|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
42-342 |
2.00e-79 |
|
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: 245.62 E-value: 2.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 42 VKARPVDQIQDYTATVEAEVKNNIAPSSPVRIDQIFVEVGDRVSKGQKLVQMDA-----------ANLKQTKLQLDNQEI 110
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPpdlqaalaqaqAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 111 EFNRIDELYKVGGASKSEWDASKMQLDVKKTAY----------KNLLENTSLQSPINGVVTARNYDNGDMYSGGEPVLVV 180
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALaaaqaaleqaRANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 181 EQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFARATLN 260
Cdd:COG0845 163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRIV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 261 FGTAENV-VVPDLAIVKQAGSgdRYVFVYK-DGKVSYNKVELGRRMGTEYELKSGVPDNSQVVVAGQSRLVNGMEVEVEA 338
Cdd:COG0845 243 LGERENAlLVPASAVVRDGGG--AYVFVVDaDGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVE 320
|
....
gi 490442507 339 SSQP 342
Cdd:COG0845 321 AAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
37-336 |
5.66e-63 |
|
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: 203.32 E-value: 5.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 37 VKLADVKARPVDQIQDYTATVEAEVKNNIAPSSPVRIDQIFVEVGDRVSKGQKLVQMDA-----------ANLKQTKLQL 105
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDddyqlalqaalAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 106 DNQEIEFNRIDELYKVGGASKSEWDASKMQLDVKKT----------AYKNLLENTSLQSPINGVVTARNYDNGDMYSGGE 175
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQAdleaakaslaSAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 176 PVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFA 255
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 256 RATLNFGTAEN-VVVPDLAIVkqAGSGDRYVFVYK-DGKVSYNKVELGRRMGTEYELKSGVPDNSQVVVAGQSRLVNGME 333
Cdd:TIGR01730 241 RVTISLKVRSSaIVVPTQAVI--EDLNGKYVYVVKnDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAK 318
|
...
gi 490442507 334 VEV 336
Cdd:TIGR01730 319 VKV 321
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
65-255 |
1.29e-27 |
|
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: 107.59 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 65 IAPSSPVRIDQIFV-EVGDRVSKGQKLVQMDAANLKQTKLQ----LDNQEIEfnRIDELYKvggASKSE---WDASKMQL 136
Cdd:pfam16576 22 VHARVEGWIEKLYVnATGDPVKKGQPLAELYSPELVAAQQEyllaLRSGDAL--SKSELLR---AARQRlrlLGMPEAQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 137 D-VKKTayKNLLENTSLQSPINGVVTARNYDNGDMYSGGEPVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGD 215
Cdd:pfam16576 97 AeLERT--GKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490442507 216 EVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFA 255
Cdd:pfam16576 175 KTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
1-344 |
4.76e-21 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 92.86 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 1 MKRSIQLVALLL--TVFMGSCtggKDKAAAEHVDAKPIVKLADVKARPVDQIQDYTA-TVEAEVKNNIAPSSPVRIDQIF 77
Cdd:PRK09859 1 MNRRRKLLIPLLfcGAMLTAC---DDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGrTVPYEVAEIRPQVGGIIIKRNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 78 VEvGDRVSKGQKLVQMDAA-----------NLKQTKLQLDNQEIEFNRIDELYKVGGASKSEWDASKMQLD-------VK 139
Cdd:PRK09859 78 IE-GDKVNQGDSLYQIDPAplqaelnsakgSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNeaeanvtVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 140 KTAYKNL---LENTSLQSPINGVVTARNYDNGDMYSG--GEPVLVVEQITPV------------KLLINVSETYFTKVKK 202
Cdd:PRK09859 157 KAAVEQAtinLQYANVTSPITGVSGKSSVTVGALVTAnqADSLVTVQRLDPIyvdltqsvqdflRMKEEVASGQIKQVQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 203 GTPVDVKLDVYGDEVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFARATLNFGTAENVV-VPDLAIVKQAGSG 281
Cdd:PRK09859 237 STPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLlVPQEGVTHNAQGK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490442507 282 DRYVFVYKDGKVSYNKVELGRRMGTEYELKSGVPDNSQVVVAGQSRLVNGMEVEVEASSQPSS 344
Cdd:PRK09859 317 ATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENA 379
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
42-342 |
2.00e-79 |
|
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: 245.62 E-value: 2.00e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 42 VKARPVDQIQDYTATVEAEVKNNIAPSSPVRIDQIFVEVGDRVSKGQKLVQMDA-----------ANLKQTKLQLDNQEI 110
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPpdlqaalaqaqAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 111 EFNRIDELYKVGGASKSEWDASKMQLDVKKTAY----------KNLLENTSLQSPINGVVTARNYDNGDMYSGGEPVLVV 180
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALaaaqaaleqaRANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 181 EQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFARATLN 260
Cdd:COG0845 163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRIV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 261 FGTAENV-VVPDLAIVKQAGSgdRYVFVYK-DGKVSYNKVELGRRMGTEYELKSGVPDNSQVVVAGQSRLVNGMEVEVEA 338
Cdd:COG0845 243 LGERENAlLVPASAVVRDGGG--AYVFVVDaDGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVE 320
|
....
gi 490442507 339 SSQP 342
Cdd:COG0845 321 AAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
37-336 |
5.66e-63 |
|
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: 203.32 E-value: 5.66e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 37 VKLADVKARPVDQIQDYTATVEAEVKNNIAPSSPVRIDQIFVEVGDRVSKGQKLVQMDA-----------ANLKQTKLQL 105
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDddyqlalqaalAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 106 DNQEIEFNRIDELYKVGGASKSEWDASKMQLDVKKT----------AYKNLLENTSLQSPINGVVTARNYDNGDMYSGGE 175
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQAdleaakaslaSAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 176 PVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFA 255
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRLLPGMFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 256 RATLNFGTAEN-VVVPDLAIVkqAGSGDRYVFVYK-DGKVSYNKVELGRRMGTEYELKSGVPDNSQVVVAGQSRLVNGME 333
Cdd:TIGR01730 241 RVTISLKVRSSaIVVPTQAVI--EDLNGKYVYVVKnDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGAK 318
|
...
gi 490442507 334 VEV 336
Cdd:TIGR01730 319 VKV 321
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
54-260 |
1.01e-34 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 129.40 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 54 TATVEAEVKNnIAPSSPVRIDQIFVEVGDRVSKGQKLVQMDA-------------------------------------- 95
Cdd:COG1566 38 DGRVEARVVT-VAAKVSGRVTEVLVKEGDRVKKGQVLARLDPtdlqaalaqaeaqlaaaeaqlarleaelgaeaeiaaae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 96 ANLKQTKLQLDNQEIEFNRIDELYKVGGASKSEWDASKMQLDVKKTAYKNL----------------------------- 146
Cdd:COG1566 117 AQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAqaqlaqaqaglreeeelaaaqaqvaqaea 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 147 --------LENTSLQSPINGVVTARNYDNGDMYSGGEPVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEVF 218
Cdd:COG1566 197 alaqaelnLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVF 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 490442507 219 TGTINLIYPTIDATT----------RTFQVEIRLDNKD-QRVRPGMFARATLN 260
Cdd:COG1566 277 EGKVTSISPGAGFTSppknatgnvvQRYPVRIRLDNPDpEPLRPGMSATVEID 329
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
65-255 |
1.29e-27 |
|
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: 107.59 E-value: 1.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 65 IAPSSPVRIDQIFV-EVGDRVSKGQKLVQMDAANLKQTKLQ----LDNQEIEfnRIDELYKvggASKSE---WDASKMQL 136
Cdd:pfam16576 22 VHARVEGWIEKLYVnATGDPVKKGQPLAELYSPELVAAQQEyllaLRSGDAL--SKSELLR---AARQRlrlLGMPEAQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 137 D-VKKTayKNLLENTSLQSPINGVVTARNYDNGDMYSGGEPVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGD 215
Cdd:pfam16576 97 AeLERT--GKVQPTVTVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490442507 216 EVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFA 255
Cdd:pfam16576 175 KTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
1-344 |
4.76e-21 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 92.86 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 1 MKRSIQLVALLL--TVFMGSCtggKDKAAAEHVDAKPIVKLADVKARPVDQIQDYTA-TVEAEVKNNIAPSSPVRIDQIF 77
Cdd:PRK09859 1 MNRRRKLLIPLLfcGAMLTAC---DDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGrTVPYEVAEIRPQVGGIIIKRNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 78 VEvGDRVSKGQKLVQMDAA-----------NLKQTKLQLDNQEIEFNRIDELYKVGGASKSEWDASKMQLD-------VK 139
Cdd:PRK09859 78 IE-GDKVNQGDSLYQIDPAplqaelnsakgSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNeaeanvtVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 140 KTAYKNL---LENTSLQSPINGVVTARNYDNGDMYSG--GEPVLVVEQITPV------------KLLINVSETYFTKVKK 202
Cdd:PRK09859 157 KAAVEQAtinLQYANVTSPITGVSGKSSVTVGALVTAnqADSLVTVQRLDPIyvdltqsvqdflRMKEEVASGQIKQVQG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 203 GTPVDVKLDVYGDEVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFARATLNFGTAENVV-VPDLAIVKQAGSG 281
Cdd:PRK09859 237 STPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLlVPQEGVTHNAQGK 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490442507 282 DRYVFVYKDGKVSYNKVELGRRMGTEYELKSGVPDNSQVVVAGQSRLVNGMEVEVEASSQPSS 344
Cdd:PRK09859 317 ATALILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQENA 379
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
73-324 |
5.83e-18 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 84.15 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 73 IDQIF-VEVGDRVSKGQKLVQMDAANLKQTklqldnqEIEFNRIDElyKVGGASKSEWDASKMQL------DVKK-TAYK 144
Cdd:PRK09783 134 IDKVYpLTVGDKVQKGTPLLDLTIPDWVEA-------QSEYLLLRE--TGGTATQTEGILERLRLagmpeaDIRRlIATR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 145 NLLENTSLQSPINGVVTARNYDNGDMYSGGEPVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEVFTGTINL 224
Cdd:PRK09783 205 KIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWT 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 225 IYPTIDATTRTFQVEIRLDNKDQRVRPGMFARATLNFGTAENVVVPDLAIVkQAGSGDRYVFVYKDGKVSYNKVELGRRM 304
Cdd:PRK09783 285 LLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQLNTASEPMLLIPSQALI-DTGSEQRVITVDADGRFVPKRVAVFQES 363
|
250 260
....*....|....*....|
gi 490442507 305 GTEYELKSGVPDNSQVVVAG 324
Cdd:PRK09783 364 QGVTAIRSGLAEGEKVVSSG 383
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
81-345 |
1.84e-17 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 82.92 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 81 GDRVSKGQKLVQMD----AANLKQTKLQL-------DNQEIEFNRIDELYKVGGASKSEWDASkmQLDVKKT-----AYK 144
Cdd:PRK11556 106 GQQVKAGDLLAEIDprpfKVALAQAQGQLakdqatlANARRDLARYQQLAKTNLVSRQELDAQ--QALVSETegtikADE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 145 NLLENTSLQ-------SPINGVVTARNYDNGDMYSGGE--PVLVVEQITPVKLLINVSETYFTKV----KKGTPVDVK-L 210
Cdd:PRK11556 184 ASVASAQLQldysritAPISGRVGLKQVDVGNQISSGDttGIVVITQTHPIDLVFTLPESDIATVvqaqKAGKPLVVEaW 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 211 D-VYGDEVFTGTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFARATLNFGTAEN-VVVPDLAIvkQAGSGDRYVFVY 288
Cdd:PRK11556 264 DrTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQNaVVIPTAAL--QMGNEGHFVWVL 341
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 490442507 289 -KDGKVSYNKVELGRRMGTEYELKSGVPDNSQVVVAGQSRLVNGMEVEVEASSQPSSK 345
Cdd:PRK11556 342 nDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTP 399
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
8-337 |
2.35e-14 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 73.59 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 8 VALLLTVFMgSCTGGKDKAAAEHVDAKPIVKLADVKARPVDQIQDYTATVEAEVKNNIAPS-SPVRIDQIFVEVGDrVSK 86
Cdd:PRK15030 12 VVLMLSGSL-ALTGCDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRIAEVRPQvSGIILKRNFKEGSD-IEA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 87 GQKLVQMDAA-----------NLKQTKLQLDNQEIEFNRIDELYKVGGASKSEWD---ASKMQLDVKKTAYKNLLEN--- 149
Cdd:PRK15030 90 GVSLYQIDPAtyqatydsakgDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDqalADAQQANAAVTAAKAAVETari 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 150 ----TSLQSPINGVVTARNYDNGDMYSGGEP--VLVVEQITPVKLLINVSETYFTKVK--------KGTPVDVKLDVYGD 215
Cdd:PRK15030 170 nlayTKVTSPISGRIGKSNVTEGALVQNGQAtaLATVQQLDPIYVDVTQSSNDFLRLKqelangtlKQENGKAKVSLITS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 216 EVFT----GTINLIYPTIDATTRTFQVEIRLDNKDQRVRPGMFARATLNFGTAENVVVPDLAIVKQAGSGDRYVFVY-KD 290
Cdd:PRK15030 250 DGIKfpqdGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDATVLVVgAD 329
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 490442507 291 GKVSYNKVELGRRMGTEYELKSGVPDNSQVVVAGQSRLVNGMEVEVE 337
Cdd:PRK15030 330 DKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQ 376
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
152-246 |
7.18e-14 |
|
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: 67.00 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 152 LQSPINGVVTARNYDNGDMYSGGEPVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEVFTGTINLIYPTIDA 231
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVDP 81
|
90
....*....|....*
gi 490442507 232 TTRTFQVEIRLDNKD 246
Cdd:pfam13437 82 DTGVIPVRVSIENPK 96
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
46-322 |
9.58e-10 |
|
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: 58.97 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 46 PVDQIQDYTATVEA-EVKNNIAPSSPVRIDQIFVEVGDRVSKGQKLVQMDA-----------ANLKQTKLQLDNQEIEFN 113
Cdd:pfam00529 3 PLTKGVEAPGRVVVsGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPtdyqaaldsaeAQLAKAQAQVARLQAELD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 114 RIDELYKVGGASKSEWDASKMQLDVKKTAYKNL----------LENTSLQSPINGVVTARNYDNGDMYSGGEPVLV--VE 181
Cdd:pfam00529 83 RLQALESELAISRQDYDGATAQLRAAQAAVKAAqaqlaqaqidLARRRVLAPIGGISRESLVTAGALVAQAQANLLatVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 182 QITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEV-----------------FTGTINLIYPTIDATTRTFQVEIRLDN 244
Cdd:pfam00529 163 QLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAelklakldlerteirapVDGTVAFLSVTVDGGTVSAGLRLMFVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 245 KDQRV-RPGMFARATLNFGTAEN-VVVPDLAIVKQAGSGDRYVFVYKDGKVSYNKVELGRRMGTEYELKSGVPDNSQVVV 322
Cdd:pfam00529 243 PEDNLlVPGMFVETQLDQVRVGQpVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
83-253 |
4.96e-09 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 56.89 E-value: 4.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 83 RVSKGQKLVQMDAAnlkQTKLqldNQEIEFNRIDELykvgGASKSEWDASKMQLDVKKTAyknlLENTSLQSPINGVVTA 162
Cdd:PRK03598 151 RSSRDQAQATLKSA---QDKL---SQYREGNRPQDI----AQAKASLAQAQAALAQAELN----LQDTELIAPSDGTILT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 163 RNYDNGDMYSGGEPVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEVFTGTINLIYPTIDATTRTfqVE--- 239
Cdd:PRK03598 217 RAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPTAEFTPKT--VEtpd 294
|
170 180
....*....|....*....|....
gi 490442507 240 ----------IRLDNKDQRVRPGM 253
Cdd:PRK03598 295 lrtdlvyrlrIVVTDADDALRQGM 318
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
1-322 |
3.47e-07 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 51.31 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 1 MKRSIQLVALLLTVFMGSCTGGkdkaaaeHVDAKPIVKLADVKARPVDQIQDYTAT--VEAEVKNNIAPSSPVRIDQIFV 78
Cdd:PRK11578 5 KKVKKRYLIALVIVLAGGITLW-------RILNAPVPTYQTLIVRPGDLQQSVLATgkLDALRKVDVGAQVSGQLKTLSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 79 EVGDRVSKGQKLVQMDA------------------ANLKQTKLQLDNQEIEFNRIDELYKVGGASKSEWDASKMQLDVKK 140
Cdd:PRK11578 78 AIGDKVKKDQLLGVIDPeqaenqikeveatlmelrAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 141 ------------------TAYKNlLENTSLQSPINGVVTARNYDNGDMYSGGEP---VLVVEQITPVKLLINVSETYFTK 199
Cdd:PRK11578 158 aqigtidaqikrnqasldTAKTN-LDYTRIVAPMAGEVTQITTLQGQTVIAAQQapnILTLADMSTMLVKAQVSEADVIH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 200 VKKGtpVDVKLDVYGD--EVFTGTINLIYPTIDATTRT--FQVEIRLDNKDQRVRPGMFARATLNFGTAENV-VVPDLAI 274
Cdd:PRK11578 237 LKPG--QKAWFTVLGDplTRYEGVLKDILPTPEKVNDAifYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVlTIPLSAL 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 490442507 275 VKQAGSGDRYVFVYKDGKVSYNKVELGRRMGTEYELKSGVPDNSQVVV 322
Cdd:PRK11578 315 GDPVGDNRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVII 362
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
147-222 |
1.97e-04 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 42.76 E-value: 1.97e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490442507 147 LENTSLQSPINGVVTARNYDNGDMYSGGEPVLVVEQITPVKLLINVSETYFTKVKKGTPVDVKLDVYGDEV-FTGTI 222
Cdd:PRK15136 213 LQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVvYTGKV 289
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
58-246 |
7.03e-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: 40.97 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 58 EAEVKNNIAPSSPV--RIDQIFVEVGDRVSKGQKLVQMD----------------------------------------- 94
Cdd:TIGR02971 10 EGEVVAVAAPSSGGtdRIKKLLVAEGDRVQAGQVLAELDsrpertaeldvartqldeakarlaqvragakkgeiaaqraa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 95 -------------AANLKQTKLQLDNQEIEFNRIDELYKVGGASKSEWDASKMQLDVKKTAYKN---------------- 145
Cdd:TIGR02971 90 raaaklfkdvaaqQATLNRLEAELETAQREVDRYRSLFRDGAVSASDLDSKALKLRTAEEELEEalasrseqidgaraal 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490442507 146 -------------------------------LLENTSLQSPINGVVTARNYDNGdMYSGGEPVLVVEQITPVKLLINVSE 194
Cdd:TIGR02971 170 aslaeevretdvdlaqaevksaleavqqaeaLLELTYVKAPIDGRVLKIHAREG-EVIGSEGILEMGDTSQMYAVAEVYE 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490442507 195 TYFTKVKKGTPV----------------DVKLDVYGDEVFTgtinlIYPTIDATTRTFQVEIRLDNKD 246
Cdd:TIGR02971 249 TDINRVRVGQRAtitstalsgplrgtvrRIGSLIAKNDVLS-----TDPAADADARVVEVKIRLDPAS 311
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
64-108 |
1.20e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 36.27 E-value: 1.20e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490442507 64 NIAPSSPVRIDQIFVEVGDRVSKGQKLVQMDAANLKQTKLQLDNQ 108
Cdd:pfam13533 4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQ 48
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
65-114 |
1.31e-03 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 40.38 E-value: 1.31e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490442507 65 IAPSSPVRIDQ---------IFVEVGDRVSKGQKLVQMDA----ANLKQTKLQLDNQEIEFNR 114
Cdd:TIGR01843 37 VVPSGNVKVVQhleggivreILVREGDRVKAGQVLVELDAtdveADAAELESQVLRLEAEVAR 99
|
|
| |
