|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
44-364 |
2.58e-79 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 246.11 E-value: 2.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 44 WWFLTRN---EETTDDAFTDGDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLGLAIAQLHQA 120
Cdd:COG1566 23 LWAAGRNgpdEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLARL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 121 QAQLALskvqyPAQRDEAKAQVLKAQADLANAQAEY-RRQRGVDPRATTQQSIDSANAQLRSAQAALASAQAQlevAEQV 199
Cdd:COG1566 103 EAELGA-----EAEIAAAEAQLAAAQAQLDLAQRELeRYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQ---LAQA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 200 QLQIRQQETNVEArERQVEQAKAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKES 278
Cdd:COG1566 175 QAGLREEEELAAA-QAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDdLWVEAYVPET 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 279 QLERMKPGDKVTVSVDAWPDMELEGHVDSIQQGSGsrfSAFPAENATGNfvkIVQRVPVKIVIDKGLDPnkPLPLGLSVA 358
Cdd:COG1566 254 DLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAG---FTSPPKNATGN---VVQRYPVRIRLDNPDPE--PLRPGMSAT 325
|
....*.
gi 504696010 359 PKVTVE 364
Cdd:COG1566 326 VEIDTE 331
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
44-356 |
4.48e-73 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 230.45 E-value: 4.48e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 44 WWFLTRNE-ETTDDAFTDGDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLGLAIAQLHQAQA 122
Cdd:TIGR00998 22 YWFLVLRDyESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAELALAKAEANLAALVRQTKQLEI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 123 QLAlskvQYPAQRDEAKAQVLKAQADLANAQAEYRR-----QRGVDPRATTQQSID---SANAQLrsaqaalasaqaqlE 194
Cdd:TIGR00998 102 TVQ----QLQAKVESLKIKLEQAREKLLQAELDLRRrvplfKKGLISREELDHARKallSAKAAL--------------N 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 195 VAEQVQLQIRQQETNVEA--RERQVEQAKAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSP-NVWV 271
Cdd:TIGR00998 164 AAIQEQLNANQALVRGTPlkKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPAeQMYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 272 VANFKESQLERMKPGDKVTVSVDAWP-DMELEGHVDSIQQGSGSRFSAFPAENATGNFVKIVQRVPVKIVIDKGLDPNKP 350
Cdd:TIGR00998 244 EANFKETQLKNVRIGQPVTIRSDLYGsDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKELDEHP 323
|
....*.
gi 504696010 351 LPLGLS 356
Cdd:TIGR00998 324 LRIGLS 329
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
44-364 |
5.74e-52 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 177.19 E-value: 5.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 44 WWFLT-RNEETTDDAFTDGDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLGLAIAQLHQaqa 122
Cdd:PRK15136 41 YWFLVlRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQ--- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 123 QLALSKvQYPAQRDEAKAQVLKAQADL--------ANAQAEYRRQRgvdpratTQQSIDSANAQLrsaqaalasaqaqlE 194
Cdd:PRK15136 118 LMINSK-QYQANIELQKTALAQAQSDLnrrvplgnANLIGREELQH-------ARDAVASAQAQL--------------D 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 195 VAEQvQLQIRQQ---ETNVEaRERQVEQAKAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLV-SPNVW 270
Cdd:PRK15136 176 VAIQ-QYNANQAmilNTPLE-DQPAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTTPLMAVVpATNLW 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 271 VVANFKESQLERMKPGDKVTVSVDAW-PDMELEGHVDSIQQGSGSRFSAFPAENATGNFVKIVQRVPVKIVIDKGLDPNK 349
Cdd:PRK15136 254 VDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQH 333
|
330
....*....|....*
gi 504696010 350 PLPLGLSVapKVTVE 364
Cdd:PRK15136 334 PLRIGLST--LVTVD 346
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
53-343 |
1.34e-46 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 161.73 E-value: 1.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 53 TTDDAFTDGDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLGLaiaqlhqAQAQLALSKVQYP 132
Cdd:PRK10476 38 STDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLAL-------ADAQIMTTQRSVD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 133 AQR---DEAKAQVLKAQADLANAQAEYRRQRGVDPRA-TTQQSIDSANAQLRSAQAALasaqaqlevaEQVQLQIRQQET 208
Cdd:PRK10476 111 AERsnaASANEQVERARANAKLATRTLERLEPLLAKGyVSAQQVDQARTAQRDAEVSL----------NQALLQAQAAAA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 209 ---NVEARERQVEQAKAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPNVW-VVANFKESQLERMK 284
Cdd:PRK10476 181 avgGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWyAIANFRETDLKNIR 260
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696010 285 PGDKVTVSVDAWPDMELEGHVDSIQQG-----SGSRFSAFPAENATGNFVKIVQRVPVKIVIDK 343
Cdd:PRK10476 261 VGDCATVYSMIDRGRPFEGKVDSIGWGvlpddGGNVPRGLPYVPRSINWVRVAQRFPVRIMLDK 324
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
62-357 |
2.53e-45 |
|
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: 157.80 E-value: 2.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 62 DVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLglaiaqlhqaqaqlalskvqypaqrdeakaq 141
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQL------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 142 vLKAQADLANAQAEYRRQRG-VDPRATTQQSIDSANAQLrsaqaalasaqaqlevaeqvqlqirqqetnvEARERQVEQA 220
Cdd:COG0845 71 -AAAQAQLELAKAELERYKAlLKKGAVSQQELDQAKAAL-------------------------------DQAQAALAAA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 221 KAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLERMKPGDKVTVSVDAWPDM 299
Cdd:COG0845 119 QAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDpLEVEFDVPESDLARLKVGQPVTVTLDAGPGK 198
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 504696010 300 ELEGHVDSIQQGsgsrfsafpAENATGNFvkivqrvPVKIVIDkglDPNKPLPLGLSV 357
Cdd:COG0845 199 TFEGKVTFIDPA---------VDPATRTV-------RVRAELP---NPDGLLRPGMFV 237
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
47-315 |
1.26e-39 |
|
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: 142.95 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 47 LTRNEETTDDAFTDGDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLGLAIAQLHQAQA---- 122
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAeldr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 123 ---------QLALSKVQYPAQRDEAKAQVLKAQADLANAQAEYRRQRGVDPR-ATTQQSIDSANAQLRSA-----QAALA 187
Cdd:pfam00529 84 lqaleselaISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIgGISRESLVTAGALVAQAqanllATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 188 SAQAQLEVAEQVQLQIRQQETNVEARERQVEQAKAQLETANLNLSYTEVRAPFDGFVTKRNVQP-GTLVQAGTALFSLVS 266
Cdd:pfam00529 164 LDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVP 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 504696010 267 PN-VWVVANFKESQLERMKPGDKVTVSVDAWPD---MELEGHVDSIQQGSGSR 315
Cdd:pfam00529 244 EDnLLVPGMFVETQLDQVRVGQPVLIPFDAFPQtktGRFTGVVVGISPDTGPV 296
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
61-308 |
9.56e-33 |
|
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: 124.35 E-value: 9.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 61 GDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDttaqrdqAQAQLGLAIAQLHQAQAQLALSKVQYPaqrdeaka 140
Cdd:TIGR01730 24 VDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDD-------YQLALQAALAQLAAAEAQLELAQRSFE-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 141 qvlkaqadlanaqaeyRRQRGVDPRATTQQSIDSANAQlrsaqaalasaqaqlevaeqvqlqirqqetnVEARERQVEQA 220
Cdd:TIGR01730 89 ----------------RAERLVKRNAVSQADLDDAKAA-------------------------------VEAAQADLEAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 221 KAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLERMKPGDKVTVSVDAWPDM 299
Cdd:TIGR01730 122 KASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDpLEADFSVPERDLPQLRRGQTLTVELDALPGE 201
|
....*....
gi 504696010 300 ELEGHVDSI 308
Cdd:TIGR01730 202 EFKGKLRFI 210
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
44-305 |
2.94e-28 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 112.36 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 44 WWFLTRNeettDDAFT-DGDV----VTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDprDTTAQRDQAQAQlglaiAQLH 118
Cdd:PRK03598 23 WWYQSRQ----DNGLTlYGNVdirtVNLGFRVGGRLASLAVDEGDAVKAGQVLGELD--AAPYENALMQAK-----ANVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 119 QAQAQLALSKVQY-PAQRDEAKAQVLKAQADLANAQAEYRRQRGVDP-RATTQQSIDSANAQlrsAQAALASAQAQLEVA 196
Cdd:PRK03598 92 VAQAQLDLMLAGYrDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLWKsRTISANDLENARSS---RDQAQATLKSAQDKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 197 EQVQLQIRQQEtnVEARERQVEQAKAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALF--SLVSPnVWVVAN 274
Cdd:PRK03598 169 SQYREGNRPQD--IAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLNAGSTVFtlSLTRP-VWVRAY 245
|
250 260 270
....*....|....*....|....*....|.
gi 504696010 275 FKESQLERMKPGDKVTVSVDAWPDMELEGHV 305
Cdd:PRK03598 246 VDERNLGQAQPGRKVLLYTDGRPDKPYHGQI 276
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
44-364 |
3.74e-27 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 109.06 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 44 WWFLTRNEETTDDAFTdGDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDprdttaqrdqaqaqlglaiaqlhQAQAQ 123
Cdd:PRK10559 29 WVFYTESPWTRDARFS-ADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTID-----------------------QPRYQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 124 LALskvqypaqrDEAKAQVLKAQADLANAQAEYRRQRGVDPRATTQQSIDSANAQLrsaqaalasaqaqlevaeqvqlqi 203
Cdd:PRK10559 85 KAL---------AEAEADVAYYQVLAQEKRREAGRRNRLGVQAMSREEIDQANNVL------------------------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 204 rqqetnvEARERQVEQAKAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLER 282
Cdd:PRK10559 132 -------QTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNsFYVLAYMEETKLEG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 283 MKPGDKVTVSvdawP---DMELEGHVDSIQQG----SGSRFSAFPAE-NATGNFVKIVQRVPVKIVIDKglDPNKPLPLG 354
Cdd:PRK10559 205 VRPGYRAEIT----PlgsNKVLKGTVDSVAAGvtnsSSTRDSKGMATiDSNLEWVRLAQRVPVRIRLDN--QQGNLYPAG 278
|
330
....*....|
gi 504696010 355 LSVAPKVTVE 364
Cdd:PRK10559 279 TTATVVITGK 288
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
62-308 |
4.43e-20 |
|
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: 87.18 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 62 DVVTIAPKTAGYVTGLHVRDN-QRVKKGDLLVVID-Prdttaqrdqaqaqlglaiaqlhqaqaqlalskvqypaqrdeak 139
Cdd:pfam16576 18 RLAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYsP------------------------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 140 aqvlkaqaDLANAQAEYRRQRGVDPRATTQQSIDSANAQLRsaqaalasaqaqlevaeqvQLQIRQQETNVEARERQVEQ 219
Cdd:pfam16576 55 --------ELVAAQQEYLLALRSGDALSKSELLRAARQRLR-------------------LLGMPEAQIAELERTGKVQP 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 220 akaqletanlnlsYTEVRAPFDGFVTKRNVQPGTLVQAGTALFSLVS-PNVWVVANFKESQLERMKPGDKVTVSVDAWPD 298
Cdd:pfam16576 108 -------------TVTVYAPISGVVTELNVREGMYVQPGDTLFTIADlSTVWVEADVPEQDLALVKVGQPAEVTLPALPG 174
|
250
....*....|
gi 504696010 299 MELEGHVDSI 308
Cdd:pfam16576 175 KTFEGKVDYI 184
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
64-309 |
9.95e-14 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 71.73 E-value: 9.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 64 VTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLGLAIAQLHQAQAQLALSKVQYPAQRDEAKAQvl 143
Cdd:PRK11578 62 VDVGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQ-- 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 144 kaqadlanaqaeyrrqrgvdprATTQQSIDSAnaqlrsaqaalasaqaqlevaeQVQLQIRQQEtnVEARERQVEQAKAQ 223
Cdd:PRK11578 140 ----------------------AVSQQDLDTA----------------------ATELAVKQAQ--IGTIDAQIKRNQAS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 224 LETANLNLSYTEVRAPFDGFVTKRnvqpgTLVQAGTALFSLVSPNV---------WVVANFKESQLERMKPGDKVTVSVD 294
Cdd:PRK11578 174 LDTAKTNLDYTRIVAPMAGEVTQI-----TTLQGQTVIAAQQAPNIltladmstmLVKAQVSEADVIHLKPGQKAWFTVL 248
|
250
....*....|....*
gi 504696010 295 AWPDMELEGHVDSIQ 309
Cdd:PRK11578 249 GDPLTRYEGVLKDIL 263
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
235-322 |
1.58e-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: 65.85 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 235 EVRAPFDGFVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLERMKPGDKVTVSVDAWPDMELEGHVDSIQQGSG 313
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDrLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVD 80
|
....*....
gi 504696010 314 SRFSAFPAE 322
Cdd:pfam13437 81 PDTGVIPVR 89
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
62-110 |
1.89e-10 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 55.53 E-value: 1.89e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 504696010 62 DVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQL 110
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQL 49
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
59-364 |
8.48e-10 |
|
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: 59.64 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 59 TDGDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLGLAIAQLHQAQA---------------- 122
Cdd:TIGR01843 39 PSGNVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAEVARLRAeadsqaaiefpddlls 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 123 --------QLALSKVQYPAQRDE-----------------------AKAQVLKAQADLANAQAEYRRQ---RGVDPRATT 168
Cdd:TIGR01843 119 aedpavpeLIKGQQSLFESRKSTlraqlelilaqikqleaelaglqAQLQALRQQLEVISEELEARRKlkeKGLVSRLEL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 169 ---QQSIDSANAQL-RSAQAALASAQAQLEVAEQVQLQI--RQQETNVEARERQVE--QAKAQLETANLNLSYTEVRAPF 240
Cdd:TIGR01843 199 lelERERAEAQGELgRLEAELEVLKRQIDELQLERQQIEqtFREEVLEELTEAQARlaELRERLNKARDRLQRLIIRSPV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 241 DGFV-TKRNVQPGTLVQAGTALFSLVSPNV--WVVANFKESQLERMKPGDKVTVSVDAWPDME---LEGHVDSIQQgsgs 314
Cdd:TIGR01843 279 DGTVqSLKVHTVGGVVQPGETLMEIVPEDDplEIEAKLSPKDIGFVHVGQPAEIKFSAFPYRRygiLNGKVKSISP---- 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 504696010 315 rfSAFPAENATGNFVKIVQRVPVKIVIDKgldpnkplPLGLSVAPKVTVE 364
Cdd:TIGR01843 355 --DTFTDERGGGPYYRVRISIDQNTLGIG--------PKGLELSPGMPVT 394
|
|
| 8a0102 |
TIGR00999 |
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, ... |
83-308 |
2.72e-09 |
|
Membrane Fusion Protein cluster 2 (function with RND porters); [Transport and binding proteins, Other]
Pssm-ID: 273386 [Multi-domain] Cd Length: 265 Bit Score: 57.45 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 83 QRVKKGDLLVVIDPrdttaqrdqaqAQLGLAIAQLHQAQAQLALSKVQYpaqrdEAKAQVLkaqadlanaqaeyrrQRGV 162
Cdd:TIGR00999 2 DPVKKGQVLAVVDS-----------PELAKMAAELKVAQKRVELARKTY-----EREKKLF---------------EQGV 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 163 dpraTTQQSIDSANAQLrsaqaalasaqaqlEVAEQvqlqirqqetnvearERQVEQAKAQLETANLNLSYTEVRAPFDG 242
Cdd:TIGR00999 51 ----IPRQEFESAEYAL--------------EEAQA---------------EVQAAKSELRSAREAKDGSYVEVRSPFDG 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504696010 243 FVTKRNVQPGTLVQAGTALFSLVSPN-VWVVANFKESQLERMKPGDKVTVSVDAwpDMELEGHVDSI 308
Cdd:TIGR00999 98 YITQKSVTLGDYVAPQAELFRVADLGaVWVEAEVPAKDVSRIRKGSKATVLLEN--GRPLPARVDYV 162
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
59-260 |
7.49e-09 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 56.72 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 59 TDGDVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPRdttaqrdqaQAQLGLAiaqlhQAQAQLAlskvqypaqrdea 138
Cdd:PRK11556 83 TAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPR---------PFKVALA-----QAQGQLA------------- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 139 kaqvlKAQADLANAQAEYRR-QRGVDPRATTQQSIDSANAqlrsaqaalasaqaqlevaeqvqlQIRQQETNVEARERQV 217
Cdd:PRK11556 136 -----KDQATLANARRDLARyQQLAKTNLVSRQELDAQQA------------------------LVSETEGTIKADEASV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504696010 218 EQAKaqletanLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTA 260
Cdd:PRK11556 187 ASAQ-------LQLDYSRITAPISGRVGLKQVDVGNQISSGDT 222
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
69-160 |
5.98e-06 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 47.87 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 69 KTAGYVTGLHVRDNQRVKKGDLLVVIDPRDTTAQRDQAQAQLGLAIAQLHQAQAQLA----LSKVQYPAQRD--EAKAQV 142
Cdd:PRK09578 69 RVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRryddLVRDRAVSERDytEAVADE 148
|
90
....*....|....*...
gi 504696010 143 LKAQADLANAQAEYRRQR 160
Cdd:PRK09578 149 RQAKAAVASAKAELARAQ 166
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
131-260 |
7.44e-06 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 47.40 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 131 YPAQRDEAKAQVLKAQADLANAQAEYRR-QRGVDPRATTQQSIDSANAQlrsaqaalasaqaqlevaeqvqlqirQQETN 209
Cdd:PRK15030 101 YQATYDSAKGDLAKAQAAANIAQLTVNRyQKLLGTQYISKQEYDQALAD--------------------------AQQAN 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504696010 210 VearerQVEQAKAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTA 260
Cdd:PRK15030 155 A-----AVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQA 200
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
97-227 |
1.61e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 97 RDTTAQRDQAQAQLGLAIAQLHQAQAQLALSKvqypAQRDEAKAQVLKAQADLANAQAEYRRQRGVdpRATTQQSIDSAN 176
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELE----AELEELRLELEELELELEEAQAEEYELLAE--LARLEQDIARLE 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 504696010 177 AQLRSAQAALASAQAQLEVAEQVQLQIRQQETNVEARERQVEQAKAQLETA 227
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
62-260 |
4.06e-05 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 45.09 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 62 DVVTIAPKTAGYVTGLHVRDNQRVKKGDLLVVIDPrdttaqrdqaqaqlglaiaqlhqAQAQLALskvqypaqrDEAKAQ 141
Cdd:PRK09859 60 EVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDP-----------------------APLQAEL---------NSAKGS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 142 VLKAQADLANAQAEYRRQRGV-DPRATTQQSIDSANAQLRsaqaalasaqaqlevaeqvqlqirQQETNVEArerqveqA 220
Cdd:PRK09859 108 LAKALSTASNARITFNRQASLlKTNYVSRQDYDTARTQLN------------------------EAEANVTV-------A 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504696010 221 KAQLETANLNLSYTEVRAPFDGFVTKRNVQPGTLVQAGTA 260
Cdd:PRK09859 157 KAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQA 196
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
105-224 |
1.90e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 43.10 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 105 QAQAQLGLAIAQLHQAQAQLALSKVQY------PAQRDEAKAQVLKAQADLANAQAEYRRQR-------GVDPRATTqqs 171
Cdd:COG1538 87 AAQEQLALAEENLALAEELLELARARYeaglasRLDVLQAEAQLAQARAQLAQAEAQLAQARnalalllGLPPPAPL--- 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 504696010 172 idSANAQLRSAQAALASAQAQLEVAEQVQLQIRQQETNVEARERQVEQAKAQL 224
Cdd:COG1538 164 --DLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAEAEIGVARAAF 214
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
102-234 |
2.60e-04 |
|
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane proteins from the TolC subfamily within the RND (Resistance-Nodulation-cell Division) efflux systems. These proteins, unlike the NodT subfamily, appear not to be lipoproteins. All are believed to participate in type I protein secretion, an ABC transporter system for protein secretion without cleavage of a signal sequence, although they may, like TolC, participate also in the efflux of smaller molecules as well. This family includes the well-documented examples TolC (E. coli), PrtF (Erwinia), and AprF (Pseudomonas aeruginosa). [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Porins]
Pssm-ID: 273829 [Multi-domain] Cd Length: 415 Bit Score: 42.74 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 102 QRDQAQAQLGLAIAQLHQAQAQLALSK-------------VQYPAQRDEAKAQVLKAQADLANAQAEYRRQRGV-DPRAT 167
Cdd:TIGR01844 121 EVLRAQEILALAEANLAALKEQLDLARarfdvglgtrtdvLQAEARYASARAQLIQAQNNLDDAKAQLRRLVGQpELAPL 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504696010 168 TQQSIDSANAQlrsaqaalaSAQAQLEVAEQVQLQIRQQETNVEARERQVEQAKAQ-LETANLNLSYT 234
Cdd:TIGR01844 201 AVPSFPAELPE---------PLDQLLEIAEASNPLLLAAQAAVDAARYQVEQARAGhLPTLSLTASTG 259
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
102-225 |
6.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 102 QRDQAQAQLGLAIAQLHQAQAQLALSKvqypAQRDEAKAQVLKAQADLANAQAEYRRQRgvdprattqQSIDSANAQLRS 181
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELEELR---------LELEELELELEE 285
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 504696010 182 AQAALASAQAQLEVAEQVQLQIRQQETNVEARERQVEQAKAQLE 225
Cdd:COG1196 286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
100-231 |
2.15e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 100 TAQRDQAQAQLGLAIAQLHQAQAQLALSKV---QYPAQRDEAKAQVLKAQADLANAQAEyrrqrgvdpRATTQQSIDSAN 176
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEE---------LEELEEELEEAE 350
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 504696010 177 AQLRSAQAALASAQAQLEVAEQVQLQIRQQETNVEARERQVEQAKAQLETANLNL 231
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
98-226 |
2.91e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 39.61 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 98 DTTAQRDQAQAQLGLAIAQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQadLANAQAEYRRQRGV----DPRA-TTQQSI 172
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQ--LAELEAELAELSARytpnHPDViALRAQI 300
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504696010 173 DSANAQLRSAQAALASA-QAQLEVAEQVQLQIRQQETNVEAR--------------ERQVEQAKAQLET 226
Cdd:COG3206 301 AALRAQLQQEAQRILASlEAELEALQAREASLQAQLAQLEARlaelpeleaelrrlEREVEVARELYES 369
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
98-227 |
4.04e-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: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 98 DTTAQRDQAQAQLGLAIAQLHQAQAQLALSKVQYPAQRDEAKA-----QVLKAQADLANAQAEYRRQRgvdpraTTQQSI 172
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqrlaEYSWDEIDVASAEREIAELE------AELERL 680
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 504696010 173 DSANAQLRSAQAALASAQAQLEVAEQ----VQLQIRQQETNVEARERQVEQAKAQLETA 227
Cdd:COG4913 681 DASSDDLAALEEQLEELEAELEELEEeldeLKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
|
| Surf_Exclu_PgrA |
TIGR04320 |
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ... |
116-231 |
6.91e-03 |
|
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.
Pssm-ID: 275124 [Multi-domain] Cd Length: 356 Bit Score: 38.17 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 116 QLHQAQAQLALSKVQY-PAQRD--EAKAQVLKAQADLANAQAEYrrqrgvdprATTQQSIDSANAQlrsaqaalasaqaq 192
Cdd:TIGR04320 255 SLAALQAKLATAQADLaAAQTAlnTAQAALTSAQTAYAAAQAAL---------ATAQKELANAQAQ-------------- 311
|
90 100 110
....*....|....*....|....*....|....*....
gi 504696010 193 leVAEQVQLQIRQQETNVEARERQVEQAKAQLETANLNL 231
Cdd:TIGR04320 312 --ALQTAQNNLATAQAALANAEARLAKAKEALANLNADL 348
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
100-241 |
7.71e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 37.93 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504696010 100 TAQRDQAQAQLgLAIAQLHQAQAQLALSKVQYPAQRDEAKAQVLKAQADLANAQAEYRRQRgvdprattqqsiDSANAQl 179
Cdd:COG2268 198 IRDARIAEAEA-ERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREA------------ETARAE- 263
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504696010 180 rsaqaalasAQAQLEVAEQVQLQIRQQETNVEARERQVE--QAKAQLETANLNLsytEVRAPFD 241
Cdd:COG2268 264 ---------AEAAYEIAEANAEREVQRQLEIAEREREIElqEKEAEREEAELEA---DVRKPAE 315
|
|
| |
