|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
28-298 |
1.12e-51 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 172.93 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 28 ASGTFEATEVIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTVQLFLQKEQL----------LKNIRSVESNRPDIN--- 94
Cdd:COG1566 37 ADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAeaqlaaaeaqLARLEAELGAEAEIAaae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 95 KQIAATRQQIATAQIEQRRIINLLKSNAANEKQLDDINGQIAVLEKQLKAQESTLQNNSNSITEQS---------SALEI 165
Cdd:COG1566 117 AQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEelaaaqaqvAQAEA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 166 QVAQIEDQLKKCSISSPINGTILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISD-YGDekr 244
Cdd:COG1566 197 ALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDaYPD--- 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2537698814 245 KEYPGIVTWISSQSEFTPKTILTKDeRANLVYAVKIAIKND--GYVKIGMYGEVKF 298
Cdd:COG1566 274 RVFEGKVTSISPGAGFTSPPKNATG-NVVQRYPVRIRLDNPdpEPLRPGMSATVEI 328
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
45-292 |
1.95e-23 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 97.73 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 45 GKIEQLDVEEGTIVTARQKLGYIDtVQLFlqKEQLLKNIRSVESNRPDINKQIAATRQQ-IATA--QIEQR--------- 112
Cdd:PRK03598 52 GRLASLAVDEGDAVKAGQVLGELD-AAPY--ENALMQAKANVSVAQAQLDLMLAGYRDEeIAQAraAVKQAqaaydyaqn 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 113 ---RIINLLKSNAANEKQLDDINGQIAVLEKQLK-AQESTLQ----NNSNSITE---QSSALEIQVAQIEDQLKKCSISS 181
Cdd:PRK03598 129 fynRQQGLWKSRTISANDLENARSSRDQAQATLKsAQDKLSQyregNRPQDIAQakaSLAQAQAALAQAELNLQDTELIA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 182 PINGTILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISDygDEKRKEYPGIVTWISSQSEFT 261
Cdd:PRK03598 209 PSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTD--GRPDKPYHGQIGFVSPTAEFT 286
|
250 260 270
....*....|....*....|....*....|..
gi 2537698814 262 PKTILTKDERANLVYAVKIAIKN-DGYVKIGM 292
Cdd:PRK03598 287 PKTVETPDLRTDLVYRLRIVVTDaDDALRQGM 318
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
27-303 |
3.00e-20 |
|
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: 88.91 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 27 DASGTFEAT-EVIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTVQLFLQKEQLLKNIRSVESnrpdinkqiaatrqQIA 105
Cdd:TIGR01730 16 TFPGSLEAVdEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEA--------------QLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 106 TAQIEQRRIINLLKSNAANEKQLDDINGQIAVLEKQLKAQESTLqnnsnsiteqssaleiqvAQIEDQLKKCSISSPING 185
Cdd:TIGR01730 82 LAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASL------------------ASAQLNLRYTEIRAPFDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 186 TILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISDygDEKRKEYPGIVTWISSQSeftpkti 265
Cdd:TIGR01730 144 TIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELD--ALPGEEFKGKLRFIDPRV------- 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 2537698814 266 ltkdERANLVYAVKIAIKN-DGYVKIGMYGEVKFTSNND 303
Cdd:TIGR01730 215 ----DSGTGTVRVRATFPNpDGRLLPGMFGRVTISLKVR 249
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
28-283 |
1.26e-14 |
|
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: 72.84 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 28 ASGTFEATE--VIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTVQLFLQKEQLLKNIRSVESNR--------------- 90
Cdd:pfam00529 10 APGRVVVSGnaKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVarlqaeldrlqales 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 91 ----------------PDINKQIAATRQQIATAQIEQRRIINLLKSNAANEKQLDDIN--------------GQIAVLEK 140
Cdd:pfam00529 90 elaisrqdydgataqlRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGalvaqaqanllatvAQLDQIYV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 141 QLKAQESTLQ----NNSNSITEQSSALEIQVAQIEDQLKKCSISSPINGTIltKYAEA---GELANTGKPLFKVADIENM 213
Cdd:pfam00529 170 QITQSAAENQaevrSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTV--AFLSVtvdGGTVSAGLRLMFVVPEDNL 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2537698814 214 YLRAYITSVQLSQVKVGQKVTVISD-YGDEKRKEYPGIVTWISSQSEFTPKTILTKDERanlVYAVKIAIK 283
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDaFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGP---YYPLRIGLS 315
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
28-298 |
1.12e-51 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 172.93 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 28 ASGTFEATEVIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTVQLFLQKEQL----------LKNIRSVESNRPDIN--- 94
Cdd:COG1566 37 ADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAeaqlaaaeaqLARLEAELGAEAEIAaae 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 95 KQIAATRQQIATAQIEQRRIINLLKSNAANEKQLDDINGQIAVLEKQLKAQESTLQNNSNSITEQS---------SALEI 165
Cdd:COG1566 117 AQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEelaaaqaqvAQAEA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 166 QVAQIEDQLKKCSISSPINGTILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISD-YGDekr 244
Cdd:COG1566 197 ALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDaYPD--- 273
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2537698814 245 KEYPGIVTWISSQSEFTPKTILTKDeRANLVYAVKIAIKND--GYVKIGMYGEVKF 298
Cdd:COG1566 274 RVFEGKVTSISPGAGFTSPPKNATG-NVVQRYPVRIRLDNPdpEPLRPGMSATVEI 328
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
27-299 |
2.20e-38 |
|
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: 137.77 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 27 DASGTFEA-TEVIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTVQLFLQKEQLlknirsvesnrpdiNKQIAATRQQIA 105
Cdd:COG0845 13 EATGTVEArREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQA--------------QAQLAAAQAQLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 106 TAQIEQRRIINLLKSNAANEKQLDDINGQIAVLEKQLKAQEStlqnnsnsiteqssaleiQVAQIEDQLKKCSISSPING 185
Cdd:COG0845 79 LAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQA------------------ALEQARANLAYTTIRAPFDG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 186 TILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISDYGDEkrKEYPGIVTWISSQseFTPKTi 265
Cdd:COG0845 141 VVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPG--KTFEGKVTFIDPA--VDPAT- 215
|
250 260 270
....*....|....*....|....*....|....*
gi 2537698814 266 ltkdeRAnlvYAVKIAIKN-DGYVKIGMYGEVKFT 299
Cdd:COG0845 216 -----RT---VRVRAELPNpDGLLRPGMFVRVRIV 242
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
45-292 |
1.95e-23 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 97.73 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 45 GKIEQLDVEEGTIVTARQKLGYIDtVQLFlqKEQLLKNIRSVESNRPDINKQIAATRQQ-IATA--QIEQR--------- 112
Cdd:PRK03598 52 GRLASLAVDEGDAVKAGQVLGELD-AAPY--ENALMQAKANVSVAQAQLDLMLAGYRDEeIAQAraAVKQAqaaydyaqn 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 113 ---RIINLLKSNAANEKQLDDINGQIAVLEKQLK-AQESTLQ----NNSNSITE---QSSALEIQVAQIEDQLKKCSISS 181
Cdd:PRK03598 129 fynRQQGLWKSRTISANDLENARSSRDQAQATLKsAQDKLSQyregNRPQDIAQakaSLAQAQAALAQAELNLQDTELIA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 182 PINGTILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISDygDEKRKEYPGIVTWISSQSEFT 261
Cdd:PRK03598 209 PSDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTD--GRPDKPYHGQIGFVSPTAEFT 286
|
250 260 270
....*....|....*....|....*....|..
gi 2537698814 262 PKTILTKDERANLVYAVKIAIKN-DGYVKIGM 292
Cdd:PRK03598 287 PKTVETPDLRTDLVYRLRIVVTDaDDALRQGM 318
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
27-303 |
3.00e-20 |
|
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: 88.91 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 27 DASGTFEAT-EVIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTVQLFLQKEQLLKNIRSVESnrpdinkqiaatrqQIA 105
Cdd:TIGR01730 16 TFPGSLEAVdEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEA--------------QLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 106 TAQIEQRRIINLLKSNAANEKQLDDINGQIAVLEKQLKAQESTLqnnsnsiteqssaleiqvAQIEDQLKKCSISSPING 185
Cdd:TIGR01730 82 LAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASL------------------ASAQLNLRYTEIRAPFDG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 186 TILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISDygDEKRKEYPGIVTWISSQSeftpkti 265
Cdd:TIGR01730 144 TIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELD--ALPGEEFKGKLRFIDPRV------- 214
|
250 260 270
....*....|....*....|....*....|....*....
gi 2537698814 266 ltkdERANLVYAVKIAIKN-DGYVKIGMYGEVKFTSNND 303
Cdd:TIGR01730 215 ----DSGTGTVRVRATFPNpDGRLLPGMFGRVTISLKVR 249
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
28-283 |
1.26e-14 |
|
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: 72.84 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 28 ASGTFEATE--VIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTVQLFLQKEQLLKNIRSVESNR--------------- 90
Cdd:pfam00529 10 APGRVVVSGnaKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVarlqaeldrlqales 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 91 ----------------PDINKQIAATRQQIATAQIEQRRIINLLKSNAANEKQLDDIN--------------GQIAVLEK 140
Cdd:pfam00529 90 elaisrqdydgataqlRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGalvaqaqanllatvAQLDQIYV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 141 QLKAQESTLQ----NNSNSITEQSSALEIQVAQIEDQLKKCSISSPINGTIltKYAEA---GELANTGKPLFKVADIENM 213
Cdd:pfam00529 170 QITQSAAENQaevrSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTV--AFLSVtvdGGTVSAGLRLMFVVPEDNL 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2537698814 214 YLRAYITSVQLSQVKVGQKVTVISD-YGDEKRKEYPGIVTWISSQSEFTPKTILTKDERanlVYAVKIAIK 283
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDaFPQTKTGRFTGVVVGISPDTGPVRVVVDKAQGP---YYPLRIGLS 315
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
179-294 |
9.12e-13 |
|
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: 63.54 E-value: 9.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 179 ISSPINGTILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISDygDEKRKEYPGIVTWISSqs 258
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLD--PGSDYTLEGKVVRISP-- 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 2537698814 259 eftpktILTKDERanlVYAVKIAIKNDGYVKIGMYG 294
Cdd:pfam13437 78 ------TVDPDTG---VIPVRVSIENPKTPIPLLPG 104
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
46-282 |
9.60e-13 |
|
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: 67.54 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 46 KIEQLDVEEGTIVTARQKLGYIDTV----QLFLQKEQLLKNIRSVESNRPDINKQIAATRQQIA---------------- 105
Cdd:TIGR02971 26 RIKKLLVAEGDRVQAGQVLAELDSRpertAELDVARTQLDEAKARLAQVRAGAKKGEIAAQRAAraaaklfkdvaaqqat 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 106 ---------TAQIEQRRIINLLKSNAANEKQLDDINGQIAVLEKQLKA-------QESTLQNNSNSITEQSSALEIQVAQ 169
Cdd:TIGR02971 106 lnrleaeleTAQREVDRYRSLFRDGAVSASDLDSKALKLRTAEEELEEalasrseQIDGARAALASLAEEVRETDVDLAQ 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 170 IEDQ------------LKKCSISSPINGTILTKYAEAGELANTgKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVIS 237
Cdd:TIGR02971 186 AEVKsaleavqqaealLELTYVKAPIDGRVLKIHAREGEVIGS-EGILEMGDTSQMYAVAEVYETDINRVRVGQRATITS 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2537698814 238 dygDEKRKEYPGIVTWISSQseFTPKTILTKDERANL---VYAVKIAI 282
Cdd:TIGR02971 265 ---TALSGPLRGTVRRIGSL--IAKNDVLSTDPAADAdarVVEVKIRL 307
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
23-293 |
1.61e-10 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 59.83 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 23 SDNMDASGTFEATE---VIVSAEANGKIEQLDV-EEGTIVTARQKLGYIDTVQLFLQKEQLLKNIRSVESNRPDinKQIA 98
Cdd:pfam16576 3 SRTIRAVGRVAYDErrlAHVHARVEGWIEKLYVnATGDPVKKGQPLAELYSPELVAAQQEYLLALRSGDALSKS--ELLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 99 ATRQQIataqieqrriinllksnaaneKQLDDINGQIAVLEKQLKAQEStlqnnsnsITeqssaleiqvaqiedqlkkcs 178
Cdd:pfam16576 81 AARQRL---------------------RLLGMPEAQIAELERTGKVQPT--------VT--------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 179 ISSPINGTILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVISDYGDEKRkeYPGIVTWISSQS 258
Cdd:pfam16576 111 VYAPISGVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKT--FEGKVDYIYPTL 188
|
250 260 270
....*....|....*....|....*....|....*.
gi 2537698814 259 EftPKTILTKderanlvyaVKIAIKN-DGYVKIGMY 293
Cdd:pfam16576 189 D--PKTRTVR---------VRIELPNpDGRLKPGMF 213
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
75-252 |
2.14e-08 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 54.70 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 75 QKEQLLKNIRSVESNrpdinkqIAATRQQIATAQIEQRRIINLLKSNAANEKQLDDINGQIAVLEKQLKAqeSTLQNNSN 154
Cdd:PRK15136 114 QTHQLMINSKQYQAN-------IELQKTALAQAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQLDV--AIQQYNAN 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 155 SIT------EQSSALEIQVAQIED---QLKKCSISSPINGTILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLS 225
Cdd:PRK15136 185 QAMilntplEDQPAVQQAATEVRNawlALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLA 264
|
170 180
....*....|....*....|....*...
gi 2537698814 226 QVKVGQKVTVISD-YGDEkrKEYPGIVT 252
Cdd:PRK15136 265 NMRIGQPATITSDiYGDD--VVYTGKVV 290
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
29-237 |
2.93e-07 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 51.18 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 29 SGTFEATEVIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTV-----------QLFLQKEQLLKNIRSV---ESNRPDIN 94
Cdd:PRK10476 41 DAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRpyeltvaqaqaDLALADAQIMTTQRSVdaeRSNAASAN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 95 KQIAATRQQIATAQIEQRRIINLLKSNAANEKQLDDI-----NGQIAVLEKQLKAQES-TLQNNSNSITEQSSALEIQVA 168
Cdd:PRK10476 121 EQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQArtaqrDAEVSLNQALLQAQAAaAAVGGVDALVAQRAAREAALA 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2537698814 169 QIEDQLKKCSISSPINGTILTKYAEAGELANTGKPLFKVADIENMYLRAYITSVQLSQVKVGQKVTVIS 237
Cdd:PRK10476 201 IAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYS 269
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
83-176 |
4.07e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 83 IRSVESNRPDINKQIAATRQQIATAQIEQRRIINLLKsnaANEKQLDDINGQIAVLEKQLKAQESTLQNNSNSITEQSSA 162
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA---ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90
....*....|....
gi 2537698814 163 LEIQVAQIEDQLKK 176
Cdd:COG4942 99 LEAQKEELAELLRA 112
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
48-171 |
8.88e-05 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 43.69 E-value: 8.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 48 EQLDVEEGTIVTARQKLgyidtvQLFLQKEQLLKNIRSVESnrpdINKQIAATRQQIATAQIEqrriINLLKSNAA-NEK 126
Cdd:COG3524 184 EEVERAEERLRDAREAL------LAFRNRNGILDPEATAEA----LLQLIATLEGQLAELEAE----LAALRSYLSpNSP 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2537698814 127 QLDDINGQIAVLEKQLKAQESTL--QNNSNSITEQSSalEIQVAQIE 171
Cdd:COG3524 250 QVRQLRRRIAALEKQIAAERARLtgASGGDSLASLLA--EYERLELE 294
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
75-163 |
4.44e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 75 QKEQLLKNIRSVESNRPDINKQIAATRQQIATAQieqRRIINLLKSNAANEKQLDDINGQIAVLEKQLKAQESTLQNNSN 154
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALE---RRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
....*....
gi 2537698814 155 SITEQSSAL 163
Cdd:COG4942 105 ELAELLRAL 113
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
37-176 |
8.14e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 37 VIVSAEANGKIEQLDVEEGTIVTARQKLgyidtVQLFLQKEQLLKNIRSVESNRPDI--NKQIAATRQQIATAQieqRRI 114
Cdd:COG3206 208 VDLSEEAKLLLQQLSELESQLAEARAEL-----AEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELE---AEL 279
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2537698814 115 INLLKSNAANEKQLDDINGQIAVLEKQLKAQE----STLQNNSNSITEQSSALEIQVAQIEDQLKK 176
Cdd:COG3206 280 AELSARYTPNHPDVIALRAQIAALRAQLQQEAqrilASLEAELEALQAREASLQAQLAQLEARLAE 345
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
85-174 |
1.43e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 85 SVESNRPDINKQIAatrQQIATAQIEQrriiNLLKSNAANEKQLDDINGQIAVLEKQLKAQESTL-----QNNSNSITEQ 159
Cdd:COG3206 141 SYTSPDPELAAAVA---NALAEAYLEQ----NLELRREEARKALEFLEEQLPELRKELEEAEAALeefrqKNGLVDLSEE 213
|
90
....*....|....*
gi 2537698814 160 SSALEIQVAQIEDQL 174
Cdd:COG3206 214 AKLLLQQLSELESQL 228
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
37-84 |
1.79e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 35.88 E-value: 1.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2537698814 37 VIVSAEANGKIEQLDVEEGTIVTARQKLGYIDTVQLFLQKEQLLKNIR 84
Cdd:pfam13533 3 VKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
75-177 |
3.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 75 QKEQLLKNIRSVESNRPDINKQIAATRQQIATAQIEQRRIINLLKSN-------------AANEKQLDDI---NGQIAVL 138
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaereiAELEAELERLdasSDDLAAL 690
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2537698814 139 EKQLKAQES---TLQNNSNSITEQSSALEIQVAQIEDQLKKC 177
Cdd:COG4913 691 EEQLEELEAeleELEEELDELKGEIGRLEKELEQAEEELDEL 732
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
41-191 |
6.24e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.21 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 41 AEANGKIEQLDVE----EGTIVTARQKLGyidtvqlflQKEQLLKNIRSvesnrpdiNKQIAATRQQIATAQieqRRIIN 116
Cdd:COG1579 48 EAAKTELEDLEKEikrlELEIEEVEARIK---------KYEEQLGNVRN--------NKEYEALQKEIESLK---RRISD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 117 LlksnaanEKQLDDINGQIAVLEKQLKAQESTLQNNSNSITEQSSALEIQVAQIEDQLKKCS-----ISSPINGTILTKY 191
Cdd:COG1579 108 L-------EDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEaereeLAAKIPPELLALY 180
|
|
| DUF4349 |
pfam14257 |
Domain of unknown function (DUF4349); This family of proteins is found in bacteria and archaea. ... |
27-144 |
7.80e-03 |
|
Domain of unknown function (DUF4349); This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 282 and 353 amino acids in length. There is a single completely conserved residue D that may be functionally important. The N-terminus contains a lipoprotein signal peptide sequence.
Pssm-ID: 464117 [Multi-domain] Cd Length: 213 Bit Score: 36.76 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 27 DASGTFEATEVIVsAEANGKIEQLDVEEGTIVTARQKLgyidTV-------QLFLQKEQLLKNIRSVESNRPDINKQIAA 99
Cdd:pfam14257 15 DVDAAAASVRAIV-EEAGGYVESSSTSGTDGGERSASL----TLrvpadrfDAFLDELAGLGTVTSRSISAEDVTEQYVD 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2537698814 100 TRQQIATAQIEQRRIINLLkSNAAN-------EKQLDDINGQIAVLEKQLKA 144
Cdd:pfam14257 90 LEARLKALRASEDRLLALL-ERAGSvedllavERELSEVQAELESLEGQLRY 140
|
|
| HlyD_2 |
pfam12700 |
HlyD family secretion protein; This family is related to pfam00529. |
132-238 |
8.24e-03 |
|
HlyD family secretion protein; This family is related to pfam00529.
Pssm-ID: 403792 [Multi-domain] Cd Length: 413 Bit Score: 37.49 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2537698814 132 NGQIAVLEKQLKAQESTLQNNSNSI-TEQSSALEIQVAQIEDQL---KKCSISSPINGTILTKYAEA-GELANTGKPLFK 206
Cdd:pfam12700 178 GKDLEALKKKKKEIENKLESNKVTIkAPISGVLSYYIDGYEEIFssdNLDKIDSKDLNSIENNNIDIdKKDVNKGDPIFK 257
|
90 100 110
....*....|....*....|....*....|..
gi 2537698814 207 VADIENMYLRAYITSVQLSQVKVGQKVTVISD 238
Cdd:pfam12700 258 IINNHVWYLATEVEKEDVKSFKEGKKVYIKVD 289
|
|
| |
