK09282 483 GVKAEGKRPFYLRVDGMPEEVVVEPLKEIV----VGGRPRASAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVL--EAM 556

                 ....*...
gi 516616581  95 KAELDVAA 102
Cdd:PRK09282 557 KMENEIQA 564
PTS_EIIA_1 pfam00358
phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1;
67-97 4.07e-03

phosphoenolpyruvate-dependent sugar phosphotransferase system, EIIA 1;


Pssm-ID: 459779 [Multi-domain]  Cd Length: 121  Bit Score: 36.59  E-value: 4.07e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 516616581   67 GKIVERLVEVGQSVKAGQLLARIDPEEQKAE 97
Cdd:pfam00358  81 GEGFESLVKEGDKVKAGDLLLEFDLEAIKAA 111
PRK05704 PRK05704
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
32-118 6.40e-03

2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;


Pssm-ID: 235571 [Multi-domain]  Cd Length: 407  Bit Score: 38.28  E-value: 6.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516616581  32 QVGVVVAKPEPLV--QGGAVTGEVRARVqtdlsfrvSGKIVERLVEVGQSVKAGQLLARIDPEEQKAELDVAAANLQSAE 109
Cdd:PRK05704  25 KPGDAVKRDEVLVeiETDKVVLEVPAPA--------AGVLSEILAEEGDTVTVGQVLGRIDEGAAAGAAAAAAAAAAAAA 96

                 ....*....
gi 516616581 110 AQQTQAQLA 118
Cdd:PRK05704  97 AAPAQAQAA 105
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
65-113 7.06e-03

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: 35.80  E-value: 7.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 516616581   65 VSGKIVERLVEVGQSVKAGQLLARI-DPEEQKAELDVAAANLQSAEAQQT 113
Cdd:pfam13437   6 VDGVVAELNVEEGQVVQAGDPLATIvPPDRLLVEAFVPAADLGSLKKGQK 55
 
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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