|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
45-385 |
1.03e-84 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 263.57 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 45 PVNVARVERRDVEQQVSGIGTVTSLHNVVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQ 124
Cdd:PRK11556 61 PVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQAT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 125 LKSAEQDLQRYRSLYAERAVSRQLLDQQQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVG 204
Cdd:PRK11556 141 LANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 205 DSLGLFSVTQIAPISVVFSL--QQEQLPQLQALLGGEAAVRAYSRDGGSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQ 282
Cdd:PRK11556 221 DTTGIVVITQTHPIDLVFTLpeSDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 283 ARLWPGQFVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRV-AADRVEAVPVRV-LQDIDGLSVVEGLASGDQVVVDGHS 360
Cdd:PRK11556 301 DALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLnDENKVSKHLVTPgIQDSQKVVISAGLSAGDRVVTDGID 380
|
330 340
....*....|....*....|....*
gi 489173481 361 RLMPGALVDIQEPRPSLAQAAERQP 385
Cdd:PRK11556 381 RLTEGAKVEVVEPQSATTPEEKATS 405
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
50-375 |
3.35e-82 |
|
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: 254.10 E-value: 3.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 50 RVERRDVEQQVSGIGTVTSLHNVVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAE 129
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 130 QDLQRYRSLYAERAVSRQLLDQQQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGDSlgL 209
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 210 FSVTQIAPISVVFSLQQEQLPQLQALlggeAAVRAYSRDGGSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQARLWPGQ 289
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVG----QPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 290 FVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRVAAD-RVEAVPVRVLQDIDGLSVV-EGLASGDQVVVDGHSRLMPGAL 367
Cdd:COG0845 236 FVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADgKVERRPVTLGRRDGDQVEVlSGLKAGDRVVVSGLQRLRDGAK 315
|
....*...
gi 489173481 368 VDIQEPRP 375
Cdd:COG0845 316 VRVVEAAA 323
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
46-371 |
6.89e-62 |
|
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: 201.77 E-value: 6.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 46 VNVARVERRDVEQQVSGIGTVTSLHNVVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQL 125
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 126 KSAEQDLQRYRSLYAERAVSRQLLDQQQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGD 205
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 206 SlgLFSVTQIAPISVVFSLQQEQLPQLQALLGGEAAVRAYSrdggSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQARL 285
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALP----GEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 286 WPGQFVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRVAAD-RVEAVPVRVLQDIDGL-SVVEGLASGDQVVVDGHSRLM 363
Cdd:TIGR01730 235 LPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDgKVSKRPVEVGLRNGGYvEIESGLKAGDQIVTAGVVKLR 314
|
....*...
gi 489173481 364 PGALVDIQ 371
Cdd:TIGR01730 315 DGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
56-356 |
5.85e-24 |
|
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: 100.96 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 56 VEQQVSGIGTVTSLHNVV-IRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAEQDLQR 134
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 135 YRSLYAERAVSRQLLDQQQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGDSLGLFSVTQ 214
Cdd:pfam00529 84 LQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 215 IAPISVVF--SLQQEQLPQLQALLGGEAAVRAYSRDGGSALGEGRLLTI-----------DNQIDSSTGTIRVRASFDNR 281
Cdd:pfam00529 164 LDQIYVQItqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIrapvdgtvaflSVTVDGGTVSAGLRLMFVVP 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489173481 282 QARLW-PGQFVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRVAADRVEAVPVRVLQDIDGLS---VVEGLASGDQVVV 356
Cdd:pfam00529 244 EDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPyypLRIGLSAGALVRL 322
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
73-102 |
1.36e-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: 1.36e-03
10 20 30
....*....|....*....|....*....|
gi 489173481 73 VIRTQIDGQLTRLLVSEGQMVEAGELLATI 102
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
45-385 |
1.03e-84 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 263.57 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 45 PVNVARVERRDVEQQVSGIGTVTSLHNVVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQ 124
Cdd:PRK11556 61 PVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQAT 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 125 LKSAEQDLQRYRSLYAERAVSRQLLDQQQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVG 204
Cdd:PRK11556 141 LANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 205 DSLGLFSVTQIAPISVVFSL--QQEQLPQLQALLGGEAAVRAYSRDGGSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQ 282
Cdd:PRK11556 221 DTTGIVVITQTHPIDLVFTLpeSDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 283 ARLWPGQFVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRV-AADRVEAVPVRV-LQDIDGLSVVEGLASGDQVVVDGHS 360
Cdd:PRK11556 301 DALFPNQFVNARMLVDTLQNAVVIPTAALQMGNEGHFVWVLnDENKVSKHLVTPgIQDSQKVVISAGLSAGDRVVTDGID 380
|
330 340
....*....|....*....|....*
gi 489173481 361 RLMPGALVDIQEPRPSLAQAAERQP 385
Cdd:PRK11556 381 RLTEGAKVEVVEPQSATTPEEKATS 405
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
50-375 |
3.35e-82 |
|
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: 254.10 E-value: 3.35e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 50 RVERRDVEQQVSGIGTVTSLHNVVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAE 129
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 130 QDLQRYRSLYAERAVSRQLLDQQQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGDSlgL 209
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 210 FSVTQIAPISVVFSLQQEQLPQLQALlggeAAVRAYSRDGGSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQARLWPGQ 289
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVG----QPVTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRPGM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 290 FVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRVAAD-RVEAVPVRVLQDIDGLSVV-EGLASGDQVVVDGHSRLMPGAL 367
Cdd:COG0845 236 FVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADgKVERRPVTLGRRDGDQVEVlSGLKAGDRVVVSGLQRLRDGAK 315
|
....*...
gi 489173481 368 VDIQEPRP 375
Cdd:COG0845 316 VRVVEAAA 323
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
46-371 |
6.89e-62 |
|
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: 201.77 E-value: 6.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 46 VNVARVERRDVEQQVSGIGTVTSLHNVVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQL 125
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 126 KSAEQDLQRYRSLYAERAVSRQLLDQQQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGD 205
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 206 SlgLFSVTQIAPISVVFSLQQEQLPQLQALLGGEAAVRAYSrdggSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQARL 285
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALP----GEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDGRL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 286 WPGQFVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRVAAD-RVEAVPVRVLQDIDGL-SVVEGLASGDQVVVDGHSRLM 363
Cdd:TIGR01730 235 LPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDgKVSKRPVEVGLRNGGYvEIESGLKAGDQIVTAGVVKLR 314
|
....*...
gi 489173481 364 PGALVDIQ 371
Cdd:TIGR01730 315 DGAKVKVV 322
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
74-372 |
1.92e-39 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 144.86 E-value: 1.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 74 IRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAEQDLQRYRSLYAERAVSRQLLDQQQ 153
Cdd:PRK15030 68 VRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQAL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 154 ATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGDSLGLFSVTQIAPISV--------VFSLQ 225
Cdd:PRK15030 148 ADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVdvtqssndFLRLK 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 226 QEQLPQLQALLGGEAAVRAYSRDGGSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQARLWPGQFVAVSLHTGVRRDQLV 305
Cdd:PRK15030 228 QELANGTLKQENGKAKVSLITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAIL 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 306 LSSKAVRRGLEGNFVYRV--AADRVEAVPVRVLQDI-DGLSVVEGLASGDQVVVDGHSRLMPGALVDIQE 372
Cdd:PRK15030 308 VPQQGVTRTPRGDATVLVvgADDKVETRPIVASQAIgDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQE 377
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
74-385 |
1.11e-27 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 112.58 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 74 IRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAEQDLQRYRSLYAERAVSRQLLDQQQ 153
Cdd:PRK09578 66 VRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 154 ATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGDSLGLFSVTQIAPISVVFSLQQEQLPQ-- 231
Cdd:PRK09578 146 ADERQAKAAVASAKAELARAQLQLDYATVTAPIDGRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEAlr 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 232 -------LQALLGGEAAVRAYSRDGGSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQARLWPGQFVAVSLHTGVRRDQL 304
Cdd:PRK09578 226 ravksgrATGIAQQDVAVTLVRADGSEYPLKGKLLFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAI 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 305 VLSSKAVRRGLEGNFVYRV-AADRVEAVPVRV--LQDIDGLsVVEGLASGDQVVVDGHSRLMPGALVdiqEPRPSLAQAA 381
Cdd:PRK09578 306 LVPRDALLRTADSASVKVVgQNGKVRDVEVEAdqMSGRDWI-VTRGLAGGERVIVDNAAQFAPGTAV---KAVERAPAAK 381
|
....
gi 489173481 382 ERQP 385
Cdd:PRK09578 382 PAPG 385
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
74-365 |
2.07e-26 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 109.03 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 74 IRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAEQDLQRYRSLYAERAVSRQLLDQQQ 153
Cdd:PRK09859 64 IRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTAR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 154 ATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGDSLGLFSVTQIAPISVVFSLQQE------ 227
Cdd:PRK09859 144 TQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQdflrmk 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 228 --QLPQLQALLGGEAAVRAYSRDGGSALGEGRLLTIDNQIDSSTGTIRVRASFDNRQARLWPGQFVAVSLHTGVRRDQLV 305
Cdd:PRK09859 224 eeVASGQIKQVQGSTPVQLNLENGKRYSQTGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLL 303
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489173481 306 LSSKAVRRGLEGNFVYRVaADRVEAVPVRVLQDIDGLS----VVEGLASGDQVVVDGHSRLMPG 365
Cdd:PRK09859 304 VPQEGVTHNAQGKATALI-LDKDDVVQLREIEASKAIGdqwvVTSGLQAGDRVIVSGLQRIRPG 366
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
56-356 |
5.85e-24 |
|
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: 100.96 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 56 VEQQVSGIGTVTSLHNVV-IRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAEQDLQR 134
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 135 YRSLYAERAVSRQLLDQQQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVGDSLGLFSVTQ 214
Cdd:pfam00529 84 LQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 215 IAPISVVF--SLQQEQLPQLQALLGGEAAVRAYSRDGGSALGEGRLLTI-----------DNQIDSSTGTIRVRASFDNR 281
Cdd:pfam00529 164 LDQIYVQItqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIrapvdgtvaflSVTVDGGTVSAGLRLMFVVP 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489173481 282 QARLW-PGQFVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRVAADRVEAVPVRVLQDIDGLS---VVEGLASGDQVVV 356
Cdd:pfam00529 244 EDNLLvPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGPyypLRIGLSAGALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
13-207 |
1.63e-23 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 99.74 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 13 VGVLAAGLVAFGGWAWLggdagakaapaparvpvnvarVERRDVEQQVSGIGTVTSlHNVVIRTQIDGQLTRLLVSEGQM 92
Cdd:COG1566 9 LLALVLLLLALGLALWA---------------------AGRNGPDEPVTADGRVEA-RVVTVAAKVSGRVTEVLVKEGDR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 93 VEAGELLATIDDRAVVAALEQAQASRA---------------------------SNQAQLKSAEQDLQRYRSLYAERAVS 145
Cdd:COG1566 67 VKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelgaeaeiaaaeaqlaAAQAQLDLAQRELERYQALYKKGAVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 146 RQLLDQQQATVDQLRATLKANDATINA---------------------------ERVRLSYTRITSPVSGKVGIRNVDVG 198
Cdd:COG1566 147 QQELDEARAALDAAQAQLEAAQAQLAQaqaglreeeelaaaqaqvaqaeaalaqAELNLARTTIRAPVDGVVTNLNVEPG 226
|
....*....
gi 489173481 199 NLVRVGDSL 207
Cdd:COG1566 227 EVVSAGQPL 235
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
51-190 |
1.21e-18 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 86.37 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 51 VERRDVEQQVSGIGTVTSLHNVVIRTQIDGQLTRLLVSEGQMVEAGELLATIDD-------RAVVAALEQAQASRASNQA 123
Cdd:PRK11578 41 VRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPeqaenqiKEVEATLMELRAQRQQAEA 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489173481 124 QLKSAEQDLQRYRSLYAERAVSRQLLDQ-------QQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKV 190
Cdd:PRK11578 121 ELKLARVTLSRQQRLAKTQAVSQQDLDTaatelavKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEV 194
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
71-165 |
3.20e-12 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 66.91 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 71 NVVIRT-----QIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQL-------------------- 125
Cdd:PRK03598 38 NVDIRTvnlgfRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLdlmlagyrdeeiaqaraavk 117
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 489173481 126 ------KSAEQDLQRYRSLYAERAVSRQLLDQQQATVDQLRATLKA 165
Cdd:PRK03598 118 qaqaayDYAQNFYNRQQGLWKSRTISANDLENARSSRDQAQATLKS 163
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
72-291 |
5.09e-09 |
|
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: 55.98 E-value: 5.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 72 VVIRTQIDGQLTRLLV-SEGQMVEAGELLATIDDRAVVAA-----LEQAQASRASNQAQLKSAEQDLQryrslyaeravs 145
Cdd:pfam16576 20 AHVHARVEGWIEKLYVnATGDPVKKGQPLAELYSPELVAAqqeylLALRSGDALSKSELLRAARQRLR------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 146 rqLLDQQQATVDQLRATLKANdatinaervrlSYTRITSPVSGKVGIRNVDVGNLVRVGDSLglFSVTQIAPISVVFSLQ 225
Cdd:pfam16576 88 --LLGMPEAQIAELERTGKVQ-----------PTVTVYAPISGVVTELNVREGMYVQPGDTL--FTIADLSTVWVEADVP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489173481 226 QEQLPQLQALLGGEAAVRAYsrdGGSALgEGRLLTIDNQIDSSTGTIRVRASFDNRQARLWPGQFV 291
Cdd:pfam16576 153 EQDLALVKVGQPAEVTLPAL---PGKTF-EGKVDYIYPTLDPKTRTVRVRIELPNPDGRLKPGMFA 214
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
70-116 |
1.25e-07 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 47.82 E-value: 1.25e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 489173481 70 HNVVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQA 116
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEA 47
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
72-207 |
3.37e-06 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 48.54 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 72 VVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASN---------------------QAQLKSAEQ 130
Cdd:PRK15136 62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSvrqthqlminskqyqanielqKTALAQAQS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 131 DLQRYRSLYAERAVSRQLLDQQQATVDQLRATL-------KANDATI-------------NAERVR-----LSYTRITSP 185
Cdd:PRK15136 142 DLNRRVPLGNANLIGREELQHARDAVASAQAQLdvaiqqyNANQAMIlntpledqpavqqAATEVRnawlaLQRTKIVSP 221
|
170 180
....*....|....*....|..
gi 489173481 186 VSGKVGIRNVDVGNLVRVGDSL 207
Cdd:PRK15136 222 MTGYVSRRSVQVGAQISPTTPL 243
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
72-204 |
1.56e-05 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 46.27 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 72 VVIRTQIDGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAEQDLQRyRSLYAERAVSRQLLDQ 151
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGR-RNRLGVQAMSREEIDQ 126
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 489173481 152 QQATVDQLRATLKANDATINAERVRLSYTRITSPVSGKVGIRNVDVGNLVRVG 204
Cdd:PRK10559 127 ANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRG 179
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
80-201 |
7.40e-05 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 44.25 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 80 GQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQL----------------------------KSAEQD 131
Cdd:PRK10476 57 GRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQImttqrsvdaersnaasaneqveraranaKLATRT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 132 LQRYRSLYAERAVSRQLLD------------------QQQA------TVDQLRATLKANDATINAERVRLSYTRITSPVS 187
Cdd:PRK10476 137 LERLEPLLAKGYVSAQQVDqartaqrdaevslnqallQAQAaaaavgGVDALVAQRAAREAALAIAELHLEDTTVRAPFD 216
|
170
....*....|....
gi 489173481 188 GKVGIRNVDVGNLV 201
Cdd:PRK10476 217 GRVVGLKVSVGEFA 230
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
82-169 |
1.00e-04 |
|
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members.
Pssm-ID: 213754 [Multi-domain] Cd Length: 327 Bit Score: 44.05 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 82 LTRLLVSEGQMVEAGELLATIDDR-AVVAALEQAQ-----------------------ASRASN---------------- 121
Cdd:TIGR02971 27 IKKLLVAEGDRVQAGQVLAELDSRpERTAELDVARtqldeakarlaqvragakkgeiaAQRAARaaaklfkdvaaqqatl 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489173481 122 ---QAQLKSAEQDLQRYRSLYAERAVSRQLLDQQQATVDQLRATLKANDAT 169
Cdd:TIGR02971 107 nrlEAELETAQREVDRYRSLFRDGAVSASDLDSKALKLRTAEEELEEALAS 157
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
73-102 |
1.36e-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: 1.36e-03
10 20 30
....*....|....*....|....*....|
gi 489173481 73 VIRTQIDGQLTRLLVSEGQMVEAGELLATI 102
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
265-358 |
1.71e-03 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 40.24 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489173481 265 IDSSTGTIRVRASFDNRQARLWPGQFVAVSLHTGVRRDQLVLSSKAVRRGLEGNFVYRVAADRVEAVPVRVLQDIDGLSV 344
Cdd:PRK09783 289 VDAATRTLQLRLEVDNADEALKPGMNAWLQLNTASEPMLLIPSQALIDTGSEQRVITVDADGRFVPKRVAVFQESQGVTA 368
|
90
....*....|....*
gi 489173481 345 V-EGLASGDQVVVDG 358
Cdd:PRK09783 369 IrSGLAEGEKVVSSG 383
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
74-102 |
7.80e-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: 38.52 E-value: 7.80e-03
10 20
....*....|....*....|....*....
gi 489173481 74 IRTQIDGQLTRLLVSEGQMVEAGELLATI 102
Cdd:COG1038 1116 ITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| PRK05704 |
PRK05704 |
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase; |
79-130 |
7.92e-03 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoyllysine-residue succinyltransferase;
Pssm-ID: 235571 [Multi-domain] Cd Length: 407 Bit Score: 38.28 E-value: 7.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 489173481 79 DGQLTRLLVSEGQMVEAGELLATIDDRAVVAALEQAQASRASNQAQLKSAEQ 130
Cdd:PRK05704 53 AGVLSEILAEEGDTVTVGQVLGRIDEGAAAGAAAAAAAAAAAAAAAPAQAQA 104
|
|
| |
