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Conserved domains on  [gi|2544989011|ref|WP_300736553|]
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efflux RND transporter periplasmic adaptor subunit [uncultured Alistipes sp.]

Protein Classification

RND family efflux transporter( domain architecture ID 1000811)

RND (Resistance, Nodulation, and cell Division) family efflux transporter which may function in nodulation, acriflavin resistance, heavy metal efflux, or multidrug resistance

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 ...
 39-338 7.34e-78

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


:

Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 241.39  E-value: 7.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  39 AEETTVRLTEEFTSEIEPYRENDITPAASGVhIDRILVDVGDVVREGQLLVTLDPTQYTQQLVQ-----------LKTVE 107
Cdd:COG0845     3 VERGDVPETVEATGTVEARREVEVRARVSGR-VEEVLVDEGDRVKKGQVLARLDPPDLQAALAQaqaqlaaaqaqLELAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 108 DDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNIE----------VRSPISGVVTARNYESGDLFSQ-QPVLH 176
Cdd:COG0845    82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEqaranlayttIRAPFDGVVGERNVEPGQLVSAgTPLFT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 177 VMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIF 256
Cdd:COG0845   162 IADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRI 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 257 DMGS-KQGVMVPDVAVQKQVGSAerYLYVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDGAPVEVK 335
Cdd:COG0845   242 VLGErENALLVPASAVVRDGGGA--YVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVV 319


                  ...
gi 2544989011 336 QEQ 338
Cdd:COG0845   320 EAA 322
DUF1425 super family cl12345
Putative periplasmic lipoprotein; This bacterial family of proteins contains members described ...
 1-52 6.57e-03

Putative periplasmic lipoprotein; This bacterial family of proteins contains members described as putative lipoproteins, some are also known as YcfL. The function of this family is unknown. Family members have also been annotated as predicted periplasmic lipoproteins (COG5633), and appear to contain an N-terminal membrane lipoprotein lipid attachment side (pfam08139), which is not included in this alignment model.


The actual alignment was detected with superfamily member COG5633:

Pssm-ID: 472303  Cd Length: 128  Bit Score: 36.12  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2544989011   1 MKKIVMLAAWAVLLSGCGGRKSATDAA-------VDPRVLTRGTVAEETTVRLTEEFTS 52
Cdd:COG5633     1 MKKLLIALLAVLLLAGCSSSPTSGIPVnsqqplvMESSVLAAGISAEKPTLSQVGGLLR 59
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 39-338 7.34e-78

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 241.39  E-value: 7.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  39 AEETTVRLTEEFTSEIEPYRENDITPAASGVhIDRILVDVGDVVREGQLLVTLDPTQYTQQLVQ-----------LKTVE 107
Cdd:COG0845     3 VERGDVPETVEATGTVEARREVEVRARVSGR-VEEVLVDEGDRVKKGQVLARLDPPDLQAALAQaqaqlaaaqaqLELAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 108 DDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNIE----------VRSPISGVVTARNYESGDLFSQ-QPVLH 176
Cdd:COG0845    82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEqaranlayttIRAPFDGVVGERNVEPGQLVSAgTPLFT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 177 VMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIF 256
Cdd:COG0845   162 IADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRI 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 257 DMGS-KQGVMVPDVAVQKQVGSAerYLYVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDGAPVEVK 335
Cdd:COG0845   242 VLGErENALLVPASAVVRDGGGA--YVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVV 319


                  ...
gi 2544989011 336 QEQ 338
Cdd:COG0845   320 EAA 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 39-334 5.71e-60

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: 195.23  E-value: 5.71e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  39 AEETTVRLTEEFTSEIEPYRENDITPAASGVhIDRILVDVGDVVREGQLLVTLDPT----QYTQQLVQLKTVE------- 107
Cdd:TIGR01730   6 VESETLANTLTFPGSLEAVDEADLAAEVAGK-ITKISVREGQKVKKGQVLARLDDDdyqlALQAALAQLAAAEaqlelaq 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 108 DDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNI----------EVRSPISGVVTARNYESGDLFS-QQPVLH 176
Cdd:TIGR01730  85 RSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLasaqlnlrytEIRAPFDGTIGRRLVEVGAYVTaGQTLAT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 177 VMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIF 256
Cdd:TIGR01730 165 IVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFGRVTI 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544989011 257 DMGSKQGVM-VPDVAVQKqvGSAERYLYVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDGAPVEV 334
Cdd:TIGR01730 245 SLKVRSSAIvVPTQAVIE--DLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKVKV 321
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 58-252 1.80e-32

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: 120.30  E-value: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  58 RENDITPAASGvHIDRILVD-VGDVVREGQLLVTLdptqYTQQLVQLktvEDDYnrlLPVYEVGGISAQQ--IEQAKAQL 134
Cdd:pfam16576  18 RLAHVHARVEG-WIEKLYVNaTGDPVKKGQPLAEL----YSPELVAA---QQEY---LLALRSGDALSKSelLRAARQRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 135 ---DIQREVVANMKK------NIEVRSPISGVVTARNYESGDLFS-QQPVLHVMQIDLLKVIVNISEQFFPNVKVGMPVT 204
Cdd:pfam16576  87 rllGMPEAQIAELERtgkvqpTVTVYAPISGVVTELNVREGMYVQpGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAE 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2544989011 205 LRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYA 252
Cdd:pfam16576 167 VTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
PRK09859 PRK09859
multidrug transporter subunit MdtE;
1-329 1.22e-24

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 102.87  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011   1 MKKIVMLAAWAVLLSGCGGRKSATDAAVDPRVltrGTVA-EETTVRLTEEFTSEIEPYRENDITPAASGVHIDRILVDvG 79
Cdd:PRK09859    5 RKLLIPLLFCGAMLTACDDKSAENAAAMTPEV---GVVTlSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIE-G 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  80 DVVREGQLLVTLDPTQYTQQLVQLK-----------TVEDDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNI 148
Cdd:PRK09859   81 DKVNQGDSLYQIDPAPLQAELNSAKgslakalstasNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 149 E----------VRSPISGVVTARNYESGDLFS---QQPVLHVMQIDLLKVIVNISEQFF------------PNVKVGMPV 203
Cdd:PRK09859  161 EqatinlqyanVTSPITGVSGKSSVTVGALVTanqADSLVTVQRLDPIYVDLTQSVQDFlrmkeevasgqiKQVQGSTPV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 204 TLRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIFDMGSKQGV-MVPDVAVQKQVGSAERYL 282
Cdd:PRK09859  241 QLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVlLVPQEGVTHNAQGKATAL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2544989011 283 yVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDG 329
Cdd:PRK09859  321 -ILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
YcfL COG5633
Uncharacterized conserved protein YcfL [Function unknown];
1-52 6.57e-03

Uncharacterized conserved protein YcfL [Function unknown];


Pssm-ID: 444360  Cd Length: 128  Bit Score: 36.12  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2544989011   1 MKKIVMLAAWAVLLSGCGGRKSATDAA-------VDPRVLTRGTVAEETTVRLTEEFTS 52
Cdd:COG5633     1 MKKLLIALLAVLLLAGCSSSPTSGIPVnsqqplvMESSVLAAGISAEKPTLSQVGGLLR 59
 
Name Accession Description Interval E-value
AcrA COG0845
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ...
 39-338 7.34e-78

Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];


Pssm-ID: 440606 [Multi-domain]  Cd Length: 324  Bit Score: 241.39  E-value: 7.34e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  39 AEETTVRLTEEFTSEIEPYRENDITPAASGVhIDRILVDVGDVVREGQLLVTLDPTQYTQQLVQ-----------LKTVE 107
Cdd:COG0845     3 VERGDVPETVEATGTVEARREVEVRARVSGR-VEEVLVDEGDRVKKGQVLARLDPPDLQAALAQaqaqlaaaqaqLELAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 108 DDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNIE----------VRSPISGVVTARNYESGDLFSQ-QPVLH 176
Cdd:COG0845    82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEqaranlayttIRAPFDGVVGERNVEPGQLVSAgTPLFT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 177 VMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIF 256
Cdd:COG0845   162 IADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRI 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 257 DMGS-KQGVMVPDVAVQKQVGSAerYLYVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDGAPVEVK 335
Cdd:COG0845   242 VLGErENALLVPASAVVRDGGGA--YVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVV 319


                  ...
gi 2544989011 336 QEQ 338
Cdd:COG0845   320 EAA 322
RND_mfp TIGR01730
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ...
 39-334 5.71e-60

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: 195.23  E-value: 5.71e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  39 AEETTVRLTEEFTSEIEPYRENDITPAASGVhIDRILVDVGDVVREGQLLVTLDPT----QYTQQLVQLKTVE------- 107
Cdd:TIGR01730   6 VESETLANTLTFPGSLEAVDEADLAAEVAGK-ITKISVREGQKVKKGQVLARLDDDdyqlALQAALAQLAAAEaqlelaq 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 108 DDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNI----------EVRSPISGVVTARNYESGDLFS-QQPVLH 176
Cdd:TIGR01730  85 RSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLasaqlnlrytEIRAPFDGTIGRRLVEVGAYVTaGQTLAT 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 177 VMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIF 256
Cdd:TIGR01730 165 IVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFGRVTI 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544989011 257 DMGSKQGVM-VPDVAVQKqvGSAERYLYVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDGAPVEV 334
Cdd:TIGR01730 245 SLKVRSSAIvVPTQAVIE--DLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAKVKV 321
HlyD_D23 pfam16576
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ...
 58-252 1.80e-32

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: 120.30  E-value: 1.80e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  58 RENDITPAASGvHIDRILVD-VGDVVREGQLLVTLdptqYTQQLVQLktvEDDYnrlLPVYEVGGISAQQ--IEQAKAQL 134
Cdd:pfam16576  18 RLAHVHARVEG-WIEKLYVNaTGDPVKKGQPLAEL----YSPELVAA---QQEY---LLALRSGDALSKSelLRAARQRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 135 ---DIQREVVANMKK------NIEVRSPISGVVTARNYESGDLFS-QQPVLHVMQIDLLKVIVNISEQFFPNVKVGMPVT 204
Cdd:pfam16576  87 rllGMPEAQIAELERtgkvqpTVTVYAPISGVVTELNVREGMYVQpGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAE 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2544989011 205 LRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYA 252
Cdd:pfam16576 167 VTLPALPGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
58-259 3.24e-30

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 117.07  E-value: 3.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  58 RENDITPAASGVhIDRILVDVGDVVREGQLLVTLDPTQYTQQL------------------------------------- 100
Cdd:COG1566    44 RVVTVAAKVSGR-VTEVLVKEGDRVKKGQVLARLDPTDLQAALaqaeaqlaaaeaqlarleaelgaeaeiaaaeaqlaaa 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 101 -VQLKTVEDDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNIE------------------------------ 149
Cdd:COG1566   123 qAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAqaqaglreeeelaaaqaqvaqaeaalaqae 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 150 -------VRSPISGVVTARNYESGDLFSQ-QPVLHVMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPEREFTGRVSL 221
Cdd:COG1566   203 lnlarttIRAPVDGVVTNLNVEPGEVVSAgQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTS 282

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2544989011 222 IYPALDATT----------RTFKVEVEVPNGDG-TLRPGMYARTIFDMG 259
Cdd:COG1566   283 ISPGAGFTSppknatgnvvQRYPVRIRLDNPDPePLRPGMSATVEIDTE 331
PRK09859 PRK09859
multidrug transporter subunit MdtE;
1-329 1.22e-24

multidrug transporter subunit MdtE;


Pssm-ID: 137559 [Multi-domain]  Cd Length: 385  Bit Score: 102.87  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011   1 MKKIVMLAAWAVLLSGCGGRKSATDAAVDPRVltrGTVA-EETTVRLTEEFTSEIEPYRENDITPAASGVHIDRILVDvG 79
Cdd:PRK09859    5 RKLLIPLLFCGAMLTACDDKSAENAAAMTPEV---GVVTlSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIE-G 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  80 DVVREGQLLVTLDPTQYTQQLVQLK-----------TVEDDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNI 148
Cdd:PRK09859   81 DKVNQGDSLYQIDPAPLQAELNSAKgslakalstasNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 149 E----------VRSPISGVVTARNYESGDLFS---QQPVLHVMQIDLLKVIVNISEQFF------------PNVKVGMPV 203
Cdd:PRK09859  161 EqatinlqyanVTSPITGVSGKSSVTVGALVTanqADSLVTVQRLDPIYVDLTQSVQDFlrmkeevasgqiKQVQGSTPV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 204 TLRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIFDMGSKQGV-MVPDVAVQKQVGSAERYL 282
Cdd:PRK09859  241 QLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVlLVPQEGVTHNAQGKATAL 320

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 2544989011 283 yVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDG 329
Cdd:PRK09859  321 -ILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPG 366
PRK15030 PRK15030
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
4-336 4.30e-16

multidrug efflux RND transporter periplasmic adaptor subunit AcrA;


Pssm-ID: 184990 [Multi-domain]  Cd Length: 397  Bit Score: 78.60  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011   4 IVMLAAWAVLLSGCGGRKSATDAAVDPRVltrGTVAEETT-VRLTEEFTSEIEPYRENDITPAASGVHIDRILVDVGDVv 82
Cdd:PRK15030   12 VVLMLSGSLALTGCDDKQAQQGGQQMPAV---GVVTVKTEpLQITTELPGRTSAYRIAEVRPQVSGIILKRNFKEGSDI- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  83 REGQLLVTLDPTQYTQQLVQLK-----------TVEDDYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNIE-- 149
Cdd:PRK15030   88 EAGVSLYQIDPATYQATYDSAKgdlakaqaaanIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVEta 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 150 --------VRSPISGVVTARNYESGDLFSQ---QPVLHVMQIDLLKVIVNISEQFFPNVKVGMPV-TLRVE--------- 208
Cdd:PRK15030  168 rinlaytkVTSPISGRIGKSNVTEGALVQNgqaTALATVQQLDPIYVDVTQSSNDFLRLKQELANgTLKQEngkakvsli 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 209 -----IFPErefTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIFDMGSK-QGVMVPDVAVQKqVGSAERYL 282
Cdd:PRK15030  248 tsdgiKFPQ---DGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNpNAILVPQQGVTR-TPRGDATV 323

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2544989011 283 YVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDGAPVEVKQ 336
Cdd:PRK15030  324 LVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQE 377
PRK11556 PRK11556
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
79-334 2.71e-15

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


Pssm-ID: 183194 [Multi-domain]  Cd Length: 415  Bit Score: 76.37  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  79 GDVVREGQLLVTLDPTQYTQQLVQ-----------LKTVEDDYNRLLPVYEVGGISAQQIE-------QAKAQLDIQREV 140
Cdd:PRK11556  106 GQQVKAGDLLAEIDPRPFKVALAQaqgqlakdqatLANARRDLARYQQLAKTNLVSRQELDaqqalvsETEGTIKADEAS 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 141 VANMKKNIE---VRSPISGVVTARNYESGDLFSQ---QPVLHVMQIDLLKVIVNISEQFFPNV----KVGMPVTlrVEIF 210
Cdd:PRK11556  186 VASAQLQLDysrITAPISGRVGLKQVDVGNQISSgdtTGIVVITQTHPIDLVFTLPESDIATVvqaqKAGKPLV--VEAW 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 211 ----PEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMY--ARTIFDMgSKQGVMVPDVAVQkqVGSAERYLYV 284
Cdd:PRK11556  264 drtnSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFvnARMLVDT-LQNAVVIPTAALQ--MGNEGHFVWV 340

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2544989011 285 IVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDGAPVEV 334
Cdd:PRK11556  341 LNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEV 390
PRK09783 PRK09783
copper/silver efflux system membrane fusion protein CusB; Provisional
 62-323 1.94e-14

copper/silver efflux system membrane fusion protein CusB; Provisional


Pssm-ID: 236625 [Multi-domain]  Cd Length: 409  Bit Score: 73.75  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  62 ITPAASGVHIDRIL-VDVGDVVREGQLLVTLDPTQYtqqlvqlktVEDDYNRLLpVYEVGGiSAQQIEQAKAQL------ 134
Cdd:PRK09783  125 IVQARAAGFIDKVYpLTVGDKVQKGTPLLDLTIPDW---------VEAQSEYLL-LRETGG-TATQTEGILERLrlagmp 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 135 --DIQREVVA-NMKKNIEVRSPISGVVTARNYESGDLFSQQPVLHVMQ-IDLLKVIVNISEQFFPNVKVGMPVTLRVEIF 210
Cdd:PRK09783  194 eaDIRRLIATrKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKIQgMDPVWVTAAIPESIAWLVKDASQFTLTVPAR 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 211 PEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIFDMGSKQGVMVPDVAVQkqvgsaerylyvivgDSV 290
Cdd:PRK09783  274 PDKTFTIRKWTLLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQLNTASEPMLLIPSQALI---------------DTG 338

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2544989011 291 AERRSVEV---GRQVGDRVDILR----------GVQAGEQVAVTAL 323
Cdd:PRK09783  339 SEQRVITVdadGRFVPKRVAVFQesqgvtairsGLAEGEKVVSSGL 384
PRK11578 PRK11578
macrolide transporter subunit MacA; Provisional
 51-320 3.15e-12

macrolide transporter subunit MacA; Provisional


Pssm-ID: 183211 [Multi-domain]  Cd Length: 370  Bit Score: 66.72  E-value: 3.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  51 TSEIEPYRENDITPAASGvHIDRILVDVGDVVREGQLLVTLDPTQYTQQL------------------VQLKTVEDDYNR 112
Cdd:PRK11578   53 TGKLDALRKVDVGAQVSG-QLKTLSVAIGDKVKKDQLLGVIDPEQAENQIkeveatlmelraqrqqaeAELKLARVTLSR 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 113 LLPVYEVGGISAQQIEQAKAQLDIQREVVANMKKNI-----------------EVRSPISGVVTARNYESGD--LFSQQP 173
Cdd:PRK11578  132 QQRLAKTQAVSQQDLDTAATELAVKQAQIGTIDAQIkrnqasldtaktnldytRIVAPMAGEVTQITTLQGQtvIAAQQA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 174 --VLHVMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPEREFTGRVSLIYPALDATTRT--FKVEVEVPNGDGTLRPG 249
Cdd:PRK11578  212 pnILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAifYYARFEVPNPNGLLRLD 291

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544989011 250 MYART-IFDMGSKQGVMVPDVAVQKQVGSaERYLYVIVGDSVAERRSVEVGRQVGDRVDILRGVQAGEQVAV 320
Cdd:PRK11578  292 MTAQVhIQLTDVKNVLTIPLSALGDPVGD-NRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVII 362
HlyD_3 pfam13437
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ...
 149-249 4.94e-12

HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.


Pssm-ID: 433206 [Multi-domain]  Cd Length: 104  Bit Score: 61.61  E-value: 4.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 149 EVRSPISGVVTARNYESGDLFSQ-QPVLHVMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPEREFTGRVSLIYPALD 227
Cdd:pfam13437   1 TIRAPVDGVVAELNVEEGQVVQAgDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80

                          90       100
                  ....*....|....*....|....
gi 2544989011 228 ATTRTFKVEVEVPNGDG--TLRPG 249
Cdd:pfam13437  81 PDTGVIPVRVSIENPKTpiPLLPG 104
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 41-320 1.55e-11

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: 64.37  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  41 ETTVRLTEEFTSEIEPYREND-ITPAASGVhIDRILVDVGDVVREGQLLVTLDPTQYTQQLVQLK-----------TVED 108
Cdd:pfam00529   1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGI-VTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEaqlakaqaqvaRLQA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 109 DYNRLLPVYEVGGISAQQIEQAKAQLDIQREVVANMK----------KNIEVRSPISGVVTARNYESGDLFSQQ---PVL 175
Cdd:pfam00529  80 ELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQaqlaqaqidlARRRVLAPIGGISRESLVTAGALVAQAqanLLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 176 HVMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIFPERE-----------------FTGRVSLIYPALDATTRTFKVEVE 238
Cdd:pfam00529 160 TVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAelklakldlerteirapVDGTVAFLSVTVDGGTVSAGLRLM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 239 VPN-GDGTLRPGMYART-IFDMGSKQGVMVPDVAVQKQVGSaeRYLYVIVGDSVA-ERRSVEVGRQVGDRVDILRGVQAG 315
Cdd:pfam00529 240 FVVpEDNLLVPGMFVETqLDQVRVGQPVLIPFDAFPQTKTG--RFTGVVVGISPDtGPVRVVVDKAQGPYYPLRIGLSAG 317


                  ....*
gi 2544989011 316 EQVAV 320
Cdd:pfam00529 318 ALVRL 322
PRK09578 PRK09578
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
2-334 4.36e-07

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


Pssm-ID: 169982 [Multi-domain]  Cd Length: 385  Bit Score: 50.95  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011   2 KKIVMLAAWAVLLSGCGGRKSATDAAVDPRVLTrgTVAEETTVRLTEEFTSEIEPYRENDITPAASGVHIDRiLVDVGDV 81
Cdd:PRK09578    8 RLLLAALVALFVLAGCGKGDSDAAAAAPREATV--VTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTAR-TYEEGQE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  82 VREGQLLVTLDPTQYTQQLVQ----LKTVE-------------DDYNRLLPVYEVGGISAQQIE-QAKAQLDIQREVVAN 143
Cdd:PRK09578   85 VKQGAVLFRIDPAPLKAARDAaagaLAKAEaahlaaldkrrryDDLVRDRAVSERDYTEAVADErQAKAAVASAKAELAR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 144 MKKNIE---VRSPISGVVTARNYESGDLFSQQ---PVLHVMQIDllKVIVNIS------EQFFPNVKVG---------MP 202
Cdd:PRK09578  165 AQLQLDyatVTAPIDGRARRALVTEGALVGQDqatPLTTVEQLD--PIYVNFSqpaadvEALRRAVKSGratgiaqqdVA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 203 VTLRVEIFPEREFTGRVSLIYPALDATTRTFKVEVEVPNGDGTLRPGMYARTIFDMG-SKQGVMVPDVAVqkqVGSAERY 281
Cdd:PRK09578  243 VTLVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAvNPRAILVPRDAL---LRTADSA 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2544989011 282 LYVIVG-DSVAERRSVEVGRQVGDRVDILRGVQAGEQVAVTALSKLYDGAPVEV 334
Cdd:PRK09578  320 SVKVVGqNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKA 373
PRK15136 PRK15136
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
73-235 1.47e-04

multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;


Pssm-ID: 185090 [Multi-domain]  Cd Length: 390  Bit Score: 43.14  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011  73 RILVDVGDVVREGQLLVTLDPTQYTQQLVQLKT--------------------------------VEDDYNRLLPVYEVG 120
Cdd:PRK15136   74 KVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTalansvrqthqlminskqyqanielqktalaqAQSDLNRRVPLGNAN 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 121 GI-------SAQQIEQAKAQLDIQRE-------VVANMK---------------------KNIEVRSPISGVVTARNYES 165
Cdd:PRK15136  154 LIgreelqhARDAVASAQAQLDVAIQqynanqaMILNTPledqpavqqaatevrnawlalQRTKIVSPMTGYVSRRSVQV 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 166 G-DLFSQQPVLHVMQIDLLKVIVNISEQFFPNVKVGMPVTLRVEIF-PEREFTGRV-----------SLIyPALDATTRT 232
Cdd:PRK15136  234 GaQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVvgldmgtgsafSLL-PAQNATGNW 312


                  ...
gi 2544989011 233 FKV 235
Cdd:PRK15136  313 IKV 315
PRK10476 PRK10476
multidrug transporter subunit MdtN;
119-222 1.67e-03

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 40.01  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544989011 119 VGGISAQ--QIEQAKAQLDI-QREVvanmkKNIEVRSPISGVVTARNYESGD-LFSQQPVLHVMQIDLLKVIVNISEQFF 194
Cdd:PRK10476  182 VGGVDALvaQRAAREAALAIaELHL-----EDTTVRAPFDGRVVGLKVSVGEfAAPMQPIFTLIDTDHWYAIANFRETDL 256

                          90       100
                  ....*....|....*....|....*...
gi 2544989011 195 PNVKVGMPVTLRVEIFPEREFTGRVSLI 222
Cdd:PRK10476  257 KNIRVGDCATVYSMIDRGRPFEGKVDSI 284
YcfL COG5633
Uncharacterized conserved protein YcfL [Function unknown];
1-52 6.57e-03

Uncharacterized conserved protein YcfL [Function unknown];


Pssm-ID: 444360  Cd Length: 128  Bit Score: 36.12  E-value: 6.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2544989011   1 MKKIVMLAAWAVLLSGCGGRKSATDAA-------VDPRVLTRGTVAEETTVRLTEEFTS 52
Cdd:COG5633     1 MKKLLIALLAVLLLAGCSSSPTSGIPVnsqqplvMESSVLAAGISAEKPTLSQVGGLLR 59
Biotin_lipoyl_2 pfam13533
Biotin-lipoyl like;
62-104 7.02e-03

Biotin-lipoyl like;


Pssm-ID: 433286  Cd Length: 50  Bit Score: 34.34  E-value: 7.02e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2544989011  62 ITPAASGVhIDRILVDVGDVVREGQLLVTLDPTQYTQQLVQLK 104
Cdd:pfam13533   5 IASPVSGK-VVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAE 46
 
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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