|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
40-358 |
7.19e-71 |
|
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: 224.05 E-value: 7.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 40 EKVSDKLFFPAVANAAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFSVIDSQ-------YR 112
Cdd:COG0845 6 GDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQlelakaeLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 113 RSQPLVEKGLLAKSQFDEIAAQRQI-------ARAELELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQQIVNIHNI 185
Cdd:COG0845 86 RYKALLKKGAVSQQELDQAKAALDQaqaalaaAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 186 DSVEVLIQLPDRLYAtqpTASELAKIETVVRVPSGQVYPARIKEFTTEPDPATGTFTVTLSLPMPEQELiLDGMAVEVSA 265
Cdd:COG0845 166 DPLEVEFDVPESDLA---RLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL-RPGMFVRVRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 266 KGQHVGlnplNTISIPIEAIFNADGDeldktaQYVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLVVAGVARLR 345
Cdd:COG0845 242 VLGERE----NALLVPASAVVRDGGG------AYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLR 311
|
330
....*....|...
gi 446614530 346 DGMKVQVLEERGH 358
Cdd:COG0845 312 DGAKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
33-352 |
4.99e-67 |
|
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: 214.10 E-value: 4.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 33 VKVAQAGEK-VSDKLFFPAVANAAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLA-------VDNAQARF 104
Cdd:TIGR01730 1 VTVATVESEtLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLAlqaalaqLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 105 SVIDSQYRRSQPLVEKGLLAKSQFDEIAAQRQIARAE-------LELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQ 177
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADleaakasLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 178 QIVNIHNIDSVEVLIQLPDRLYatqPTASELAKIETVVRVPSGQVYPARIKEFTTEPDPATGTFTVTLSLPMPEQELiLD 257
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDL---PQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRL-LP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 258 GMAVEVSAkgqhVGLNPLNTISIPIEAIFnadgdeLDKTAQYVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLV 337
Cdd:TIGR01730 237 GMFGRVTI----SLKVRSSAIVVPTQAVI------EDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIV 306
|
330
....*....|....*
gi 446614530 338 VAGVARLRDGMKVQV 352
Cdd:TIGR01730 307 TAGVVKLRDGAKVKV 321
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
30-354 |
4.33e-27 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 110.65 E-value: 4.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 30 LPRVKVAQAGEK-VSDKLFFPAVANAAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARF---- 104
Cdd:PRK11556 59 LAPVQAATATEQaVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLakdq 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 105 SVIDSQYR---RSQPLVEKGLLAKSQFDeiaAQRQIAR----------AELELAKLRLSFTQLRAPIDGiisRVSAEQfe 171
Cdd:PRK11556 139 ATLANARRdlaRYQQLAKTNLVSRQELD---AQQALVSetegtikadeASVASAQLQLDYSRITAPISG---RVGLKQ-- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 172 sVQVGQQ--------IVNIHNIDSVEVLIQLPDRLYAT----QPTASELAkIETVVRVPSGQVYPARIKEFTTEPDPATG 239
Cdd:PRK11556 211 -VDVGNQissgdttgIVVITQTHPIDLVFTLPESDIATvvqaQKAGKPLV-VEAWDRTNSKKLSEGTLLSLDNQIDATTG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 240 tfTVTLSLPMPEQELILdgmavevsAKGQHVGLNPL-----NTISIPIEAIfnadgdELDKTAQYVWLLNNDNTVSKRQV 314
Cdd:PRK11556 289 --TIKLKARFNNQDDAL--------FPNQFVNARMLvdtlqNAVVIPTAAL------QMGNEGHFVWVLNDENKVSKHLV 352
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446614530 315 RLAKASRSHVQVSEGINAGDRLVVAGVARLRDGMKVQVLE 354
Cdd:PRK11556 353 TPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVE 392
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
54-338 |
3.09e-25 |
|
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: 104.04 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 54 AAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFSVIDSQYRRSQPLVEKG------------ 121
Cdd:pfam00529 17 SGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLqaleselaisrq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 122 --LLAKSQFDEIAAQRQIARAELELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQQIVN--IHNIDSVEVLIQLPD- 196
Cdd:pfam00529 97 dyDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLatVAQLDQIYVQITQSAa 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 197 --------RLYATQPTASEL-AKIE--------TVVRVPSgqvyPARIKEFTTEPDPATGTFTVTLSLPMPEQELILDGM 259
Cdd:pfam00529 177 enqaevrsELSGAQLQIAEAeAELKlakldlerTEIRAPV----DGTVAFLSVTVDGGTVSAGLRLMFVVPEDNLLVPGM 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446614530 260 AVEVSAKGQHVGLnplntisiPIEAIFNADGDELDKTAqYVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLVV 338
Cdd:pfam00529 253 FVETQLDQVRVGQ--------PVLIPFDAFPQTKTGRF-TGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
66-92 |
3.08e-05 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 41.62 E-value: 3.08e-05
10 20
....*....|....*....|....*..
gi 446614530 66 GEISKFHVKEGARVKQGDILAEIEpTD 92
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVE-TD 40
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
40-358 |
7.19e-71 |
|
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: 224.05 E-value: 7.19e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 40 EKVSDKLFFPAVANAAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFSVIDSQ-------YR 112
Cdd:COG0845 6 GDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQlelakaeLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 113 RSQPLVEKGLLAKSQFDEIAAQRQI-------ARAELELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQQIVNIHNI 185
Cdd:COG0845 86 RYKALLKKGAVSQQELDQAKAALDQaqaalaaAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 186 DSVEVLIQLPDRLYAtqpTASELAKIETVVRVPSGQVYPARIKEFTTEPDPATGTFTVTLSLPMPEQELiLDGMAVEVSA 265
Cdd:COG0845 166 DPLEVEFDVPESDLA---RLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLL-RPGMFVRVRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 266 KGQHVGlnplNTISIPIEAIFNADGDeldktaQYVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLVVAGVARLR 345
Cdd:COG0845 242 VLGERE----NALLVPASAVVRDGGG------AYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLR 311
|
330
....*....|...
gi 446614530 346 DGMKVQVLEERGH 358
Cdd:COG0845 312 DGAKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
33-352 |
4.99e-67 |
|
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: 214.10 E-value: 4.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 33 VKVAQAGEK-VSDKLFFPAVANAAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLA-------VDNAQARF 104
Cdd:TIGR01730 1 VTVATVESEtLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLAlqaalaqLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 105 SVIDSQYRRSQPLVEKGLLAKSQFDEIAAQRQIARAE-------LELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQ 177
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADleaakasLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 178 QIVNIHNIDSVEVLIQLPDRLYatqPTASELAKIETVVRVPSGQVYPARIKEFTTEPDPATGTFTVTLSLPMPEQELiLD 257
Cdd:TIGR01730 161 TLATIVDLDPLEADFSVPERDL---PQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRL-LP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 258 GMAVEVSAkgqhVGLNPLNTISIPIEAIFnadgdeLDKTAQYVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLV 337
Cdd:TIGR01730 237 GMFGRVTI----SLKVRSSAIVVPTQAVI------EDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIV 306
|
330
....*....|....*
gi 446614530 338 VAGVARLRDGMKVQV 352
Cdd:TIGR01730 307 TAGVVKLRDGAKVKV 321
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
54-263 |
4.84e-28 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 111.68 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 54 AAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFSVIDSQ----------------------- 110
Cdd:COG1566 42 EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQlarleaelgaeaeiaaaeaqlaa 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 111 -----------YRRSQPLVEKGLLAKSQFDEI------------AAQRQI----------------------ARAELELA 145
Cdd:COG1566 122 aqaqldlaqreLERYQALYKKGAVSQQELDEAraaldaaqaqleAAQAQLaqaqaglreeeelaaaqaqvaqAEAALAQA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 146 KLRLSFTQLRAPIDGIISRVSAEQFESVQVGQQIVNIHNIDSVEVLIQLPDRlyatqptasELAKI----ETVVRVPS-- 219
Cdd:COG1566 202 ELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPET---------DLGRVkpgqPVEVRVDAyp 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446614530 220 GQVYPARIK------EFTTEPDPATG----TFTVTLSLPMPEQELILDGMAVEV 263
Cdd:COG1566 273 DRVFEGKVTsispgaGFTSPPKNATGnvvqRYPVRIRLDNPDPEPLRPGMSATV 326
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
30-354 |
4.33e-27 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 110.65 E-value: 4.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 30 LPRVKVAQAGEK-VSDKLFFPAVANAAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARF---- 104
Cdd:PRK11556 59 LAPVQAATATEQaVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLakdq 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 105 SVIDSQYR---RSQPLVEKGLLAKSQFDeiaAQRQIAR----------AELELAKLRLSFTQLRAPIDGiisRVSAEQfe 171
Cdd:PRK11556 139 ATLANARRdlaRYQQLAKTNLVSRQELD---AQQALVSetegtikadeASVASAQLQLDYSRITAPISG---RVGLKQ-- 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 172 sVQVGQQ--------IVNIHNIDSVEVLIQLPDRLYAT----QPTASELAkIETVVRVPSGQVYPARIKEFTTEPDPATG 239
Cdd:PRK11556 211 -VDVGNQissgdttgIVVITQTHPIDLVFTLPESDIATvvqaQKAGKPLV-VEAWDRTNSKKLSEGTLLSLDNQIDATTG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 240 tfTVTLSLPMPEQELILdgmavevsAKGQHVGLNPL-----NTISIPIEAIfnadgdELDKTAQYVWLLNNDNTVSKRQV 314
Cdd:PRK11556 289 --TIKLKARFNNQDDAL--------FPNQFVNARMLvdtlqNAVVIPTAAL------QMGNEGHFVWVLNDENKVSKHLV 352
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446614530 315 RLAKASRSHVQVSEGINAGDRLVVAGVARLRDGMKVQVLE 354
Cdd:PRK11556 353 TPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVE 392
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
54-338 |
3.09e-25 |
|
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: 104.04 E-value: 3.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 54 AAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFSVIDSQYRRSQPLVEKG------------ 121
Cdd:pfam00529 17 SGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLqaleselaisrq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 122 --LLAKSQFDEIAAQRQIARAELELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQQIVN--IHNIDSVEVLIQLPD- 196
Cdd:pfam00529 97 dyDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLatVAQLDQIYVQITQSAa 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 197 --------RLYATQPTASEL-AKIE--------TVVRVPSgqvyPARIKEFTTEPDPATGTFTVTLSLPMPEQELILDGM 259
Cdd:pfam00529 177 enqaevrsELSGAQLQIAEAeAELKlakldlerTEIRAPV----DGTVAFLSVTVDGGTVSAGLRLMFVVPEDNLLVPGM 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446614530 260 AVEVSAKGQHVGLnplntisiPIEAIFNADGDELDKTAqYVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLVV 338
Cdd:pfam00529 253 FVETQLDQVRVGQ--------PVLIPFDAFPQTKTGRF-TGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
48-354 |
5.19e-21 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 93.24 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 48 FPAVANAAERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNA-------QARFSVIDSQYRRSQPLVEK 120
Cdd:PRK15030 56 LPGRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAkgdlakaQAAANIAQLTVNRYQKLLGT 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 121 GLLAKSQFDEIAAQRQ-------IARAELELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQQ--IVNIHNIDS--VE 189
Cdd:PRK15030 136 QYISKQEYDQALADAQqanaavtAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQAtaLATVQQLDPiyVD 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 190 VLIQLPDRLYATQPTAS-----ELAKIETVVRVPSGQVYP-ARIKEFT-TEPDPATGTFTVTLSLPMPEQELiLDGMAVE 262
Cdd:PRK15030 216 VTQSSNDFLRLKQELANgtlkqENGKAKVSLITSDGIKFPqDGTLEFSdVTVDQTTGSITLRAIFPNPDHTL-LPGMFVR 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 263 VSAKGqhvGLNPlNTISIPIEAIFNAD-GDELdktaqyVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLVVAGV 341
Cdd:PRK15030 295 ARLEE---GLNP-NAILVPQQGVTRTPrGDAT------VLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRVVISGL 364
|
330
....*....|...
gi 446614530 342 ARLRDGMKVQVLE 354
Cdd:PRK15030 365 QKVRPGVQVKAQE 377
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
63-353 |
1.58e-19 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 88.62 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 63 RVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFSVIDS-------QYRRSQPLVEKGLL-------AKSQF 128
Cdd:PRK09859 67 QVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALStasnariTFNRQASLLKTNYVsrqdydtARTQL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 129 DEIAAQRQIARAELELAKLRLSFTQLRAPIDGIISR--------VSAEQFESVQVGQQIVNIHnID---SVEVLIQLPDR 197
Cdd:PRK09859 147 NEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKssvtvgalVTANQADSLVTVQRLDPIY-VDltqSVQDFLRMKEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 198 LYATQPTASElAKIETVVRVPSGQVYPARIKEFTTEP--DPATGTFTVTLSLPMPEQELiLDGMAVE-VSAKGQHvglnp 274
Cdd:PRK09859 226 VASGQIKQVQ-GSTPVQLNLENGKRYSQTGTLKFSDPtvDETTGSVTLRAIFPNPNGDL-LPGMYVTaLVDEGSR----- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 275 LNTISIPIEAI-FNADGDeldKTAqyvWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLVVAGVARLRDGMKVQVL 353
Cdd:PRK09859 299 QNVLLVPQEGVtHNAQGK---ATA---LILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAI 372
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
10-354 |
7.01e-14 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 72.13 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 10 LAHLLLIAGCS-EPTKLERDTLPRVKVAQAGE-KVSDKLFFPAVANAAERSHLSFRVAGEISKFHVKEGARVKQGDILAE 87
Cdd:PRK09578 14 LVALFVLAGCGkGDSDAAAAAPREATVVTVRPtSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 88 IEPTDYRLAVDNAQARFSVIDSQY-------RRSQPLVEKGLLAKSQF-----DEIAAQRQI--ARAELELAKLRLSFTQ 153
Cdd:PRK09578 94 IDPAPLKAARDAAAGALAKAEAAHlaaldkrRRYDDLVRDRAVSERDYteavaDERQAKAAVasAKAELARAQLQLDYAT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 154 LRAPIDGIISRvsAEQFESVQVGQQ----IVNIHNIDSVEV--------LIQLPDRLYATQPTASELAKIETVVRVPSGQ 221
Cdd:PRK09578 174 VTAPIDGRARR--ALVTEGALVGQDqatpLTTVEQLDPIYVnfsqpaadVEALRRAVKSGRATGIAQQDVAVTLVRADGS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 222 VYPARIKEFTTE--PDPATGTFTVTLSLPMPEQELiLDGMAVEVSAKGqhvGLNPlNTISIPIEAifnadgdeLDKTAQ- 298
Cdd:PRK09578 252 EYPLKGKLLFSDlaVDPTTDTVAMRALFPNPEREL-LPGAYVRIALDR---AVNP-RAILVPRDA--------LLRTADs 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446614530 299 -YVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLVVAGVARLRDGMKVQVLE 354
Cdd:PRK09578 319 aSVKVVGQNGKVRDVEVEADQMSGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAVE 375
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
63-338 |
3.69e-12 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 66.72 E-value: 3.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 63 RVAGEISKFHVKEGARVKQGDILAEIEP--------------TDYRLAVDNAQARFSVIDSQYRRSQPLVEKGLLAKSQF 128
Cdd:PRK11578 67 QVSGQLKTLSVAIGDKVKKDQLLGVIDPeqaenqikeveatlMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 129 DE--------------IAAQRQIARAELELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQQIVNIHNidsvevLIQL 194
Cdd:PRK11578 147 DTaatelavkqaqigtIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILT------LADM 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 195 PDRLYATQPTASELAKIE-------TVVRVPsGQVYPARIKEFTTEPDPATGT--FTVTLSLPMPEQELILDgMAVEVSA 265
Cdd:PRK11578 221 STMLVKAQVSEADVIHLKpgqkawfTVLGDP-LTRYEGVLKDILPTPEKVNDAifYYARFEVPNPNGLLRLD-MTAQVHI 298
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446614530 266 KGQHVGlnplNTISIPIEAIfnadGDELDKTAQYVWLLNNDNTvSKRQVRLAKASRSHVQVSEGINAGDRLVV 338
Cdd:PRK11578 299 QLTDVK----NVLTIPLSAL----GDPVGDNRYKVKLLRNGET-REREVTIGARNDTDVEIVKGLEAGDEVII 362
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
55-170 |
1.08e-11 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 65.05 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 55 AERSHLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFSVIDSQ------------------------ 110
Cdd:PRK10476 46 ADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQimttqrsvdaersnaasaneqver 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 111 -----------YRRSQPLVEKGLLAKSQFDEIA-------------------------------AQRQIARAELELAKLR 148
Cdd:PRK10476 126 aranaklatrtLERLEPLLAKGYVSAQQVDQARtaqrdaevslnqallqaqaaaaavggvdalvAQRAAREAALAIAELH 205
|
170 180
....*....|....*....|....
gi 446614530 149 LSFTQLRAPIDGIIS--RVSAEQF 170
Cdd:PRK10476 206 LEDTTVRAPFDGRVVglKVSVGEF 229
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
154-256 |
4.68e-09 |
|
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: 53.52 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 154 LRAPIDGIISRVSAEQFESVQVGQQIVNIHNIDSVEVLIQLPDRLYAtqpTASELAKIETVVRVPSGQVYPARIKEFTTE 233
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLG---SLKKGQKVTLKLDPGSDYTLEGKVVRISPT 78
|
90 100
....*....|....*....|...
gi 446614530 234 PDPATGTFTVTLSLPMPEQELIL 256
Cdd:pfam13437 79 VDPDTGVIPVRVSIENPKTPIPL 101
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
64-191 |
1.09e-08 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 55.90 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 64 VAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFS----VIDSQYRRSQPLVEKGLLAKSQfDEI-------- 131
Cdd:PRK10559 54 VSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAyyqvLAQEKRREAGRRNRLGVQAMSR-EEIdqannvlq 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446614530 132 AAQRQIARAE--LELAKLRLSFTQLRAPIDGIISRVSAEQFESVQVGQQIVNIHNIDSVEVL 191
Cdd:PRK10559 133 TVLHQLAKAQatRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVL 194
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
58-254 |
2.79e-08 |
|
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: 53.66 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 58 SHLSFRVAGEISKFHVK-EGARVKQGDILAEIEPTD-------YRLAVDNAQARfsvidsqyrRSQPLVEKGL------- 122
Cdd:pfam16576 20 AHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPElvaaqqeYLLALRSGDAL---------SKSELLRAARqrlrllg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 123 LAKSQFDEIAAQRQIARaelelaklRLSFtqlRAPIDGIISRVSAEQFESVQVGQQIVNIHNIDSVEVLIQLPDRlyatq 202
Cdd:pfam16576 91 MPEAQIAELERTGKVQP--------TVTV---YAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQ----- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446614530 203 ptasELAKIET----VVRVPS--GQVYPARIKEFTTEPDPATGTFTVTLSLPMPEQEL 254
Cdd:pfam16576 155 ----DLALVKVgqpaEVTLPAlpGKTFEGKVDYIYPTLDPKTRTVRVRIELPNPDGRL 208
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
60-105 |
4.00e-08 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 48.98 E-value: 4.00e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446614530 60 LSFRVAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNAQARFS 105
Cdd:pfam13533 5 IASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
63-341 |
5.70e-08 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 54.10 E-value: 5.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 63 RVAGEISK-FHVKEGARVKQGDILAEIEPTDYRlavdNAQARFSVIDS---QYRRSQPLVEKGLLAKSQFDEIaaQRQIA 138
Cdd:PRK09783 129 RAAGFIDKvYPLTVGDKVQKGTPLLDLTIPDWV----EAQSEYLLLREtggTATQTEGILERLRLAGMPEADI--RRLIA 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 139 RAelelaKLRLSFTqLRAPIDGIISRVSAEQFESVQVGQQIVNIHNIDSVEVLIQLPDRLYATQPTASELAkietvVRVP 218
Cdd:PRK09783 203 TR-----KIQTRFT-LKAPIDGVITAFDLRAGMNIAKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFT-----LTVP 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 219 SgqvYPA---RIKEFTTEP--DPATGTFTVTLSLPMPEQELildgmavevsakgqHVGLNP---LNTIS-----IPIEAI 285
Cdd:PRK09783 272 A---RPDktfTIRKWTLLPsvDAATRTLQLRLEVDNADEAL--------------KPGMNAwlqLNTASepmllIPSQAL 334
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446614530 286 FNAdGDEldktaQYVWLLNNDNTVSKRQVRLAKASRSHVQVSEGINAGDRLVVAGV 341
Cdd:PRK09783 335 IDT-GSE-----QRVITVDADGRFVPKRVAVFQESQGVTAIRSGLAEGEKVVSSGL 384
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
59-165 |
7.94e-08 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 53.43 E-value: 7.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 59 HLSFRVAGEISKFHVKEGARVKQGDILAEIEPTDY---------------------------------RLAVDNAQARFS 105
Cdd:PRK03598 45 NLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYenalmqakanvsvaqaqldlmlagyrdeeiaqaRAAVKQAQAAYD 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 106 VIDSQYRRSQPLVEKGLLAKSQFD------------------------------EIA-AQRQIARAELELAKLRLSF--T 152
Cdd:PRK03598 125 YAQNFYNRQQGLWKSRTISANDLEnarssrdqaqatlksaqdklsqyregnrpqDIAqAKASLAQAQAALAQAELNLqdT 204
|
170
....*....|....
gi 446614530 153 QLRAPIDG-IISRV 165
Cdd:PRK03598 205 ELIAPSDGtILTRA 218
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
64-179 |
6.81e-07 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 50.46 E-value: 6.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 64 VAGEISKFHVKEGARVKQGDILAEIEPTDYRLAVDNA---------QARFSVIDS-QY------------------RRSQ 115
Cdd:PRK15136 68 VSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAktalansvrQTHQLMINSkQYqanielqktalaqaqsdlNRRV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 116 PLVEKGLLAKSQFDEIAAQRQIARAELELAK--------------------------------LRLSFTQLRAPIDGIIS 163
Cdd:PRK15136 148 PLGNANLIGREELQHARDAVASAQAQLDVAIqqynanqamilntpledqpavqqaatevrnawLALQRTKIVSPMTGYVS 227
|
170
....*....|....*.
gi 446614530 164 RvsaeqfESVQVGQQI 179
Cdd:PRK15136 228 R------RSVQVGAQI 237
|
|
| lipoyl_domain |
cd06849 |
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. ... |
66-92 |
3.08e-05 |
|
Lipoyl domain of the dihydrolipoyl acyltransferase component (E2) of 2-oxo acid dehydrogenases. 2-oxo acid dehydrogenase multienzyme complexes, like pyruvate dehydrogenase (PDH), 2-oxoglutarate dehydrogenase (OGDH) and branched-chain 2-oxo acid dehydrogenase (BCDH), contain at least three different enzymes, 2-oxo acid dehydrogenase (E1), dihydrolipoyl acyltransferase (E2) and dihydrolipoamide dehydrogenase (E3) and play a key role in redox regulation. E2, the central component of the complex, catalyzes the transfer of the acyl group of CoA from E1 to E3 via reductive acetylation of a lipoyl group covalently attached to a lysine residue.
Pssm-ID: 133458 [Multi-domain] Cd Length: 74 Bit Score: 41.62 E-value: 3.08e-05
10 20
....*....|....*....|....*..
gi 446614530 66 GEISKFHVKEGARVKQGDILAEIEpTD 92
Cdd:cd06849 15 GTIVEWLVKEGDSVEEGDVLAEVE-TD 40
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
66-92 |
1.04e-04 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 40.05 E-value: 1.04e-04
10 20
....*....|....*....|....*..
gi 446614530 66 GEISKFHVKEGARVKQGDILAEIEpTD 92
Cdd:COG0508 17 GTIVEWLVKEGDTVKEGDPLAEVE-TD 42
|
|
| PRK11892 |
PRK11892 |
pyruvate dehydrogenase subunit beta; Provisional |
66-92 |
4.02e-04 |
|
pyruvate dehydrogenase subunit beta; Provisional
Pssm-ID: 237011 [Multi-domain] Cd Length: 464 Bit Score: 42.21 E-value: 4.02e-04
10 20
....*....|....*....|....*..
gi 446614530 66 GEISKFHVKEGARVKQGDILAEIEpTD 92
Cdd:PRK11892 17 GTLAKWLKKEGDKVKSGDVIAEIE-TD 42
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
66-182 |
8.54e-04 |
|
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: 41.15 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446614530 66 GEISKFHVKEGARVKQGDILAEIEPTDYR--------------------LAVDNAQARFSVIDSQYRRSQPLVEKglLAK 125
Cdd:TIGR01843 52 GIVREILVREGDRVKAGQVLVELDATDVEadaaelesqvlrleaevarlRAEADSQAAIEFPDDLLSAEDPAVPE--LIK 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 446614530 126 SQFDEIAAQRQIARAELELAKLRLSftQLRAPIDGIISRVSAEQfESVQVGQQIVNI 182
Cdd:TIGR01843 130 GQQSLFESRKSTLRAQLELILAQIK--QLEAELAGLQAQLQALR-QQLEVISEELEA 183
|
|
| PRK11856 |
PRK11856 |
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed |
66-92 |
4.54e-03 |
|
branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed
Pssm-ID: 237001 [Multi-domain] Cd Length: 411 Bit Score: 38.62 E-value: 4.54e-03
10 20
....*....|....*....|....*..
gi 446614530 66 GEISKFHVKEGARVKQGDILAEIEpTD 92
Cdd:PRK11856 17 GEIVEWLVKVGDTVKEGQPLAEVE-TD 42
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
64-89 |
8.37e-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: 34.70 E-value: 8.37e-03
10 20
....*....|....*....|....*.
gi 446614530 64 VAGEISKFHVKEGARVKQGDILAEIE 89
Cdd:cd06850 6 MPGTVVKVLVKEGDKVEAGQPLAVLE 31
|
|
| |
