|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
1-415 |
0e+00 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 790.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 1 MKGSYKSRWVIVIVVVIAAIAAFWFWQGRNDSRSAAPGATKQAQQSPAGGRRGMRSGPLAPVQAATAVEQAVPRYLTGLG 80
Cdd:PRK11556 1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQAVPRYLTGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 81 TITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLV 160
Cdd:PRK11556 81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 240
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQN 320
Cdd:PRK11556 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 321 AVVIPSAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTPE 400
Cdd:PRK11556 321 AVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE 400
|
410
....*....|....*
gi 446601658 401 EKATSREYAKKGARS 415
Cdd:PRK11556 401 EKATSREYAKKGARS 415
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
66-396 |
1.74e-105 |
|
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: 314.57 E-value: 1.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 66 TAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANAR 145
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 146 RDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTtgI 225
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 226 VVITQTHPIDLLFTLPESDIATVVQAQKagkplvVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFP 305
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQP------VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 306 NQFVNARMLVDTEQNAVVIPSAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEG 385
Cdd:COG0845 234 GMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
330
....*....|.
gi 446601658 386 AKVEVVEAQSA 396
Cdd:COG0845 314 AKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
62-391 |
5.26e-76 |
|
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: 239.14 E-value: 5.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 62 VQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 141
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 142 ANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGD 221
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 222 TtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDD 301
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----RRGQTLTVEL--DALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 302 ALFPNQFVNARMLVDTEQNAVVIPSAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDR 381
Cdd:TIGR01730 233 RLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 446601658 382 LTEGAKVEVV 391
Cdd:TIGR01730 313 LRDGAKVKVV 322
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
81-376 |
4.52e-32 |
|
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: 123.69 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 81 TITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLV 160
Cdd:pfam00529 14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 240
Cdd:pfam00529 94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 241 PESDIATVVQAQKAGKPL--------VVEAWD---RTNSKKLSEGTLLSLDNQIDATTGTIKVKARF-NNQDDALFPNQF 308
Cdd:pfam00529 174 SAAENQAEVRSELSGAQLqiaeaeaeLKLAKLdleRTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFvVPEDNLLVPGMF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446601658 309 VNARMLVDTEQNAVVIPSAALQMGNEGHF-VWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 376
Cdd:pfam00529 254 VETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
89-118 |
4.90e-04 |
|
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: 38.17 E-value: 4.90e-04
10 20 30
....*....|....*....|....*....|
gi 446601658 89 TVRSRVDGQLMALHFQEGQQVKAGDLLAEI 118
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
1-415 |
0e+00 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 790.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 1 MKGSYKSRWVIVIVVVIAAIAAFWFWQGRNDSRSAAPGATKQAQQSPAGGRRGMRSGPLAPVQAATAVEQAVPRYLTGLG 80
Cdd:PRK11556 1 MKGSRKSRWVIVIVVVIAAIAAFWFWQGRSTSSSAAPGAAKQAQQSPAGGRRGMRSGPLAPVQAATATEQAVPRYLTGLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 81 TITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLV 160
Cdd:PRK11556 81 TVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 240
Cdd:PRK11556 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVFTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQN 320
Cdd:PRK11556 241 PESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKLKARFNNQDDALFPNQFVNARMLVDTLQN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 321 AVVIPSAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTPE 400
Cdd:PRK11556 321 AVVIPTAALQMGNEGHFVWVLNDENKVSKHLVTPGIQDSQKVVISAGLSAGDRVVTDGIDRLTEGAKVEVVEPQSATTPE 400
|
410
....*....|....*
gi 446601658 401 EKATSREYAKKGARS 415
Cdd:PRK11556 401 EKATSREYAKKGARS 415
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
66-396 |
1.74e-105 |
|
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: 314.57 E-value: 1.74e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 66 TAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANAR 145
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 146 RDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTtgI 225
Cdd:COG0845 82 AELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTP--L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 226 VVITQTHPIDLLFTLPESDIATVVQAQKagkplvVEAWDRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDDALFP 305
Cdd:COG0845 160 FTIADLDPLEVEFDVPESDLARLKVGQP------VTVTLDAGPGKTFEGKVTFIDPAVDPATRTVRVRAELPNPDGLLRP 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 306 NQFVNARMLVDTEQNAVVIPSAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEG 385
Cdd:COG0845 234 GMFVRVRIVLGERENALLVPASAVVRDGGGAYVFVVDADGKVERRPVTLGRRDGDQVEVLSGLKAGDRVVVSGLQRLRDG 313
|
330
....*....|.
gi 446601658 386 AKVEVVEAQSA 396
Cdd:COG0845 314 AKVRVVEAAAP 324
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
62-391 |
5.26e-76 |
|
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: 239.14 E-value: 5.26e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 62 VQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATL 141
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 142 ANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGD 221
Cdd:TIGR01730 81 ELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 222 TtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTLLSLDNQIDATTGTIKVKARFNNQDD 301
Cdd:TIGR01730 161 T--LATIVDLDPLEADFSVPERDLPQL----RRGQTLTVEL--DALPGEEFKGKLRFIDPRVDSGTGTVRVRATFPNPDG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 302 ALFPNQFVNARMLVDTEQNAVVIPSAALQMGNEGHFVWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDR 381
Cdd:TIGR01730 233 RLLPGMFGRVTISLKVRSSAIVVPTQAVIEDLNGKYVYVVKNDGKVSKRPVEVGLRNGGYVEIESGLKAGDQIVTAGVVK 312
|
330
....*....|
gi 446601658 382 LTEGAKVEVV 391
Cdd:TIGR01730 313 LRDGAKVKVV 322
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
50-399 |
9.73e-41 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 148.79 E-value: 9.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 50 GRRGMRSGPLAP--VQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVAL 127
Cdd:PRK09578 24 GKGDSDAAAAAPreATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 128 AQAQGQLAKDKATLANARRDLARYQQLAKTNLVSrqELDAQQALVSETEGtiKADEAS----VASAQLQLDWSRITSPVD 203
Cdd:PRK09578 104 DAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVS--ERDYTEAVADERQA--KAAVASakaeLARAQLQLDYATVTAPID 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 204 GRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTLPESDIATVVQAQKAGKPLVVEAWDRTNSKKLSEGT-------L 276
Cdd:PRK09578 180 GRARRALVTEGALVGQDQATPLTTVEQLDPIYVNFSQPAADVEALRRAVKSGRATGIAQQDVAVTLVRADGSeyplkgkL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 277 LSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVVIPSAALQMGNEGHFVWVLNSENKVSK-HLVTPG 355
Cdd:PRK09578 260 LFSDLAVDPTTDTVAMRALFPNPERELLPGAYVRIALDRAVNPRAILVPRDALLRTADSASVKVVGQNGKVRDvEVEADQ 339
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446601658 356 IQDSQKVVIRaGISAGDRVVTDGIDRLTEGAKVEVVEAQSATTP 399
Cdd:PRK09578 340 MSGRDWIVTR-GLAGGERVIVDNAAQFAPGTAVKAVERAPAAKP 382
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
39-401 |
1.66e-40 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 148.32 E-value: 1.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 39 ATKQAQQSPAGGRRGMRSGPLapvQAATAVEqavpryltglGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEI 118
Cdd:PRK15030 30 AQQGGQQMPAVGVVTVKTEPL---QITTELP----------GRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 119 DPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRI 198
Cdd:PRK15030 97 DPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQYISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 199 TSPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTLPESDIATVVQ-------AQKAGKPlVVEAWDRTNSKKL 271
Cdd:PRK15030 177 TSPISGRIGKSNVTEGALVQNGQATALATVQQLDPIYVDVTQSSNDFLRLKQelangtlKQENGKA-KVSLITSDGIKFP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 272 SEGTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVVIPSAALQMGNEGH-FVWVLNSENKVSKH 350
Cdd:PRK15030 256 QDGTLEFSDVTVDQTTGSITLRAIFPNPDHTLLPGMFVRARLEEGLNPNAILVPQQGVTRTPRGDaTVLVVGADDKVETR 335
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446601658 351 LVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVE--------AQSATTPEE 401
Cdd:PRK15030 336 PIVASQAIGDKWLVTEGLKAGDRVVISGLQKVRPGVQVKAQEvtadnnqqAASGAQPEQ 394
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
90-402 |
2.58e-39 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 144.86 E-value: 2.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 90 VRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLVSRQELDAQQ 169
Cdd:PRK09859 64 IRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTAR 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 170 ALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTLPESDIATVV 249
Cdd:PRK09859 144 TQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQADSLVTVQRLDPIYVDLTQSVQDFLRMK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 250 QAQKAGKPLVVE-----AWDRTNSKKLSE-GTLLSLDNQIDATTGTIKVKARFNNQDDALFPNQFVNARMLVDTEQNAVV 323
Cdd:PRK09859 224 EEVASGQIKQVQgstpvQLNLENGKRYSQtGTLKFSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTALVDEGSRQNVLL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 324 IPSAALQMGNEGHFV-WVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVTDGIDRLTEGAKVEVVEA--QSATTPE 400
Cdd:PRK09859 304 VPQEGVTHNAQGKATaLILDKDDVVQLREIEASKAIGDQWVVTSGLQAGDRVIVSGLQRIRPGIKARAISSsqENASTES 383
|
..
gi 446601658 401 EK 402
Cdd:PRK09859 384 KQ 385
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
81-376 |
4.52e-32 |
|
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: 123.69 E-value: 4.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 81 TITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAKTNLV 160
Cdd:pfam00529 14 VVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 161 SRQELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLLFTL 240
Cdd:pfam00529 94 SRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 241 PESDIATVVQAQKAGKPL--------VVEAWD---RTNSKKLSEGTLLSLDNQIDATTGTIKVKARF-NNQDDALFPNQF 308
Cdd:pfam00529 174 SAAENQAEVRSELSGAQLqiaeaeaeLKLAKLdleRTEIRAPVDGTVAFLSVTVDGGTVSAGLRLMFvVPEDNLLVPGMF 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446601658 309 VNARMLVDTEQNAVVIPSAALQMGNEGHF-VWVLNSENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 376
Cdd:pfam00529 254 VETQLDQVRVGQPVLIPFDAFPQTKTGRFtGVVVGISPDTGPVRVVVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
70-316 |
4.25e-31 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 121.31 E-value: 4.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 70 QAVPRYLTGLGTITAaNTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLA-------------- 135
Cdd:COG1566 29 NGPDEPVTADGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAaaeaqlarleaelg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 136 -------------KDKATLANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKAD-------------------- 182
Cdd:COG1566 108 aeaeiaaaeaqlaAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAqaqlaqaqaglreeeelaaa 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 183 -------EASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESDIATVVQAQKAg 255
Cdd:COG1566 188 qaqvaqaEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQP--LLTIVPLDDLWVEAYVPETDLGRVKPGQPV- 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446601658 256 kPLVVEAWDrtnSKKLsEGTLLSLDNQIDATTG----------TIKVKARFNNQD-DALFPNQFVNARMLVD 316
Cdd:COG1566 265 -EVRVDAYP---DRVF-EGKVTSISPGAGFTSPpknatgnvvqRYPVRIRLDNPDpEPLRPGMSATVEIDTE 331
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
56-376 |
4.75e-22 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 96.77 E-value: 4.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 56 SGPLAPVQAATAVEQAVPRYLTGLGTITAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFK-------VALA 128
Cdd:PRK11578 30 NAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAEnqikeveATLM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 129 QAQGQLAKDKATLANARRDLARYQQLAKTNLVSRQELD-------AQQALVSETEGTIKADEASVASAQLQLDWSRITSP 201
Cdd:PRK11578 110 ELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDtaatelaVKQAQIGTIDAQIKRNQASLDTAKTNLDYTRIVAP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 202 VDGRVglkqvdvgNQISS--GDTtgiVVITQTHPIDLlfTLpeSDIAT-VVQAQkagkplVVEAwDRTNSKKLSEGTLLS 278
Cdd:PRK11578 190 MAGEV--------TQITTlqGQT---VIAAQQAPNIL--TL--ADMSTmLVKAQ------VSEA-DVIHLKPGQKAWFTV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 279 LDNQIDATTGTIK-VKARFNNQDDALF---------PNQFVNARM------LVDTEQNAVVIPSAAL--QMGNEGHFVWV 340
Cdd:PRK11578 248 LGDPLTRYEGVLKdILPTPEKVNDAIFyyarfevpnPNGLLRLDMtaqvhiQLTDVKNVLTIPLSALgdPVGDNRYKVKL 327
|
330 340 350
....*....|....*....|....*....|....*.
gi 446601658 341 LNsENKVSKHLVTPGIQDSQKVVIRAGISAGDRVVT 376
Cdd:PRK11578 328 LR-NGETREREVTIGARNDTDVEIVKGLEAGDEVII 362
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
87-234 |
4.88e-15 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 75.77 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 87 TVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLA------------------------ 142
Cdd:PRK03598 43 TVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDlmlagyrdeeiaqaraavkqaqaa 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 143 --NARRDLARYQQLAKTNLVSRQELD---------------AQQAL-----------VSETEGTIKADEASVASAQLQLD 194
Cdd:PRK03598 123 ydYAQNFYNRQQGLWKSRTISANDLEnarssrdqaqatlksAQDKLsqyregnrpqdIAQAKASLAQAQAALAQAELNLQ 202
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446601658 195 WSRITSPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPI 234
Cdd:PRK03598 203 DTELIAPSDGTILTRAVEPGTMLNAGST--VFTLSLTRPV 240
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
85-244 |
1.40e-14 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 74.29 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARR------------------ 146
Cdd:PRK10476 46 ADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMTTQRsvdaersnaasaneqver 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 147 ----------DLARYQQLAKTNLVSRQELD---------------------AQQALVSET---EGTIKADEASVASAQLQ 192
Cdd:PRK10476 126 aranaklatrTLERLEPLLAKGYVSAQQVDqartaqrdaevslnqallqaqAAAAAVGGVdalVAQRAAREAALAIAELH 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446601658 193 LDWSRITSPVDGRVglkqvdVGNQISSGDTTGivvitqthPIDLLFTLPESD 244
Cdd:PRK10476 206 LEDTTVRAPFDGRV------VGLKVSVGEFAA--------PMQPIFTLIDTD 243
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
84-220 |
5.26e-12 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 67.03 E-value: 5.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 84 AANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKD---------------------KATLA 142
Cdd:PRK15136 58 AGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSvrqthqlminskqyqanielqKTALA 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 143 NARRDLARYQQLAKTNLVSRQEL---------------------DAQQALVSET----EGTIKADEASVASAQLQLDWSR 197
Cdd:PRK15136 138 QAQSDLNRRVPLGNANLIGREELqhardavasaqaqldvaiqqyNANQAMILNTpledQPAVQQAATEVRNAWLALQRTK 217
|
170 180
....*....|....*....|...
gi 446601658 198 ITSPVDGRVGLKQVDVGNQISSG 220
Cdd:PRK15136 218 IVSPMTGYVSRRSVQVGAQISPT 240
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
86-135 |
7.05e-12 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 59.76 E-value: 7.05e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 446601658 86 NTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLA 135
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
84-248 |
8.66e-11 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 62.45 E-value: 8.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 84 AANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQLAKDKATLANARRDLARYQQLAkTNLVSRQ 163
Cdd:PRK10559 44 SADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRREAGRRNRLG-VQAMSRE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 164 ELDAQQALVSETEGTIKADEASVASAQLQLDWSRITSPVDGRVGLKQVDVGNQISSGDTTgiVVITQTHPIDLLFTLPES 243
Cdd:PRK10559 123 EIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTA--VALVKQNSFYVLAYMEET 200
|
....*
gi 446601658 244 DIATV 248
Cdd:PRK10559 201 KLEGV 205
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
23-379 |
4.18e-07 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 51.79 E-value: 4.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 23 FWFWQGRNDSRSAAPGAT---------KQAQQSPAGGRRGMRSGPlAPVQAATAVEQAVPRyltglGTITAANT------ 87
Cdd:PRK09783 44 FWYDPMYPNTRFDKPGKSpfmdmdlvpKYADEESSASSGGVRIDP-TQTQNLGVKTATVTR-----GPLTFAQTfpanvs 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 88 ------VTVRSRVDGQLMALH-FQEGQQVKAGDLLAEID-PSQFKvalAQAQGQLAKDKATLANARRDLARYQQLAKTNL 159
Cdd:PRK09783 118 yneyqyAIVQARAAGFIDKVYpLTVGDKVQKGTPLLDLTiPDWVE---AQSEYLLLRETGGTATQTEGILERLRLAGMPE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 160 VSRQELDAQQALvsETEGTIKAdeasvasaqlqldwsritsPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFT 239
Cdd:PRK09783 195 ADIRRLIATRKI--QTRFTLKA-------------------PIDGVITAFDLRAGMNIAKDNV--VAKIQGMDPVWVTAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 240 LPESdIATVVQAQKAGKpLVVEAWDRTnSKKLSEGTLLSldnQIDATTGTIKVKARFNNQDDALFPNqfVNARMLVDTE- 318
Cdd:PRK09783 252 IPES-IAWLVKDASQFT-LTVPARPDK-TFTIRKWTLLP---SVDAATRTLQLRLEVDNADEALKPG--MNAWLQLNTAs 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446601658 319 QNAVVIPSAAL-QMGNEGHFVWVLNSENKVSKHLVTpgIQDSQKVV-IRAGISAGDRVVTDGI 379
Cdd:PRK09783 324 EPMLLIPSQALiDTGSEQRVITVDADGRFVPKRVAV--FQESQGVTaIRSGLAEGEKVVSSGL 384
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
74-309 |
7.27e-06 |
|
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: 46.73 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 74 RYLTGLGTITA--ANTVTVRSRVDGQLMALHFQ-EGQQVKAGDLLAEIDPSQfkvaLAQAQGQLAkdkatLANARRDLAR 150
Cdd:pfam16576 4 RTIRAVGRVAYdeRRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYSPE----LVAAQQEYL-----LALRSGDALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 151 YQQLAKTnlvSRQELdaqqALVSETEGTIKADEASVASAQlqldWSRITSPVDGRVGLKQVDVGNQISSGDTtgIVVITQ 230
Cdd:pfam16576 75 KSELLRA---ARQRL----RLLGMPEAQIAELERTGKVQP----TVTVYAPISGVVTELNVREGMYVQPGDT--LFTIAD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 231 THPIDLLFTLPESDIATVvqaqKAGKPLVV-------EAWdrtnskklsEGTLLSLDNQIDATTGTIKVKARFNNQDDAL 303
Cdd:pfam16576 142 LSTVWVEADVPEQDLALV----KVGQPAEVtlpalpgKTF---------EGKVDYIYPTLDPKTRTVRVRIELPNPDGRL 208
|
....*.
gi 446601658 304 FPNQFV 309
Cdd:pfam16576 209 KPGMFA 214
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
126-227 |
4.96e-05 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 45.39 E-value: 4.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 126 ALAQAQGQLAKDKATLANARRDLARYQQlaktNLVSRQELDAQQALVSETEGTIKADEAS--VASAQLQLDWSRITSPVD 203
Cdd:TIGR01843 204 ERAEAQGELGRLEAELEVLKRQIDELQL----ERQQIEQTFREEVLEELTEAQARLAELRerLNKARDRLQRLIIRSPVD 279
|
90 100
....*....|....*....|....*
gi 446601658 204 GRV-GLKQVDVGNQISSGDTTGIVV 227
Cdd:TIGR01843 280 GTVqSLKVHTVGGVVQPGETLMEIV 304
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
82-156 |
7.70e-05 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 44.62 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 82 ITAANTVTVRSRVD-------GQLMALHFQEGQQVKAGDLLAEIDPSQFKVALAQAQGQlakdkatLANARRDLARYQQL 154
Cdd:TIGR01843 31 ATATGKVVPSGNVKvvqhlegGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQ-------VLRLEAEVARLRAE 103
|
..
gi 446601658 155 AK 156
Cdd:TIGR01843 104 AD 105
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
89-118 |
4.90e-04 |
|
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: 38.17 E-value: 4.90e-04
10 20 30
....*....|....*....|....*....|
gi 446601658 89 TVRSRVDGQLMALHFQEGQQVKAGDLLAEI 118
Cdd:cd06850 38 EVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
197-303 |
1.47e-03 |
|
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: 37.73 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446601658 197 RITSPVDGRVGLKQVDVGNQISSGDTtgIVVITQTHPIDLLFTLPESDIATVvqaqKAGKPLVVEAwdRTNSKKLSEGTL 276
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDP--LATIVPPDRLLVEAFVPAADLGSL----KKGQKVTLKL--DPGSDYTLEGKV 72
|
90 100
....*....|....*....|....*..
gi 446601658 277 LSLDNQIDATTGTIKVKARFNNQDDAL 303
Cdd:pfam13437 73 VRISPTVDPDTGVIPVRVSIENPKTPI 99
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
89-139 |
2.09e-03 |
|
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: 37.34 E-value: 2.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446601658 89 TVRSRVDGQLMALHFQEGQQVKAGDLLAEI-DPSQFKVALAQAQGQLAKDKA 139
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIvPPDRLLVEAFVPAADLGSLKK 52
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
89-120 |
3.65e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 39.74 E-value: 3.65e-03
10 20 30
....*....|....*....|....*....|..
gi 446601658 89 TVRSRVDGQLMALHFQEGQQVKAGDLLAEIDP 120
Cdd:PRK12999 1115 TITAPVDGTVKRVLVKAGDQVEAGDLLVELEP 1146
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
89-118 |
3.80e-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: 39.68 E-value: 3.80e-03
10 20 30
....*....|....*....|....*....|
gi 446601658 89 TVRSRVDGQLMALHFQEGQQVKAGDLLAEI 118
Cdd:COG1038 1115 TITAPRDGTVKEVLVKEGDQVEAGDLLIEL 1144
|
|
| |
