|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
1-377 |
1.61e-106 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 317.87 E-value: 1.61e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 1 MNITPKQRKIALLALVPVLAIGWLAWPS-KAPEPVL-TAEVTRQDVEQTVLASGVLQAIEQVDVGAQVSGQVTYLAVEAG 78
Cdd:PRK11578 1 MKKRKKVKKRYLIALVIVLAGGITLWRIlNAPVPTYqTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 79 QKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQLKIKQAQLKQNELSWRRQQQMFRQEASSRADLESAEAQLAVTRAEL 158
Cdd:PRK11578 81 DKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 159 QGALAEVDNAQIKVERAKTELGYNRIQAPMDGTVVSIVTRQGQTLAASQTVPTLLKLANLETMTVKAQISEADVTRVKAG 238
Cdd:PRK11578 161 GTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 239 MPVYFTLMGDPDTRYHGTLRTVELAPTNINEqatsttatnnaAVYYYALFDVPNPDHTLRVAMTTQVTIVLGERKQVLTI 318
Cdd:PRK11578 241 QKAWFTVLGDPLTRYEGVLKDILPTPEKVND-----------AIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTI 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 516391317 319 PQTALGKKLGENEYEVTLLKEdDQKETRRIKTGMKDDIKVEVVSGLSEQEKVTLNQGSP 377
Cdd:PRK11578 310 PLSALGDPVGDNRYKVKLLRN-GETREREVTIGARNDTDVEIVKGLEAGDEVIIGEAKP 367
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
39-379 |
1.10e-73 |
|
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: 232.14 E-value: 1.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 39 VTRQDVEQTVLASGVLQAIEQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQLKIKQA 118
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 119 QLKqnelswrRQQQMFRQEASSRADLESAEAQLAVtraelqgALAEVDNAQIKVERAKTELGYNRIQAPMDGTVVSIVTR 198
Cdd:COG0845 83 ELE-------RYKALLKKGAVSQQELDQAKAALDQ-------AQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 199 QGQTLAASQtvpTLLKLANLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGTLRTVELAPtnineqatsttatN 278
Cdd:COG0845 149 PGQLVSAGT---PLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAV-------------D 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 279 NAAVYYYALFDVPNPDHTLRVAMTTQVTIVLGERKQVLTIPQTALGKKLGENeyEVTLLKEDDQKETRRIKTGMKDDIKV 358
Cdd:COG0845 213 PATRTVRVRAELPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGA--YVFVVDADGKVERRPVTLGRRDGDQV 290
|
330 340
....*....|....*....|....*..
gi 516391317 359 EVVSGLSEQEKV------TLNQGSPVS 379
Cdd:COG0845 291 EVLSGLKAGDRVvvsglqRLRDGAKVR 317
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
34-379 |
3.73e-55 |
|
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: 184.44 E-value: 3.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 34 VLTAEVTRQDVEQTVLASGVLQAIEQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQL 113
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 114 KIKQAQLkqnelswRRQQQMFRQEASSRADLESAEAQLAVTRAELQGALAEVDNAQIkveraktELGYNRIQAPMDGTVV 193
Cdd:TIGR01730 81 ELAQRSF-------ERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQL-------NLRYTEIRAPFDGTIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 194 SIVTRQGQTLAASQTVPTllkLANLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGTLRtvelaptNINEQATS 273
Cdd:TIGR01730 147 RRLVEVGAYVTAGQTLAT---IVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLR-------FIDPRVDS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 274 TTATnnaavyYYALFDVPNPDHTLRVAMTTQVTIVLGERKQVLTIPQTALgkKLGENEYEVTLLKEDDQKETRRIKTGMK 353
Cdd:TIGR01730 217 GTGT------VRVRATFPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAV--IEDLNGKYVYVVKNDGKVSKRPVEVGLR 288
|
330 340 350
....*....|....*....|....*....|..
gi 516391317 354 DDIKVEVVSGLSEQEKV------TLNQGSPVS 379
Cdd:TIGR01730 289 NGGYVEIESGLKAGDQIvtagvvKLRDGAKVK 320
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
41-372 |
8.36e-18 |
|
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: 83.24 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 41 RQDVEQTVLASGVLQAIEQVD-VGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQLKIKQAQ 119
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 120 LKQNELSWRRQQQMFRQEASSRADLESAEAQLAVTRAELQGALAEVDNAQIKVE------RAKTELGYNRIQApmDGTVV 193
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPiggisrESLVTAGALVAQA--QANLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 194 SIVTRQGQTLA-ASQTVPTLLKLANLETMTVKAQISEADVTRVKAgmpvyftlmgdpdtRYHGTLRTVELAPTNINEQAT 272
Cdd:pfam00529 159 ATVAQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEAELKLA--------------KLDLERTEIRAPVDGTVAFLS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 273 STTATNNAAVYYYALFDVPNpDHTLRVAMTTQVTIVLGERKQVLTIPQTALGKKLGeNEYEVTLLKEDDQKETRRIKTGM 352
Cdd:pfam00529 225 VTVDGGTVSAGLRLMFVVPE-DNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKT-GRFTGVVVGISPDTGPVRVVVDK 302
|
330 340
....*....|....*....|
gi 516391317 353 KDDIKVEVVSGLSEQEKVTL 372
Cdd:pfam00529 303 AQGPYYPLRIGLSAGALVRL 322
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
64-90 |
9.33e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 34.31 E-value: 9.33e-03
10 20
....*....|....*....|....*..
gi 516391317 64 AQVSGQVTYLAVEAGQKVKQGDLLAEI 90
Cdd:cd06850 41 APVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
1-377 |
1.61e-106 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 317.87 E-value: 1.61e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 1 MNITPKQRKIALLALVPVLAIGWLAWPS-KAPEPVL-TAEVTRQDVEQTVLASGVLQAIEQVDVGAQVSGQVTYLAVEAG 78
Cdd:PRK11578 1 MKKRKKVKKRYLIALVIVLAGGITLWRIlNAPVPTYqTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 79 QKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQLKIKQAQLKQNELSWRRQQQMFRQEASSRADLESAEAQLAVTRAEL 158
Cdd:PRK11578 81 DKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 159 QGALAEVDNAQIKVERAKTELGYNRIQAPMDGTVVSIVTRQGQTLAASQTVPTLLKLANLETMTVKAQISEADVTRVKAG 238
Cdd:PRK11578 161 GTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 239 MPVYFTLMGDPDTRYHGTLRTVELAPTNINEqatsttatnnaAVYYYALFDVPNPDHTLRVAMTTQVTIVLGERKQVLTI 318
Cdd:PRK11578 241 QKAWFTVLGDPLTRYEGVLKDILPTPEKVND-----------AIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTI 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 516391317 319 PQTALGKKLGENEYEVTLLKEdDQKETRRIKTGMKDDIKVEVVSGLSEQEKVTLNQGSP 377
Cdd:PRK11578 310 PLSALGDPVGDNRYKVKLLRN-GETREREVTIGARNDTDVEIVKGLEAGDEVIIGEAKP 367
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
39-379 |
1.10e-73 |
|
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: 232.14 E-value: 1.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 39 VTRQDVEQTVLASGVLQAIEQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQLKIKQA 118
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 119 QLKqnelswrRQQQMFRQEASSRADLESAEAQLAVtraelqgALAEVDNAQIKVERAKTELGYNRIQAPMDGTVVSIVTR 198
Cdd:COG0845 83 ELE-------RYKALLKKGAVSQQELDQAKAALDQ-------AQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 199 QGQTLAASQtvpTLLKLANLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGTLRTVELAPtnineqatsttatN 278
Cdd:COG0845 149 PGQLVSAGT---PLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAV-------------D 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 279 NAAVYYYALFDVPNPDHTLRVAMTTQVTIVLGERKQVLTIPQTALGKKLGENeyEVTLLKEDDQKETRRIKTGMKDDIKV 358
Cdd:COG0845 213 PATRTVRVRAELPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGGGA--YVFVVDADGKVERRPVTLGRRDGDQV 290
|
330 340
....*....|....*....|....*..
gi 516391317 359 EVVSGLSEQEKV------TLNQGSPVS 379
Cdd:COG0845 291 EVLSGLKAGDRVvvsglqRLRDGAKVR 317
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
34-379 |
3.73e-55 |
|
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: 184.44 E-value: 3.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 34 VLTAEVTRQDVEQTVLASGVLQAIEQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQL 113
Cdd:TIGR01730 1 VTVATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 114 KIKQAQLkqnelswRRQQQMFRQEASSRADLESAEAQLAVTRAELQGALAEVDNAQIkveraktELGYNRIQAPMDGTVV 193
Cdd:TIGR01730 81 ELAQRSF-------ERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQL-------NLRYTEIRAPFDGTIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 194 SIVTRQGQTLAASQTVPTllkLANLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGTLRtvelaptNINEQATS 273
Cdd:TIGR01730 147 RRLVEVGAYVTAGQTLAT---IVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLR-------FIDPRVDS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 274 TTATnnaavyYYALFDVPNPDHTLRVAMTTQVTIVLGERKQVLTIPQTALgkKLGENEYEVTLLKEDDQKETRRIKTGMK 353
Cdd:TIGR01730 217 GTGT------VRVRATFPNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAV--IEDLNGKYVYVVKNDGKVSKRPVEVGLR 288
|
330 340 350
....*....|....*....|....*....|..
gi 516391317 354 DDIKVEVVSGLSEQEKV------TLNQGSPVS 379
Cdd:TIGR01730 289 NGGYVEIESGLKAGDQIvtagvvKLRDGAKVK 320
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1-310 |
1.54e-47 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 164.45 E-value: 1.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 1 MNITPKQRKIALLALVPVLAIGWLAWPSKAPEPVLTAevtrqdveqtvlaSGVLQAiEQVDVGAQVSGQVTYLAVEAGQK 80
Cdd:COG1566 1 MKALKKRRLLALVLLLLALGLALWAAGRNGPDEPVTA-------------DGRVEA-RVVTVAAKVSGRVTEVLVKEGDR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 81 VKQGDLLAEIDPLIAQNNLKTAEADLASRRAQL--------------------KIKQAQLKQNELSWRRQQQMFRQEASS 140
Cdd:COG1566 67 VKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLarleaelgaeaeiaaaeaqlAAAQAQLDLAQRELERYQALYKKGAVS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 141 RADLESAEAQLAVTRAELQGAL--------------------AEVDNAQIKVERAKTELGYNRIQAPMDGTVVSIVTRQG 200
Cdd:COG1566 147 QQELDEARAALDAAQAQLEAAQaqlaqaqaglreeeelaaaqAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 201 QTLAASQTvptLLKLANLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGTLRTVELAptnINEQATSTTATNNA 280
Cdd:COG1566 227 EVVSAGQP---LLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPG---AGFTSPPKNATGNV 300
|
330 340 350
....*....|....*....|....*....|.
gi 516391317 281 AVYYYALFDVPNPD-HTLRVAMTTQVTIVLG 310
Cdd:COG1566 301 VQRYPVRIRLDNPDpEPLRPGMSATVEIDTE 331
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
6-256 |
3.00e-24 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 101.96 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 6 KQRKIALLALVPVLAIGWLAWpskapepvltaEVTRQDVEQTVLASGVlqAIEQVDVGAQVSGQVTYLAVEAGQKVKQGD 85
Cdd:PRK03598 3 KKVVIGLAVVVLAAAVAGGWW-----------WYQSRQDNGLTLYGNV--DIRTVNLGFRVGGRLASLAVDEGDAVKAGQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 86 LLAEIDPLIAQNNLKTAEADLASRRAQL-------------------KIKQAQLKQNELSWRRQQQMFRQEASSRADLES 146
Cdd:PRK03598 70 VLGELDAAPYENALMQAKANVSVAQAQLdlmlagyrdeeiaqaraavKQAQAAYDYAQNFYNRQQGLWKSRTISANDLEN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 147 AEAQLAVTRAELQGAL-------------------AEVDNAQIKVERAKTELGYNRIQAPMDGTVVSIVTRQGQTLAASQ 207
Cdd:PRK03598 150 ARSSRDQAQATLKSAQdklsqyregnrpqdiaqakASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGS 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 516391317 208 TVPTL-LKlanlETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGT 256
Cdd:PRK03598 230 TVFTLsLT----RPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQ 275
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
30-370 |
1.49e-21 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 95.24 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 30 APEPVLTAEVTRQDVEQTVLASGVLQAIEQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASR 109
Cdd:PRK11556 58 PLAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 110 RAQLKIKQAQLKqnelswrRQQQMFRQEASSRADLESAEAQLAVTRAELQGALAEVDNAQIkveraktELGYNRIQAPMD 189
Cdd:PRK11556 138 QATLANARRDLA-------RYQQLAKTNLVSRQELDAQQALVSETEGTIKADEASVASAQL-------QLDYSRITAPIS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 190 GTVVSIVTRQGQTLAASQTVPtLLKLANLETMTVKAQISEADVTRV----KAGMPVYFTLMGDPDTRY--HGTLrtvela 263
Cdd:PRK11556 204 GRVGLKQVDVGNQISSGDTTG-IVVITQTHPIDLVFTLPESDIATVvqaqKAGKPLVVEAWDRTNSKKlsEGTL------ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 264 pTNINEQATSTTATnnaaVYYYALFDvpNPDHTLRVAMTTQVTIVLGERKQVLTIPQTALgkKLGENEYEVTLLKEDDQK 343
Cdd:PRK11556 277 -LSLDNQIDATTGT----IKLKARFN--NQDDALFPNQFVNARMLVDTLQNAVVIPTAAL--QMGNEGHFVWVLNDENKV 347
|
330 340
....*....|....*....|....*..
gi 516391317 344 ETRRIKTGMKDDIKVEVVSGLSEQEKV 370
Cdd:PRK11556 348 SKHLVTPGIQDSQKVVISAGLSAGDRV 374
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
58-256 |
2.70e-18 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 85.08 E-value: 2.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 58 EQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLI-------AQNNLKTAEADLASRR--------------AQLKIK 116
Cdd:PRK10476 47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPyeltvaqAQADLALADAQIMTTQrsvdaersnaasanEQVERA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 117 QAQLKQNELSWRR-----------QQQMFRQEASSR---ADLESAEAQLAVTRA---ELQGALAEVDNAQIKVERAKTEL 179
Cdd:PRK10476 127 RANAKLATRTLERlepllakgyvsAQQVDQARTAQRdaeVSLNQALLQAQAAAAavgGVDALVAQRAAREAALAIAELHL 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516391317 180 GYNRIQAPMDGTVVSIVTRQGQTLAASQTVPTLLklaNLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGT 256
Cdd:PRK10476 207 EDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLI---DTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGK 280
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
41-372 |
8.36e-18 |
|
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: 83.24 E-value: 8.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 41 RQDVEQTVLASGVLQAIEQVD-VGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQLKIKQAQ 119
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 120 LKQNELSWRRQQQMFRQEASSRADLESAEAQLAVTRAELQGALAEVDNAQIKVE------RAKTELGYNRIQApmDGTVV 193
Cdd:pfam00529 81 LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPiggisrESLVTAGALVAQA--QANLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 194 SIVTRQGQTLA-ASQTVPTLLKLANLETMTVKAQISEADVTRVKAgmpvyftlmgdpdtRYHGTLRTVELAPTNINEQAT 272
Cdd:pfam00529 159 ATVAQLDQIYVqITQSAAENQAEVRSELSGAQLQIAEAEAELKLA--------------KLDLERTEIRAPVDGTVAFLS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 273 STTATNNAAVYYYALFDVPNpDHTLRVAMTTQVTIVLGERKQVLTIPQTALGKKLGeNEYEVTLLKEDDQKETRRIKTGM 352
Cdd:pfam00529 225 VTVDGGTVSAGLRLMFVVPE-DNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKT-GRFTGVVVGISPDTGPVRVVVDK 302
|
330 340
....*....|....*....|
gi 516391317 353 KDDIKVEVVSGLSEQEKVTL 372
Cdd:pfam00529 303 AQGPYYPLRIGLSAGALVRL 322
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
43-301 |
7.49e-17 |
|
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: 78.70 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 43 DVEQTVLASGVLQAIE--QVDVGAQVSGQVTYLAVEA-GQKVKQGDLLAEID-PLI--AQNNLktaeadLASRRAQLKIK 116
Cdd:pfam16576 1 PLSRTIRAVGRVAYDErrLAHVHARVEGWIEKLYVNAtGDPVKKGQPLAELYsPELvaAQQEY------LLALRSGDALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 117 QAQLkqnelswrrqqqmfrqeassradLESAEAQLAvtraelqgaLAEVDNAQIK-VERAKTELGYNRIQAPMDGTVVSI 195
Cdd:pfam16576 75 KSEL-----------------------LRAARQRLR---------LLGMPEAQIAeLERTGKVQPTVTVYAPISGVVTEL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 196 VTRQGQTLAASQTvptLLKLANLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGTLrtvelapTNINEQATSTT 275
Cdd:pfam16576 123 NVREGMYVQPGDT---LFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKV-------DYIYPTLDPKT 192
|
250 260
....*....|....*....|....*.
gi 516391317 276 ATNNAAVyyyalfDVPNPDHTLRVAM 301
Cdd:pfam16576 193 RTVRVRI------ELPNPDGRLKPGM 212
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
58-373 |
1.09e-15 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 77.83 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 58 EQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLAsrRAQLKIKQAQLKQNelswrRQQQMFRQE 137
Cdd:PRK09859 60 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLA--KALSTASNARITFN-----RQASLLKTN 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 138 ASSRADLESAeaqlavtRAELQGALAEVDNAQIKVERAKTELGYNRIQAPMDG-------TVVSIVT-RQGQTLAASQTV 209
Cdd:PRK09859 133 YVSRQDYDTA-------RTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGvsgkssvTVGALVTaNQADSLVTVQRL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 210 -PTLLKLAN--LETMTVKAQISEADVTRVKAGMPVYFTLmgDPDTRYHGTlRTVELAPTNINEQATSTTATnnaavyyyA 286
Cdd:PRK09859 206 dPIYVDLTQsvQDFLRMKEEVASGQIKQVQGSTPVQLNL--ENGKRYSQT-GTLKFSDPTVDETTGSVTLR--------A 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 287 LFdvPNPDHTLRVAMTTQVTIVLGERKQVLTIPQTALGKKlGENEYEVTLLKEDDQKETRRIKTGMKDDIKVEVVSGLSE 366
Cdd:PRK09859 275 IF--PNPNGDLLPGMYVTALVDEGSRQNVLLVPQEGVTHN-AQGKATALILDKDDVVQLREIEASKAIGDQWVVTSGLQA 351
|
....*..
gi 516391317 367 QEKVTLN 373
Cdd:PRK09859 352 GDRVIVS 358
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
8-190 |
4.40e-12 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 66.74 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 8 RKIALLALVPVLAIGWL--AWPSKAPEPVLTAEV---TRQDVEQTVLASGVLQAIEQVDVGAQVSGQVTYLAVEAGQKVK 82
Cdd:PRK09578 7 RRLLLAALVALFVLAGCgkGDSDAAAAAPREATVvtvRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 83 QGDLLAEIDPLIAQNNLKTAEADLAsrRAQLKIKQAQLKQnelswRRQQQMFRQEASSRADLESAEAqlavtrAELQgAL 162
Cdd:PRK09578 87 QGAVLFRIDPAPLKAARDAAAGALA--KAEAAHLAALDKR-----RRYDDLVRDRAVSERDYTEAVA------DERQ-AK 152
|
170 180
....*....|....*....|....*...
gi 516391317 163 AEVDNAQIKVERAKTELGYNRIQAPMDG 190
Cdd:PRK09578 153 AAVASAKAELARAQLQLDYATVTAPIDG 180
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
52-373 |
6.25e-12 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 66.66 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 52 GVLQAIEQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQLKIKQaqlkqneLSWRRQQ 131
Cdd:PRK15030 58 GRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQ-------LTVNRYQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 132 QMFRQEASSRADLESAeaqlavtRAELQGALAEVDNAQIKVERAKTELGYNRIQAPMDGTVVSIVTRQGQTLAASQTVpT 211
Cdd:PRK15030 131 KLLGTQYISKQEYDQA-------LADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQAT-A 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 212 LLKLANLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYH-GTLRTVELAPTNINEQATSTTATNNAAVYYYALFdv 290
Cdd:PRK15030 203 LATVQQLDPIYVDVTQSSNDFLRLKQELANGTLKQENGKAKVSlITSDGIKFPQDGTLEFSDVTVDQTTGSITLRAIF-- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 291 PNPDHTLRVAMTTQVTIVLGERKQVLTIPQTALgKKLGENEYEVTLLKEDDQKETRRIKTGMKDDIKVEVVSGLSEQEKV 370
Cdd:PRK15030 281 PNPDHTLLPGMFVRARLEEGLNPNAILVPQQGV-TRTPRGDATVLVVGADDKVETRPIVASQAIGDKWLVTEGLKAGDRV 359
|
...
gi 516391317 371 TLN 373
Cdd:PRK15030 360 VIS 362
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
60-266 |
8.89e-10 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 59.37 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 60 VDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAqlkikQAQLKQNElSWRRQQqmFRQEAS 139
Cdd:PRK10559 48 VAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQV-----LAQEKRRE-AGRRNR--LGVQAM 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 140 SRADLESAEAQLAVTRAELQGALAEVDNAQIKVERAKtelgynrIQAPMDGTVVSIVTRQGQTLAASQTVPTLLKlanLE 219
Cdd:PRK10559 120 SREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTV-------IRAPADGWVTNLNVYTGEFITRGSTAVALVK---QN 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 516391317 220 TMTVKAQISEADVTRVKAGMPVYFTLMGDpDTRYHGTLRTVELAPTN 266
Cdd:PRK10559 190 SFYVLAYMEETKLEGVRPGYRAEITPLGS-NKVLKGTVDSVAAGVTN 235
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
59-255 |
1.65e-09 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 58.94 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 59 QVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLAS---RRAQLKI--KQAQ----LKQNELSwRR 129
Cdd:PRK15136 61 QVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANsvrQTHQLMInsKQYQanieLQKTALA-QA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 130 QQQMFRQEASSRADL-------------ESAEAQLAVTRAELQGALAEVDNA----QIKVERAKTE-------LGYNRIQ 185
Cdd:PRK15136 140 QSDLNRRVPLGNANLigreelqhardavASAQAQLDVAIQQYNANQAMILNTpledQPAVQQAATEvrnawlaLQRTKIV 219
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516391317 186 APMDGTVVSivtRQGQTLAASQTVPTLLKLANLETMTVKAQISEADVTRVKAGMPVYFT--LMGDpDTRYHG 255
Cdd:PRK15136 220 SPMTGYVSR---RSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITsdIYGD-DVVYTG 287
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
183-299 |
1.12e-07 |
|
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: 49.67 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 183 RIQAPMDGTVVSIVTRQGQTLAASQTvptLLKLANLETMTVKAQISEADVTRVKAGMPVYFTLMGDPDTRYHGTLRTVel 262
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDP---LATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRI-- 75
|
90 100 110
....*....|....*....|....*....|....*..
gi 516391317 263 aptnineqATSTTATNNaAVYYYALFDVPNPDHTLRV 299
Cdd:pfam13437 76 --------SPTVDPDTG-VIPVRVSIENPKTPIPLLP 103
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
58-107 |
1.78e-06 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 44.36 E-value: 1.78e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 516391317 58 EQVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLA 107
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| OEP |
pfam02321 |
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ... |
76-175 |
1.18e-04 |
|
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.
Pssm-ID: 396757 [Multi-domain] Cd Length: 181 Bit Score: 42.51 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 76 EAGQKVKQGDLLAEIDPLIAQNNLKTAEADLASRRAQLKIKQAQLKQNELSWRRQQQMFRQEASSRADLESAEAQLAVTR 155
Cdd:pfam02321 80 AAKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLISLLDVLQAEVELLEAR 159
|
90 100
....*....|....*....|
gi 516391317 156 AELQGALAEVDNAQIKVERA 175
Cdd:pfam02321 160 LELLNAEADLELALAQLEQL 179
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
69-169 |
4.79e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 41.95 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 69 QVTYLAVEAGQKVKQGDLLAEIdpliaqnnlKTAEADLASRRAQLKIKQAQLKQNELSWRRQQQMFRQEASSRADLESAE 148
Cdd:COG1538 57 KAQAEAAEADLRAARLDLAAEV---------AQAYFDLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAE 127
|
90 100
....*....|....*....|.
gi 516391317 149 AQLAVTRAELQGALAEVDNAQ 169
Cdd:COG1538 128 AQLAQARAQLAQAEAQLAQAR 148
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
85-179 |
2.69e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 85 DLLAEIDpliaqNNLKT--AEADLASR----RAQLKIKQAQLKQNELSWRRQQQ--MFRQEASSRADLESAEAQLAVTRA 156
Cdd:COG1196 193 DILGELE-----RQLEPleRQAEKAERyrelKEELKELEAELLLLKLRELEAELeeLEAELEELEAELEELEAELAELEA 267
|
90 100
....*....|....*....|...
gi 516391317 157 ELQGALAEVDNAQIKVERAKTEL 179
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEE 290
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
34-175 |
5.97e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 38.48 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516391317 34 VLTAEVTRQDVEQTVLAS------GVLQAIEQVDVgAQVSGQVTYLAVEAGQKVKQGDLLAEIDPLIAQNNLKTAEADLA 107
Cdd:COG1538 60 AEAAEADLRAARLDLAAEvaqayfDLLAAQEQLAL-AEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQARAQLA 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516391317 108 SRRAQLKIKQAQLKQ----NELSWRRQQQMFRQEASSRADLESAEAQLAVTRAELQGALAEVD--NAQIKVERA 175
Cdd:COG1538 139 QAEAQLAQARNALALllglPPPAPLDLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEaaEAEIGVARA 212
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
62-90 |
6.35e-03 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 38.97 E-value: 6.35e-03
10 20
....*....|....*....|....*....
gi 516391317 62 VGAQVSGQVTYLAVEAGQKVKQGDLLAEI 90
Cdd:PRK12999 1079 VGAPMPGSVVTVLVKEGDEVKAGDPLAVI 1107
|
|
| Biotin_lipoyl |
pfam00364 |
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue ... |
59-90 |
7.54e-03 |
|
Biotin-requiring enzyme; This family covers two Prosite entries, the conserved lysine residue binds biotin in one group and lipoic acid in the other. Note that the HMM does not currently recognize the Glycine cleavage system H proteins.
Pssm-ID: 395290 [Multi-domain] Cd Length: 73 Bit Score: 34.88 E-value: 7.54e-03
10 20 30
....*....|....*....|....*....|..
gi 516391317 59 QVDVGAQVSGQVTYLAVEAGQKVKQGDLLAEI 90
Cdd:pfam00364 42 EMEIPAPVAGVVKEILVPEGDTVEVGDPLAKI 73
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
64-90 |
9.33e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 34.31 E-value: 9.33e-03
10 20
....*....|....*....|....*..
gi 516391317 64 AQVSGQVTYLAVEAGQKVKQGDLLAEI 90
Cdd:cd06850 41 APVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
