|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
63-376 |
5.64e-84 |
|
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: 259.11 E-value: 5.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 63 IRGRQDIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELARKNIIS 142
Cdd:COG0845 18 VEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALLKKGAVS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 143 EYDLQMAENTLASQKAALAQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSmaTPLTTVADNSEMYVYFSLN 222
Cdd:COG0845 98 QQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG--TPLFTIADLDPLEVEFDVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 223 EKELLKmttdgsLKKMPEVQLQLVDGSIYPEKGTVETLSGVIDQTAGGARVRATFKNPNQVLRSGGSGNILIP-EKLDST 301
Cdd:COG0845 176 ESDLAR------LKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRIVlGERENA 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172971104 302 IVIPQSATVEAQDKIFAFVVTDSSTVNQTMIQVLPInNGQQYVVTGGLNPGDRIVVEGVGFIKNGMPIKPITPEE 376
Cdd:COG0845 250 LLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRR-DGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVEAAA 323
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
44-372 |
2.57e-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: 216.03 E-value: 2.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 44 TITLEPTSIELNNTYPAAaIRGRQDIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVA 123
Cdd:TIGR01730 3 VATVESETLANTLTFPGS-LEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 124 TAQLTADNKRELARKNIISEYDLQMAENTLASQKAALAQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSma 203
Cdd:TIGR01730 82 LAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 204 TPLTTVADNSEMYVYFSLNEKELLKMTTDgslkKMPEVQLQLVDGSIYpeKGTVETLSGVIDQTAGGARVRATFKNPNQV 283
Cdd:TIGR01730 160 QTLATIVDLDPLEADFSVPERDLPQLRRG----QTLTVELDALPGEEF--KGKLRFIDPRVDSGTGTVRVRATFPNPDGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 284 LRSGGSGNILIPEKLD-STIVIPQSATVEAQDKIFAFVVTDSSTVNQTMIQVLPINNGqQYVVTGGLNPGDRIVVEGVGF 362
Cdd:TIGR01730 234 LLPGMFGRVTISLKVRsSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGG-YVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 1172971104 363 IKNGMPIKPI 372
Cdd:TIGR01730 313 LRDGAKVKVV 322
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
1-376 |
3.42e-45 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 160.27 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 1 MKIRKSMLIQsqrfflLTALGATFFSCGTKQQAGMMGGVPEYATITLEPTSIELNNTYPAAAIRgRQDIEIRPNVSGFIT 80
Cdd:PRK09859 1 MNRRRKLLIP------LLFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVP-YEVAEIRPQVGGIII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 81 KLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELARKNIISEYDLQMAENTLASQKAAL 160
Cdd:PRK09859 74 KRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 161 AQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSMATPLTTVADNSEMYVYFSLNEKELLKMTTD---GSLKK 237
Cdd:PRK09859 154 TVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEvasGQIKQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 238 M---PEVQLQLVDGSIYPEKGTVETLSGVIDQTAGGARVRATFKNPNQVLRSGGSGNILIPE-KLDSTIVIPQSA-TVEA 312
Cdd:PRK09859 234 VqgsTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEgSRQNVLLVPQEGvTHNA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172971104 313 QDKIFAFVVTDSSTVNQTMIQVLPInNGQQYVVTGGLNPGDRIVVEGVGFIKNGMPIKPITPEE 376
Cdd:PRK09859 314 QGKATALILDKDDVVQLREIEASKA-IGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQ 376
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
58-357 |
1.21e-26 |
|
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: 108.66 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 58 YPAAAIRGRQDIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELAR 137
Cdd:pfam00529 10 APGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 138 KNIISEYDLQMAENTLASQKAALAQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSMATPLTTVADNSEMYV 217
Cdd:pfam00529 90 ELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 218 YFSLNEKELLKM---TTDGSLKKMPEVQLQLV----DGSIYPEK----GTVETLSGVIDQTAGGARVRATFKNPNQvlrs 286
Cdd:pfam00529 170 QITQSAAENQAEvrsELSGAQLQIAEAEAELKlaklDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMFVVPED---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 287 ggsgNILIP-----EKLDsTIVIPQSATV-------EAQDKIFAFVVTDSSTVNQTMIQVLPiNNGQQYVVTGGLNPGDR 354
Cdd:pfam00529 246 ----NLLVPgmfveTQLD-QVRVGQPVLIpfdafpqTKTGRFTGVVVGISPDTGPVRVVVDK-AQGPYYPLRIGLSAGAL 319
|
...
gi 1172971104 355 IVV 357
Cdd:pfam00529 320 VRL 322
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
63-376 |
5.64e-84 |
|
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: 259.11 E-value: 5.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 63 IRGRQDIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELARKNIIS 142
Cdd:COG0845 18 VEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKAELERYKALLKKGAVS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 143 EYDLQMAENTLASQKAALAQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSmaTPLTTVADNSEMYVYFSLN 222
Cdd:COG0845 98 QQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG--TPLFTIADLDPLEVEFDVP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 223 EKELLKmttdgsLKKMPEVQLQLVDGSIYPEKGTVETLSGVIDQTAGGARVRATFKNPNQVLRSGGSGNILIP-EKLDST 301
Cdd:COG0845 176 ESDLAR------LKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGMFVRVRIVlGERENA 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1172971104 302 IVIPQSATVEAQDKIFAFVVTDSSTVNQTMIQVLPInNGQQYVVTGGLNPGDRIVVEGVGFIKNGMPIKPITPEE 376
Cdd:COG0845 250 LLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRR-DGDQVEVLSGLKAGDRVVVSGLQRLRDGAKVRVVEAAA 323
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
44-372 |
2.57e-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: 216.03 E-value: 2.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 44 TITLEPTSIELNNTYPAAaIRGRQDIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVA 123
Cdd:TIGR01730 3 VATVESETLANTLTFPGS-LEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 124 TAQLTADNKRELARKNIISEYDLQMAENTLASQKAALAQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSma 203
Cdd:TIGR01730 82 LAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 204 TPLTTVADNSEMYVYFSLNEKELLKMTTDgslkKMPEVQLQLVDGSIYpeKGTVETLSGVIDQTAGGARVRATFKNPNQV 283
Cdd:TIGR01730 160 QTLATIVDLDPLEADFSVPERDLPQLRRG----QTLTVELDALPGEEF--KGKLRFIDPRVDSGTGTVRVRATFPNPDGR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 284 LRSGGSGNILIPEKLD-STIVIPQSATVEAQDKIFAFVVTDSSTVNQTMIQVLPINNGqQYVVTGGLNPGDRIVVEGVGF 362
Cdd:TIGR01730 234 LLPGMFGRVTISLKVRsSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGG-YVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 1172971104 363 IKNGMPIKPI 372
Cdd:TIGR01730 313 LRDGAKVKVV 322
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
1-376 |
3.42e-45 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 160.27 E-value: 3.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 1 MKIRKSMLIQsqrfflLTALGATFFSCGTKQQAGMMGGVPEYATITLEPTSIELNNTYPAAAIRgRQDIEIRPNVSGFIT 80
Cdd:PRK09859 1 MNRRRKLLIP------LLFCGAMLTACDDKSAENAAAMTPEVGVVTLSPGSVNVLSELPGRTVP-YEVAEIRPQVGGIII 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 81 KLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELARKNIISEYDLQMAENTLASQKAAL 160
Cdd:PRK09859 74 KRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 161 AQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSMATPLTTVADNSEMYVYFSLNEKELLKMTTD---GSLKK 237
Cdd:PRK09859 154 TVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMKEEvasGQIKQ 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 238 M---PEVQLQLVDGSIYPEKGTVETLSGVIDQTAGGARVRATFKNPNQVLRSGGSGNILIPE-KLDSTIVIPQSA-TVEA 312
Cdd:PRK09859 234 VqgsTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEgSRQNVLLVPQEGvTHNA 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172971104 313 QDKIFAFVVTDSSTVNQTMIQVLPInNGQQYVVTGGLNPGDRIVVEGVGFIKNGMPIKPITPEE 376
Cdd:PRK09859 314 QGKATALILDKDDVVQLREIEASKA-IGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSSQ 376
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
27-370 |
1.52e-38 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 142.93 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 27 CGTKQQAGMMGGVPEYATITLEPTSIELNNTYPAAAIRGRQdIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEE 106
Cdd:PRK15030 25 CDDKQAQQGGQQMPAVGVVTVKTEPLQITTELPGRTSAYRI-AEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 107 AVKVAEANVNVAKAAVATAQLTADNKRELARKNIIS--EYDLQMAENTLASqkAALAQAEAQLTNAKNNLSYTQVTSPSN 184
Cdd:PRK15030 104 TYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISkqEYDQALADAQQAN--AAVTAAKAAVETARINLAYTKVTSPIS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 185 GVVGEIPYRVGSLVSPSMATPLTTVADNSEMYVYFSLNEKELLKMT---TDGSLKK---MPEVQLQLVDGSIYPEKGTVE 258
Cdd:PRK15030 182 GRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKqelANGTLKQengKAKVSLITSDGIKFPQDGTLE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 259 TLSGVIDQTAGGARVRATFKNPNQVLRSGGSGNILIPEKLDST-IVIPQSATVEAQ--DKIFAFVVTDSSTVNQTMIQVL 335
Cdd:PRK15030 262 FSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNaILVPQQGVTRTPrgDATVLVVGADDKVETRPIVASQ 341
|
330 340 350
....*....|....*....|....*....|....*
gi 1172971104 336 PInnGQQYVVTGGLNPGDRIVVEGVGFIKNGMPIK 370
Cdd:PRK15030 342 AI--GDKWLVTEGLKAGDRVVISGLQKVRPGVQVK 374
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
13-372 |
2.24e-34 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 131.07 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 13 RFFLLTALGATFF--SCGTKQQAGMMGGVPEYATITLEPTSIELNNTYPAAAIRGRQdIEIRPNVSGFITKLCVDEGATV 90
Cdd:PRK09578 7 RRLLLAALVALFVlaGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQ-AEVRARVAGIVTARTYEEGQEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 91 KKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELARKNIISEYDLQMAENTLASQKAALAQAEAQLTNA 170
Cdd:PRK09578 86 KQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 171 KNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSMATPLTTVADNSEMYVYFSLNEKELLKMT-------TDGSLKKMPEVQL 243
Cdd:PRK09578 166 QLQLDYATVTAPIDGRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRravksgrATGIAQQDVAVTL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 244 QLVDGSIYPEKGTVETLSGVIDQTAGGARVRATFKNPNQVLRSGGSGNILIPEKLD-STIVIPQSATVEAQDKIFAFVVT 322
Cdd:PRK09578 246 VRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNpRAILVPRDALLRTADSASVKVVG 325
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1172971104 323 DSSTVNQTMIQVLPInNGQQYVVTGGLNPGDRIVVEGVGFIKNGMPIKPI 372
Cdd:PRK09578 326 QNGKVRDVEVEADQM-SGRDWIVTRGLAGGERVIVDNAAQFAPGTAVKAV 374
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
61-294 |
3.80e-27 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 110.14 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 61 AAIRGRQdIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVAT---------------- 124
Cdd:COG1566 39 GRVEARV-VTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARleaelgaeaeiaaaea 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 125 -----------AQLTADNKRELARKNIISEYDLQMAENTLASQKAALAQAEAQL-------------------------- 167
Cdd:COG1566 118 qlaaaqaqldlAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLaqaqaglreeeelaaaqaqvaqaeaa 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 168 -TNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSmaTPLTTVADNSEMYVYFSLNEKELlkmttdGSLKK-MP-EVQLQ 244
Cdd:COG1566 198 lAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAG--QPLLTIVPLDDLWVEAYVPETDL------GRVKPgQPvEVRVD 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172971104 245 LVDGSIYpeKGTVETLSGVI-----DQTAGGA-----RVRATFKNPNQV-LRSGGSGNILI 294
Cdd:COG1566 270 AYPDRVF--EGKVTSISPGAgftspPKNATGNvvqryPVRIRLDNPDPEpLRPGMSATVEI 328
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
58-357 |
1.21e-26 |
|
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: 108.66 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 58 YPAAAIRGRQDIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELAR 137
Cdd:pfam00529 10 APGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 138 KNIISEYDLQMAENTLASQKAALAQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSMATPLTTVADNSEMYV 217
Cdd:pfam00529 90 ELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 218 YFSLNEKELLKM---TTDGSLKKMPEVQLQLV----DGSIYPEK----GTVETLSGVIDQTAGGARVRATFKNPNQvlrs 286
Cdd:pfam00529 170 QITQSAAENQAEvrsELSGAQLQIAEAEAELKlaklDLERTEIRapvdGTVAFLSVTVDGGTVSAGLRLMFVVPED---- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 287 ggsgNILIP-----EKLDsTIVIPQSATV-------EAQDKIFAFVVTDSSTVNQTMIQVLPiNNGQQYVVTGGLNPGDR 354
Cdd:pfam00529 246 ----NLLVPgmfveTQLD-QVRVGQPVLIpfdafpqTKTGRFTGVVVGISPDTGPVRVVVDK-AQGPYYPLRIGLSAGAL 319
|
...
gi 1172971104 355 IVV 357
Cdd:pfam00529 320 VRL 322
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
71-375 |
1.90e-23 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 101.02 E-value: 1.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 71 IRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELARKNIISEYDLQMAE 150
Cdd:PRK11556 90 VRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLVSRQELDAQQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 151 NTLASQKAALAQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSMATPLTTVADNSEMYVYFSLNEKELlkMT 230
Cdd:PRK11556 170 ALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTLPESDI--AT 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 231 TDGSLKKMPEVQLQLVD--GSIYPEKGTVETLSGVIDQTAGGARVRATFKN------PNQVLrsggsgNI-LIPEKLDST 301
Cdd:PRK11556 248 VVQAQKAGKPLVVEAWDrtNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNqddalfPNQFV------NArMLVDTLQNA 321
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1172971104 302 IVIPQSATVEAQDKIFAFVVTDSSTVNQTMIQVlPINNGQQYVVTGGLNPGDRIVVEGVGFIKNGMPIKPITPE 375
Cdd:PRK11556 322 VVIPTAALQMGNEGHFVWVLNDENKVSKHLVTP-GIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQ 394
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
35-217 |
9.47e-14 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 72.11 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 35 MMGGVPEYATITLEPTSIELN--NTYPAAAIRgrqDIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAE 112
Cdd:PRK11578 29 LNAPVPTYQTLIVRPGDLQQSvlATGKLDALR---KVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 113 -------ANVNVAKAAVATAQLTADNKRELARKNIISEYDLQMAENTLASQKAALAQ-------AEAQLTNAKNNLSYTQ 178
Cdd:PRK11578 106 atlmelrAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQIGTidaqikrNQASLDTAKTNLDYTR 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1172971104 179 VTSPSNGVVGEIPYRVGSLVSPSMATP-LTTVADNSEMYV 217
Cdd:PRK11578 186 IVAPMAGEVTQITTLQGQTVIAAQQAPnILTLADMSTMLV 225
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
71-287 |
1.26e-10 |
|
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: 60.60 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 71 IRPNVSGFITKLCVD-EGATVKKGQTLFIIDpvqfeeAVKVAEANVNVAKAAVATAQLTADNKRELARKNIISeydLQMA 149
Cdd:pfam16576 22 VHARVEGWIEKLYVNaTGDPVKKGQPLAELY------SPELVAAQQEYLLALRSGDALSKSELLRAARQRLRL---LGMP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 150 ENTLASqkaalaqaeaqLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSMatPLTTVADNSEMYVYFSLNEKELlkm 229
Cdd:pfam16576 93 EAQIAE-----------LERTGKVQPTVTVYAPISGVVTELNVREGMYVQPGD--TLFTIADLSTVWVEADVPEQDL--- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 230 ttdGSLK--KMPEVQLQLVDGSIYpeKGTVETLSGVIDQTAGGARVRATFKNPNQVLRSG 287
Cdd:pfam16576 157 ---ALVKvgQPAEVTLPALPGKTF--EGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPG 211
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
69-226 |
1.49e-10 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 61.68 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 69 IEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAavataqLTADNKRELARKN-----IISE 143
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQV------LAQEKRREAGRRNrlgvqAMSR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 144 YDLQMAENTLASQKAALAQAEAQLTNAKNNLSYTQVTSPSNGVVGEIPYRVGSLVSPSmATPLTTVADNSeMYVYFSLNE 223
Cdd:PRK10559 122 EEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRG-STAVALVKQNS-FYVLAYMEE 199
|
...
gi 1172971104 224 KEL 226
Cdd:PRK10559 200 TKL 202
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
69-226 |
4.52e-09 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 57.34 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 69 IEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRE-------------- 134
Cdd:PRK10476 49 VHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMTTQRSVDAERSnaasaneqverara 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 135 --------------LARKNIIS--EYD-----LQMAENTLASQKAALAQAEAQLTN-----------------AKNNLSY 176
Cdd:PRK10476 129 naklatrtlerlepLLAKGYVSaqQVDqartaQRDAEVSLNQALLQAQAAAAAVGGvdalvaqraareaalaiAELHLED 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1172971104 177 TQVTSPSNGVVGEIPYRVGSLVSPsmATPLTTVADNSEMYVYFSLNEKEL 226
Cdd:PRK10476 209 TTVRAPFDGRVVGLKVSVGEFAAP--MQPIFTLIDTDHWYAIANFRETDL 256
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
75-200 |
1.03e-08 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 56.12 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 75 VSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVNVAKA-------------------AVATAQLTADN---- 131
Cdd:PRK03598 50 VGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAqldlmlagyrdeeiaqaraAVKQAQAAYDYaqnf 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 132 ---KRELARKNIISEYDLQMAENT--------------------------LASQKAALAQAEAQLTNAKNNLSYTQVTSP 182
Cdd:PRK03598 130 ynrQQGLWKSRTISANDLENARSSrdqaqatlksaqdklsqyregnrpqdIAQAKASLAQAQAALAQAELNLQDTELIAP 209
|
170 180
....*....|....*....|.
gi 1172971104 183 SNGVvgeIPYRV---GSLVSP 200
Cdd:PRK03598 210 SDGT---ILTRAvepGTMLNA 227
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
69-116 |
1.35e-08 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 50.52 E-value: 1.35e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1172971104 69 IEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAEANVN 116
Cdd:pfam13533 3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
179-281 |
1.70e-08 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 51.98 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 179 VTSPSNGVVGEIPYRVGSLVSPsmATPLTTVADNSEMYVYFSLNEKELlkmttdGSLKKMPEVQLQLVDGSIYPEKGTVE 258
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQA--GDPLATIVPPDRLLVEAFVPAADL------GSLKKGQKVTLKLDPGSDYTLEGKVV 73
|
90 100
....*....|....*....|...
gi 1172971104 259 TLSGVIDQTAGGARVRATFKNPN 281
Cdd:pfam13437 74 RISPTVDPDTGVIPVRVSIENPK 96
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
61-229 |
3.46e-08 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 55.09 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 61 AAIRGRQdIEIRPNVSGFITKLCVDEGATVKKGQTLFIIDPVQFEEAVKVAE---------------------ANVNVAK 119
Cdd:PRK15136 55 AYVAGNQ-VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKtalansvrqthqlminskqyqANIELQK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172971104 120 AAVATAQltAD-NKRE-LARKNIISEYDLQMAENTLASQKAA-------------------------LAQAEAQLTNAKN 172
Cdd:PRK15136 134 TALAQAQ--SDlNRRVpLGNANLIGREELQHARDAVASAQAQldvaiqqynanqamilntpledqpaVQQAATEVRNAWL 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1172971104 173 NLSYTQVTSPSNGVVGEIPYRVGSLVSPSmaTPLTTVADNSEMYVYFSLNEKELLKM 229
Cdd:PRK15136 212 ALQRTKIVSPMTGYVSRRSVQVGAQISPT--TPLMAVVPATNLWVDANFKETQLANM 266
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
70-100 |
2.69e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 37.95 E-value: 2.69e-03
10 20 30
....*....|....*....|....*....|.
gi 1172971104 70 EIRPNVSGFITKLCVDEGATVKKGQTLFIID 100
Cdd:COG0511 106 EIEAPVSGTVVEILVENGQPVEYGQPLFVIE 136
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
76-122 |
3.19e-03 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 39.68 E-value: 3.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1172971104 76 SGFITKLCVDEGATVKKGQTLFIIdpvqfeEAVKVaEANVNVAKAAV 122
Cdd:COG1038 1084 PGTVVKVLVKEGDEVKKGDPLLTI------EAMKM-ETTITAPRDGT 1123
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
68-138 |
6.04e-03 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 38.56 E-value: 6.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172971104 68 DIEIRPNVSGFITKLCVDEGATVKKGQTLFII------DPVQFEEAVKVAEANVNVAKAAVATAQLTADNKRELARK 138
Cdd:TIGR01347 43 VLEVPSPADGVLQEILFKEGDTVESGQVLAILeegndaTAAPPAKSGEEKEETPAASAAAAPTAAANRPSLSPAARR 119
|
|
| |
