|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
49-357 |
2.23e-89 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 271.82 E-value: 2.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 49 VSLDTAPRTFYGVGELEAGSQVLVAAETNGRITKIAFESGQQVKKGQLLVQLNDAVEQADLSRYQAQL-------RNAAR 121
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLaaaqaqlELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 122 LYERTRSLSAQHLVAEAQVDSTRAERDIAQGLIRQTQALIAQ-------KTIRAPFDGTIGIRQVHEGQYLNPGEAIASL 194
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQaranlayTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 195 VDTQTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFPARITAIDPLI-GKSRTIALQATLENSDGTLKAGMYANVNVV 273
Cdd:COG0845 163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVdPATRTVRVRAELPNPDGLLRPGMFVRVRIV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 274 RQASNEVITIPETAVTYTAYGDTVFITQGEGdamTVKRVSVKTGQRWDGKIEIEHGLSANDKVVTSGQLRLNDGSAVTPV 353
Cdd:COG0845 243 LGERENALLVPASAVVRDGGGAYVFVVDADG---KVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVV 319
|
....
gi 1393763572 354 AQDT 357
Cdd:COG0845 320 EAAA 323
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
44-353 |
1.30e-75 |
|
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: 236.44 E-value: 1.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 44 VALAPVSLDTAPRTFYGVGELEAGSQVLVAAETNGRITKIAFESGQQVKKGQLLVQLNDAVEQ-------ADLSRYQAQL 116
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQlalqaalAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 117 RNAARLYERTRSLSAQHLVAEAQVDSTRAERDIAQGLIR-------QTQALIAQKTIRAPFDGTIGIRQVHEGQYLNPGE 189
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEaakaslaSAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 190 AIASLVDTQTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFPARITAIDPLI-GKSRTIALQATLENSDGTLKAGMYA 268
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVdSGTGTVRVRATFPNPDGRLLPGMFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 269 NVNVVRQASNEVITIPETAVTYTAYGDTVFITQGEGdamTVKRVSVKTGQRWDGKIEIEHGLSANDKVVTSGQLRLNDGS 348
Cdd:TIGR01730 241 RVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDG---KVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGA 317
|
....*
gi 1393763572 349 AVTPV 353
Cdd:TIGR01730 318 KVKVV 322
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
40-369 |
2.35e-33 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 128.37 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 40 PPVKVALApvSLDTAPRTFYGVGELEAGSQVLVAAETNGRITKIAFESGQQVKKGQLL---------VQLNDAveQADLS 110
Cdd:PRK11556 60 APVQAATA--TEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLaeidprpfkVALAQA--QGQLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 111 RYQAQLRNAARLYERTRSLSAQHLVAEAQVDSTRAERDIAQGLIRQTQALIA----QKT---IRAPFDGTIGIRQVHEGQ 183
Cdd:PRK11556 136 KDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVAsaqlQLDysrITAPISGRVGLKQVDVGN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 184 YLNPGEAIASLVDTQT--LKLNFSLDEQASPELHQGQIV--DITVDAY--PNKTFPARIT------AIDPLIGksrTIAL 251
Cdd:PRK11556 216 QISSGDTTGIVVITQThpIDLVFTLPESDIATVVQAQKAgkPLVVEAWdrTNSKKLSEGTllsldnQIDATTG---TIKL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 252 QATLENSDGTLKAGMYANVNVVRQASNEVITIPETAVTYTAYGDTVFITQGEGdamTVKRVSVKTGQRWDGKIEIEHGLS 331
Cdd:PRK11556 293 KARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDEN---KVSKHLVTPGIQDSQKVVISAGLS 369
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1393763572 332 ANDKVVTSGQLRLNDGS---AVTPVAQDTLSEPVANTAQGS 369
Cdd:PRK11556 370 AGDRVVTDGIDRLTEGAkveVVEPQSATTPEEKATSREYAK 410
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
69-268 |
1.33e-29 |
|
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: 113.37 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 69 QVLVAAETNGRITKIAFES-GQQVKKGQLLVQLN--DAVE-QADL--------SRYQAQLRNAARlyERTRSLSaqhlVA 136
Cdd:pfam16576 19 LAHVHARVEGWIEKLYVNAtGDPVKKGQPLAELYspELVAaQQEYllalrsgdALSKSELLRAAR--QRLRLLG----MP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 137 EAQVDSTRAERDIAQGLirqtqaliaqkTIRAPFDGTIGIRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQASPELHQ 216
Cdd:pfam16576 93 EAQIAELERTGKVQPTV-----------TVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1393763572 217 GQIVDITVDAYPNKTFPARITAIDPLI-GKSRTIALQATLENSDGTLKAGMYA 268
Cdd:pfam16576 162 GQPAEVTLPALPGKTFEGKVDYIYPTLdPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
72-100 |
1.04e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 37.01 E-value: 1.04e-03
10 20
....*....|....*....|....*....
gi 1393763572 72 VAAETNGRITKIAFESGQQVKKGQLLVQL 100
Cdd:cd06850 39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
49-357 |
2.23e-89 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 271.82 E-value: 2.23e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 49 VSLDTAPRTFYGVGELEAGSQVLVAAETNGRITKIAFESGQQVKKGQLLVQLNDAVEQADLSRYQAQL-------RNAAR 121
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLaaaqaqlELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 122 LYERTRSLSAQHLVAEAQVDSTRAERDIAQGLIRQTQALIAQ-------KTIRAPFDGTIGIRQVHEGQYLNPGEAIASL 194
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQaranlayTTIRAPFDGVVGERNVEPGQLVSAGTPLFTI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 195 VDTQTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFPARITAIDPLI-GKSRTIALQATLENSDGTLKAGMYANVNVV 273
Cdd:COG0845 163 ADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVdPATRTVRVRAELPNPDGLLRPGMFVRVRIV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 274 RQASNEVITIPETAVTYTAYGDTVFITQGEGdamTVKRVSVKTGQRWDGKIEIEHGLSANDKVVTSGQLRLNDGSAVTPV 353
Cdd:COG0845 243 LGERENALLVPASAVVRDGGGAYVFVVDADG---KVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVV 319
|
....
gi 1393763572 354 AQDT 357
Cdd:COG0845 320 EAAA 323
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
44-353 |
1.30e-75 |
|
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: 236.44 E-value: 1.30e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 44 VALAPVSLDTAPRTFYGVGELEAGSQVLVAAETNGRITKIAFESGQQVKKGQLLVQLNDAVEQ-------ADLSRYQAQL 116
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQlalqaalAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 117 RNAARLYERTRSLSAQHLVAEAQVDSTRAERDIAQGLIR-------QTQALIAQKTIRAPFDGTIGIRQVHEGQYLNPGE 189
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEaakaslaSAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 190 AIASLVDTQTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFPARITAIDPLI-GKSRTIALQATLENSDGTLKAGMYA 268
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVdSGTGTVRVRATFPNPDGRLLPGMFG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 269 NVNVVRQASNEVITIPETAVTYTAYGDTVFITQGEGdamTVKRVSVKTGQRWDGKIEIEHGLSANDKVVTSGQLRLNDGS 348
Cdd:TIGR01730 241 RVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDG---KVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVKLRDGA 317
|
....*
gi 1393763572 349 AVTPV 353
Cdd:TIGR01730 318 KVKVV 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
66-272 |
1.27e-35 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 132.48 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 66 AGSQVLVAAETNGRITKIAFESGQQVKKGQLLVQLND-----AVEQA-----------------------------DLSR 111
Cdd:COG1566 42 EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPtdlqaALAQAeaqlaaaeaqlarleaelgaeaeiaaaeaQLAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 112 YQAQLRNAARLYERTRSLSAQHLVAEAQVDSTRAERDIAQGLIRQTQALIAQK--------------------------- 164
Cdd:COG1566 122 AQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAqaglreeeelaaaqaqvaqaeaalaqa 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 165 -------TIRAPFDGTIGIRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFPARIT 237
Cdd:COG1566 202 elnlartTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVT 281
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1393763572 238 AIDPLIGKS-----------RTIALQATLENSDG-TLKAGMYANVNV 272
Cdd:COG1566 282 SISPGAGFTsppknatgnvvQRYPVRIRLDNPDPePLRPGMSATVEI 328
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
40-369 |
2.35e-33 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 128.37 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 40 PPVKVALApvSLDTAPRTFYGVGELEAGSQVLVAAETNGRITKIAFESGQQVKKGQLL---------VQLNDAveQADLS 110
Cdd:PRK11556 60 APVQAATA--TEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLaeidprpfkVALAQA--QGQLA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 111 RYQAQLRNAARLYERTRSLSAQHLVAEAQVDSTRAERDIAQGLIRQTQALIA----QKT---IRAPFDGTIGIRQVHEGQ 183
Cdd:PRK11556 136 KDQATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVAsaqlQLDysrITAPISGRVGLKQVDVGN 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 184 YLNPGEAIASLVDTQT--LKLNFSLDEQASPELHQGQIV--DITVDAY--PNKTFPARIT------AIDPLIGksrTIAL 251
Cdd:PRK11556 216 QISSGDTTGIVVITQThpIDLVFTLPESDIATVVQAQKAgkPLVVEAWdrTNSKKLSEGTllsldnQIDATTG---TIKL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 252 QATLENSDGTLKAGMYANVNVVRQASNEVITIPETAVTYTAYGDTVFITQGEGdamTVKRVSVKTGQRWDGKIEIEHGLS 331
Cdd:PRK11556 293 KARFNNQDDALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLNDEN---KVSKHLVTPGIQDSQKVVISAGLS 369
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1393763572 332 ANDKVVTSGQLRLNDGS---AVTPVAQDTLSEPVANTAQGS 369
Cdd:PRK11556 370 AGDRVVTDGIDRLTEGAkveVVEPQSATTPEEKATSREYAK 410
|
|
| 8a0102 |
TIGR00999 |
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, ... |
88-344 |
7.23e-33 |
|
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, Other]
Pssm-ID: 273386 [Multi-domain] Cd Length: 265 Bit Score: 123.32 E-value: 7.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 88 GQQVKKGQLLVQL---NDAVEQADLSRYQAQLRNAARLYERTRSLSAQHLVAEAQVDSTRAERDIAQG-LIRQTQALIAQ 163
Cdd:TIGR00999 1 GDPVKKGQVLAVVdspELAKMAAELKVAQKRVELARKTYEREKKLFEQGVIPRQEFESAEYALEEAQAeVQAAKSELRSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 164 K--------TIRAPFDGTIGIRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQASPELHQGQivDITVDAYPNKTFPAR 235
Cdd:TIGR00999 81 ReakdgsyvEVRSPFDGYITQKSVTLGDYVAPQAELFRVADLGAVWVEAEVPAKDVSRIRKGS--KATVLLENGRPLPAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 236 ITAIDPLIGK-SRTIALQATLENSDGTLKAGMYANVNVVRQASNEVITIPETAVTYTAYGDTVFITQGEGdamtVKRVSV 314
Cdd:TIGR00999 159 VDYVGPEVDGsSRTAKVRVLIKNENLTLKPGLFVQVRVETKIGEPAIAVPEDAVQDLGGRKVVFVRTQEG----FRPRPV 234
|
250 260 270
....*....|....*....|....*....|
gi 1393763572 315 KTGQRWDGKIEIEHGLSANDKVVTSGQLRL 344
Cdd:TIGR00999 235 KVGRRLGGYYEVLEGLKPGERVAVENTFLL 264
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
69-268 |
1.33e-29 |
|
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: 113.37 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 69 QVLVAAETNGRITKIAFES-GQQVKKGQLLVQLN--DAVE-QADL--------SRYQAQLRNAARlyERTRSLSaqhlVA 136
Cdd:pfam16576 19 LAHVHARVEGWIEKLYVNAtGDPVKKGQPLAELYspELVAaQQEYllalrsgdALSKSELLRAAR--QRLRLLG----MP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 137 EAQVDSTRAERDIAQGLirqtqaliaqkTIRAPFDGTIGIRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQASPELHQ 216
Cdd:pfam16576 93 EAQIAELERTGKVQPTV-----------TVYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1393763572 217 GQIVDITVDAYPNKTFPARITAIDPLI-GKSRTIALQATLENSDGTLKAGMYA 268
Cdd:pfam16576 162 GQPAEVTLPALPGKTFEGKVDYIYPTLdPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
18-361 |
3.08e-14 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 73.29 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 18 AGSAIYSTYAQNEEDEQAAYQYPPvKVALAPVSLDTAPRTFYGVGELEAGSQVLVAAETNGRITKIAFESGQQVKKGQLL 97
Cdd:PRK09578 13 ALVALFVLAGCGKGDSDAAAAAPR-EATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 98 VQLNDA-------VEQADLSRYQAQLRNAARLYERTRSLSAQHLVAE-----AQVDSTRAERDI--AQGLIRQTQALIAQ 163
Cdd:PRK09578 92 FRIDPAplkaardAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSErdyteAVADERQAKAAVasAKAELARAQLQLDY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 164 KTIRAPFDGTIGIRQVHEGQYLNPGEA--IASLVDTQTLKLNFSldeQASPE-------LHQGQIV-----DITV----- 224
Cdd:PRK09578 172 ATVTAPIDGRARRALVTEGALVGQDQAtpLTTVEQLDPIYVNFS---QPAADvealrraVKSGRATgiaqqDVAVtlvra 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 225 --DAYP--NKTFPARItAIDPligKSRTIALQATLENSDGTLKAGMYANVNVVRQASNEVITIPETAVTYTAYGDTVFIT 300
Cdd:PRK09578 249 dgSEYPlkGKLLFSDL-AVDP---TTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVV 324
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393763572 301 QGEGdamTVKRVSVKTGQRWDGKIEIEHGLSANDKVVTSGQLRLNDGSAVTPVAQDTLSEP 361
Cdd:PRK09578 325 GQNG---KVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAVERAPAAKP 382
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
66-338 |
6.62e-14 |
|
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: 71.69 E-value: 6.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 66 AGSQVLVAAETNGRITKIAFESGQQVKKGQLLVQLNDAVEQADLSRYQAQLRNA----ARLY---ERTRSLSAQHLVAEA 138
Cdd:pfam00529 17 SGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAqaqvARLQaelDRLQALESELAISRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 139 QVDSTRAERDIAQGLIRQTQALIAQ-------KTIRAPFDGTIGIRQVHEGQYLNPGEAI--ASLVDTQTLKLNFSLDEQ 209
Cdd:pfam00529 97 DYDGATAQLRAAQAAVKAAQAQLAQaqidlarRRVLAPIGGISRESLVTAGALVAQAQANllATVAQLDQIYVQITQSAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 210 ASPELHQGQIVDITVDAYPNKT-----------------FPARITAIDPLI-GKSRTIALQATLEN-SDGTLKAGMYANV 270
Cdd:pfam00529 177 ENQAEVRSELSGAQLQIAEAEAelklakldlerteirapVDGTVAFLSVTVdGGTVSAGLRLMFVVpEDNLLVPGMFVET 256
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1393763572 271 NVVRQASNEVITIPETAVTYTAYGD-TVFITqgeGDAMTVKRVSVKTGQRWDGKIEIEHGLSANDKVVT 338
Cdd:pfam00529 257 QLDQVRVGQPVLIPFDAFPQTKTGRfTGVVV---GISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
165-265 |
8.18e-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: 8.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 165 TIRAPFDGTIGIRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFPARITAIDPLIG 244
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
90 100
....*....|....*....|....
gi 1393763572 245 -KSRTIALQATLENSDG--TLKAG 265
Cdd:pfam13437 81 pDTGVIPVRVSIENPKTpiPLLPG 104
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
1-369 |
8.20e-14 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 72.05 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 1 MNKKTIMTLCSVLIAVGAGSAIysTYAQNEEDEQAAYQYPPVKValapVSLDTAPR--TFYGVGELEAGSQVLVAAETNG 78
Cdd:PRK15030 1 MNKNRGFTPLAVVLMLSGSLAL--TGCDDKQAQQGGQQMPAVGV----VTVKTEPLqiTTELPGRTSAYRIAEVRPQVSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 79 RITKIAFESGQQVKKGQLLVQLNDAVEQA-------DLSRYQAQLRNAARLYERTRSLSAQHLVAEAQVDSTRAERDIAQ 151
Cdd:PRK15030 75 IILKRNFKEGSDIEAGVSLYQIDPATYQAtydsakgDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQAN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 152 GLIRQTQALI-------AQKTIRAPFDGTIGIRQVHEGQYLNPGEAIAsLVDTQTLKLNFSLDEQAS-------PELHQG 217
Cdd:PRK15030 155 AAVTAAKAAVetarinlAYTKVTSPISGRIGKSNVTEGALVQNGQATA-LATVQQLDPIYVDVTQSSndflrlkQELANG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 218 QIVD---------ITVDA--YPNK-TFPARITAIDPLIGksrTIALQATLENSDGTLKAGMYANVNVVRQASNEVITIPE 285
Cdd:PRK15030 234 TLKQengkakvslITSDGikFPQDgTLEFSDVTVDQTTG---SITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 286 TAVTYTAYGDTVFITQGEGDAMTVKRV--SVKTGQRWdgkiEIEHGLSANDKVVTSGQLRLNDGSAVTpvAQDTLSEPVA 363
Cdd:PRK15030 311 QGVTRTPRGDATVLVVGADDKVETRPIvaSQAIGDKW----LVTEGLKAGDRVVISGLQKVRPGVQVK--AQEVTADNNQ 384
|
....*.
gi 1393763572 364 NTAQGS 369
Cdd:PRK15030 385 QAASGA 390
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
70-366 |
8.49e-14 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 72.21 E-value: 8.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 70 VLVAAETNGRITKI-AFESGQQVKKGQLLVQLN--DAVE-QAD---LSRYQAQLRNAARLYERTRsLSAQhlvaeaqvds 142
Cdd:PRK09783 124 AIVQARAAGFIDKVyPLTVGDKVQKGTPLLDLTipDWVEaQSEyllLRETGGTATQTEGILERLR-LAGM---------- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 143 trAERDIAQglIRQTQALIAQKTIRAPFDGTIGIRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQASPELHQGQIVDI 222
Cdd:PRK09783 193 --PEADIRR--LIATRKIQTRFTLKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 223 TVDAYPNKTFPARITAIDPLI-GKSRTIALQATLENSDGTLKAGMYANVNVVRQaSNEVITIPETAVTYTAYGDTVFITQ 301
Cdd:PRK09783 269 TVPARPDKTFTIRKWTLLPSVdAATRTLQLRLEVDNADEALKPGMNAWLQLNTA-SEPMLLIPSQALIDTGSEQRVITVD 347
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1393763572 302 GEGDAMTvKRVSVKtgQRWDGKIEIEHGLSANDKVVTSGqLRLNDGSAVTPVAQDTLSEPVANTA 366
Cdd:PRK09783 348 ADGRFVP-KRVAVF--QESQGVTAIRSGLAEGEKVVSSG-LFLIDSEANISGALERMRSESATHA 408
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
75-356 |
4.77e-12 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 66.66 E-value: 4.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 75 ETNGRITKIAFESGQQVKKGQLLVQLNDAVEQA-------DLSRYQAQLRNAARLYERTRSLSAQHLVAEAQVDSTRAER 147
Cdd:PRK09859 67 QVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAelnsakgSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 148 DIAQGLIRQTQALIAQKTIR-------APFDGTIGIRQVHEGQYLNPGEAiASLVDTQTLK-----LNFSLDE--QASPE 213
Cdd:PRK09859 147 NEAEANVTVAKAAVEQATINlqyanvtSPITGVSGKSSVTVGALVTANQA-DSLVTVQRLDpiyvdLTQSVQDflRMKEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 214 LHQGQI--------VDITVDAYPNKTFPARITAIDPLIGKSR-TIALQATLENSDGTLKAGMYANVNVVRQASNEVITIP 284
Cdd:PRK09859 226 VASGQIkqvqgstpVQLNLENGKRYSQTGTLKFSDPTVDETTgSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLLVP 305
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393763572 285 ETAVTYTAYGDTVFITQGEGDAMTVKRV--SVKTGQRWdgkiEIEHGLSANDKVVTSGQLRLNDGSAVTPVAQD 356
Cdd:PRK09859 306 QEGVTHNAQGKATALILDKDDVVQLREIeaSKAIGDQW----VVTSGLQAGDRVIVSGLQRIRPGIKARAISSS 375
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
62-339 |
5.78e-12 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 66.34 E-value: 5.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 62 GELEAGSQVLVAAETNGRITKIAFESGQQVKKGQLLVQLNDAVEQ--------------ADLSRYQAQLRNAARLYERTR 127
Cdd:PRK11578 54 GKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveatlmelrAQRQQAEAELKLARVTLSRQQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 128 SLSAQHLVAEAQVDSTRAERDIAQGLIRQTQALIAQ--------KT------IRAPFDGTIGIRQVHEGQYLNPGEA--- 190
Cdd:PRK11578 134 RLAKTQAVSQQDLDTAATELAVKQAQIGTIDAQIKRnqasldtaKTnldytrIVAPMAGEVTQITTLQGQTVIAAQQapn 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 191 IASLVDTQTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFPARITAIDPLIGK-SRTIALQATLE--NSDGTLKAGMY 267
Cdd:PRK11578 214 ILTLADMSTMLVKAQVSEADVIHLKPGQKAWFTVLGDPLTRYEGVLKDILPTPEKvNDAIFYYARFEvpNPNGLLRLDMT 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393763572 268 ANVNVVRQASNEVITIPETAVtytayGDTVFITQGEGDAM----TVKRVsVKTGQRWDGKIEIEHGLSANDKVVTS 339
Cdd:PRK11578 294 AQVHIQLTDVKNVLTIPLSAL-----GDPVGDNRYKVKLLrngeTRERE-VTIGARNDTDVEIVKGLEAGDEVIIG 363
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
70-197 |
2.71e-10 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 61.20 E-value: 2.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 70 VLVAAETNGRITKIAFESGQQVKKGQLLVQLN-----DAVEQA--DLSRYQAQLRN------------------------ 118
Cdd:PRK10476 49 VHVASEVGGRIVELAVTENQAVKKGDLLFRIDprpyeLTVAQAqaDLALADAQIMTtqrsvdaersnaasaneqverara 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 119 ----AARLYERTRSLSAQHLVAEAQVDSTR-----AERDIAQGLIRQTQA---------LIAQK---------------- 164
Cdd:PRK10476 129 naklATRTLERLEPLLAKGYVSAQQVDQARtaqrdAEVSLNQALLQAQAAaaavggvdaLVAQRaareaalaiaelhled 208
|
170 180 190
....*....|....*....|....*....|....
gi 1393763572 165 -TIRAPFDGTIGIRQVHEGQYLNPGEAIASLVDT 197
Cdd:PRK10476 209 tTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDT 242
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
2-241 |
2.11e-09 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 58.05 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 2 NKKTIMTLCSVLIAVGAGSAIYSTYAQNEEDeqaayqyppvkvalapvsldtaPRTFYGVGELEagsQVLVAAETNGRIT 81
Cdd:PRK03598 1 MKKKVVIGLAVVVLAAAVAGGWWWYQSRQDN----------------------GLTLYGNVDIR---TVNLGFRVGGRLA 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 82 KIAFESGQQVKKGQLLVQLNDA--------------VEQADLSRY-------------------QAQLRNAARLYERTRS 128
Cdd:PRK03598 56 SLAVDEGDAVKAGQVLGELDAApyenalmqakanvsVAQAQLDLMlagyrdeeiaqaraavkqaQAAYDYAQNFYNRQQG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 129 LSAQHLVAEAQVDSTRAERDIAQGLIR--------------------------QTQALIAQK-------TIRAPFDGTIG 175
Cdd:PRK03598 136 LWKSRTISANDLENARSSRDQAQATLKsaqdklsqyregnrpqdiaqakaslaQAQAALAQAelnlqdtELIAPSDGTIL 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393763572 176 IRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFPARITAIDP 241
Cdd:PRK03598 216 TRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSP 281
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
66-240 |
9.56e-07 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 50.08 E-value: 9.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 66 AGSQVLVAAETNGRITKIAFESGQQVKKGQLLVQLND-----AVEQA----------------DLSRYQA-------QLR 117
Cdd:PRK15136 58 AGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPtdaeqAFEKAktalansvrqthqlmiNSKQYQAnielqktALA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 118 NAARLYERTRSLSAQHLV-------AEAQVDSTRAERDIA-------QGLIRQT---------QA--------LIAQKT- 165
Cdd:PRK15136 138 QAQSDLNRRVPLGNANLIgreelqhARDAVASAQAQLDVAiqqynanQAMILNTpledqpavqQAatevrnawLALQRTk 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1393763572 166 IRAPFDGTIGIRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQASPELHQGQIVDITVDAY-PNKTFPARITAID 240
Cdd:PRK15136 218 IVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVVGLD 293
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
70-223 |
6.97e-06 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 47.43 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 70 VLVAAETNGRITKIAFESGQQVKKGQLLVQLND-----AVE--QADLSRYQAQLRNAARLYERTRSLSAQHLVAEA---- 138
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQpryqkALAeaEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEidqa 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 139 ---------QVDSTRAERDIAQGLIRQTqaliaqkTIRAPFDGTIGIRQVHEGQYLNPGEAIASLVDTQTLKLNFSLDEQ 209
Cdd:PRK10559 128 nnvlqtvlhQLAKAQATRDLAKLDLERT-------VIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEET 200
|
170
....*....|....
gi 1393763572 210 ASPELHQGQIVDIT 223
Cdd:PRK10559 201 KLEGVRPGYRAEIT 214
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
69-117 |
1.18e-05 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 42.04 E-value: 1.18e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1393763572 69 QVLVAAETNGRITKIAFESGQQVKKGQLLVQLNDAVEQADLSRYQAQLR 117
Cdd:pfam13533 2 VVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
91-241 |
2.63e-05 |
|
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: 45.77 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 91 VKKGQLLVQLNDAVE-QADLSRYQAQLRNAARLYERTRsLSAQHLVAEAQVDSTRAERDIAQGLIRQTQAL------IAQ 163
Cdd:TIGR01843 193 VSRLELLELERERAEaQGELGRLEAELEVLKRQIDELQ-LERQQIEQTFREEVLEELTEAQARLAELRERLnkardrLQR 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763572 164 KTIRAPFDGTI-GIRQVHEGQYLNPGEAIASLVDT-QTLKLNFSLDEQASPELHQGQIVDITVDAYPNKTFP---ARITA 238
Cdd:TIGR01843 272 LIIRSPVDGTVqSLKVHTVGGVVQPGETLMEIVPEdDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRYGilnGKVKS 351
|
...
gi 1393763572 239 IDP 241
Cdd:TIGR01843 352 ISP 354
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
72-100 |
1.04e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 37.01 E-value: 1.04e-03
10 20
....*....|....*....|....*....
gi 1393763572 72 VAAETNGRITKIAFESGQQVKKGQLLVQL 100
Cdd:cd06850 39 VTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
