|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
11-342 |
2.84e-84 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 258.05 E-value: 2.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 11 VVAIGILLAGVVFFIWWVSK-GRFIQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARL 89
Cdd:COG1566 9 LLALVLLLLALGLALWAAGRnGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 90 EAKIKSSKANLESIQATIAMQQSIiQSASETWQAVKHEEQKRLRDTERYEKLAQSAAISQQIIDNARFDYQQvAAKERKA 169
Cdd:COG1566 89 EAQLAAAEAQLARLEAELGAEAEI-AAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDA-AQAQLEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 170 ANDFLVEKQRLAVLSAQEENVRASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTSLVSLVPVSELWV 249
Cdd:COG1566 167 AQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 250 DANYKENQIAGMKPGMKAEIRADILKGEVFHGHIESLSPATGASFsliPIENATGNftkIVQRVPVRIAFDDakELKQLL 329
Cdd:COG1566 247 EAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDN--PDPEPL 318
|
330
....*....|...
gi 446509668 330 RPGLSVTVSVDER 342
Cdd:COG1566 319 RPGMSATVEIDTE 331
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
5-339 |
8.64e-78 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 241.62 E-value: 8.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 5 KKQLIGVVAIGILLAGVVFFIWWVSKGRFIQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRA 84
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 85 NVARLEAKIKSSKANLESIQATIAMQQSIIQSASETWQAVKHEEQKRLRDTERYEKLAQSAAISQQIIDNARfdYQQVAA 164
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAREKLLQAELDLRRRVPLFKKGLISREELDHAR--KALLSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 165 KERKAANDFLVEKQRLAVLSAQEENVRASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTSLVSLVPV 244
Cdd:TIGR00998 159 KAALNAAIQEQLNANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 245 SELWVDANYKENQIAGMKPGMKAEIRADIL-KGEVFHGHIESLSPATGASFSLIPIENATGNFTKIVQRVPVRIAFDDAK 323
Cdd:TIGR00998 239 EQMYVEANFKETQLKNVRIGQPVTIRSDLYgSDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKE 318
|
330
....*....|....*.
gi 446509668 324 ELKQLLRPGLSVTVSV 339
Cdd:TIGR00998 319 LDEHPLRIGLSAEVEI 334
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
17-342 |
1.04e-61 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 201.85 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 17 LLAGVVFFIWWVSKGRFIQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIKSS 96
Cdd:PRK15136 32 IIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 97 -------KANLESIQATIAMQQSIIQSASEtwqavkheeqkrlrDTERYEKLAQSAAISQQIIDNARfdyQQVA------ 163
Cdd:PRK15136 112 vrqthqlMINSKQYQANIELQKTALAQAQS--------------DLNRRVPLGNANLIGREELQHAR---DAVAsaqaql 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 164 --AKERKAANDFLV-----EKQrlavlsaqeenvrASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGT 236
Cdd:PRK15136 175 dvAIQQYNANQAMIlntplEDQ-------------PAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 237 SLVSLVPVSELWVDANYKENQIAGMKPGMKAEIRADIL-KGEVFHGHIESLSPATGASFSLIPIENATGNFTKIVQRVPV 315
Cdd:PRK15136 242 PLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPV 321
|
330 340
....*....|....*....|....*...
gi 446509668 316 RIAFdDAKELKQL-LRPGLSVTVSVDER 342
Cdd:PRK15136 322 RIEL-DAKQLAQHpLRIGLSTLVTVDTA 348
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
34-340 |
6.55e-41 |
|
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: 145.64 E-value: 6.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 34 IQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIKSSKANLESIQATIAMQQSI 113
Cdd:pfam00529 8 VEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 114 I-----------------QSASETWQAVKHEEQKRLRDTERYEKLAQSAAISQQIIDNARFDYQQVAA--KERKAANDFL 174
Cdd:pfam00529 88 EselaisrqdydgataqlRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQAnlLATVAQLDQI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 175 ------VEKQRLAVLSAQEENVRASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHT-GSWVEGGTSLVSLVPVSEL 247
Cdd:pfam00529 168 yvqitqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 248 WVDANYKENQIAGMKPGMKAEIRADIL---KGEVFHGHIESLSPATGasfslipienatgnftkivqrvPVRIAFDDAKE 324
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDAFpqtKTGRFTGVVVGISPDTG----------------------PVRVVVDKAQG 305
|
330
....*....|....*.
gi 446509668 325 LKQLLRPGLSVTVSVD 340
Cdd:pfam00529 306 PYYPLRIGLSAGALVR 321
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
11-342 |
2.84e-84 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 258.05 E-value: 2.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 11 VVAIGILLAGVVFFIWWVSK-GRFIQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARL 89
Cdd:COG1566 9 LLALVLLLLALGLALWAAGRnGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 90 EAKIKSSKANLESIQATIAMQQSIiQSASETWQAVKHEEQKRLRDTERYEKLAQSAAISQQIIDNARFDYQQvAAKERKA 169
Cdd:COG1566 89 EAQLAAAEAQLARLEAELGAEAEI-AAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDA-AQAQLEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 170 ANDFLVEKQRLAVLSAQEENVRASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTSLVSLVPVSELWV 249
Cdd:COG1566 167 AQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQPLLTIVPLDDLWV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 250 DANYKENQIAGMKPGMKAEIRADILKGEVFHGHIESLSPATGASFsliPIENATGNftkIVQRVPVRIAFDDakELKQLL 329
Cdd:COG1566 247 EAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTS---PPKNATGN---VVQRYPVRIRLDN--PDPEPL 318
|
330
....*....|...
gi 446509668 330 RPGLSVTVSVDER 342
Cdd:COG1566 319 RPGMSATVEIDTE 331
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
5-339 |
8.64e-78 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 241.62 E-value: 8.64e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 5 KKQLIGVVAIGILLAGVVFFIWWVSKGRFIQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRA 84
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 85 NVARLEAKIKSSKANLESIQATIAMQQSIIQSASETWQAVKHEEQKRLRDTERYEKLAQSAAISQQIIDNARfdYQQVAA 164
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAREKLLQAELDLRRRVPLFKKGLISREELDHAR--KALLSA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 165 KERKAANDFLVEKQRLAVLSAQEENVRASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTSLVSLVPV 244
Cdd:TIGR00998 159 KAALNAAIQEQLNANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFVQVGQVVSPGQPLMAVVPA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 245 SELWVDANYKENQIAGMKPGMKAEIRADIL-KGEVFHGHIESLSPATGASFSLIPIENATGNFTKIVQRVPVRIAFDDAK 323
Cdd:TIGR00998 239 EQMYVEANFKETQLKNVRIGQPVTIRSDLYgSDVVFEGKVTGISMGTGSAFSLLPAQNATGNWIKVVQRLPVRIKLDPKE 318
|
330
....*....|....*.
gi 446509668 324 ELKQLLRPGLSVTVSV 339
Cdd:TIGR00998 319 LDEHPLRIGLSAEVEI 334
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
17-342 |
1.04e-61 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 201.85 E-value: 1.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 17 LLAGVVFFIWWVSKGRFIQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIKSS 96
Cdd:PRK15136 32 IIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 97 -------KANLESIQATIAMQQSIIQSASEtwqavkheeqkrlrDTERYEKLAQSAAISQQIIDNARfdyQQVA------ 163
Cdd:PRK15136 112 vrqthqlMINSKQYQANIELQKTALAQAQS--------------DLNRRVPLGNANLIGREELQHAR---DAVAsaqaql 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 164 --AKERKAANDFLV-----EKQrlavlsaqeenvrASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGT 236
Cdd:PRK15136 175 dvAIQQYNANQAMIlntplEDQ-------------PAVQQAATEVRNAWLALQRTKIVSPMTGYVSRRSVQVGAQISPTT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 237 SLVSLVPVSELWVDANYKENQIAGMKPGMKAEIRADIL-KGEVFHGHIESLSPATGASFSLIPIENATGNFTKIVQRVPV 315
Cdd:PRK15136 242 PLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKVVGLDMGTGSAFSLLPAQNATGNWIKVVQRLPV 321
|
330 340
....*....|....*....|....*...
gi 446509668 316 RIAFdDAKELKQL-LRPGLSVTVSVDER 342
Cdd:PRK15136 322 RIEL-DAKQLAQHpLRIGLSTLVTVDTA 348
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
5-339 |
1.53e-45 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 158.65 E-value: 1.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 5 KKQLIGVVAIGILLAGVVFFIWWVSKGrfiQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRA 84
Cdd:PRK10476 10 RKKLPALAIVALAIVALVFVIWRTDSA---PSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 85 NVARLEAKIKSSKANLESIQATIAMQQSIIQSASETWQAVKHEEQKRLRDTERYEKLAQSAAISQQIIDNARFdYQQVAA 164
Cdd:PRK10476 87 TVAQAQADLALADAQIMTTQRSVDAERSNAASANEQVERARANAKLATRTLERLEPLLAKGYVSAQQVDQART-AQRDAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 165 KERKAANdflveKQRLAVLSA--QEENVRASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTSLVSLV 242
Cdd:PRK10476 166 VSLNQAL-----LQAQAAAAAvgGVDALVAQRAAREAALAIAELHLEDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 243 PVSELWVDANYKENQIAGMKPGMKAEIRADILKGEVFHGHIESLS----PATGASF--SLiPIENATGNFTKIVQRVPVR 316
Cdd:PRK10476 241 DTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSIGwgvlPDDGGNVprGL-PYVPRSINWVRVAQRFPVR 319
|
330 340
....*....|....*....|...
gi 446509668 317 IAFDDAKElkQLLRPGLSVTVSV 339
Cdd:PRK10476 320 IMLDKPDP--ELFRIGASAVVEL 340
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
45-340 |
1.95e-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: 157.41 E-value: 1.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 45 NITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIKSSKANLESIQatiamqqsiiqsasetwqav 124
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAK-------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 125 kheeqkrlRDTERYEKLAQSAAISQQIIDNARFDYQQVaakerkaandflvekqrlavlsaqeenvRASIEEVQAALTQA 204
Cdd:COG0845 82 --------AELERYKALLKKGAVSQQELDQAKAALDQA----------------------------QAALAAAQAALEQA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 205 LLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTSLVSLVPVSELWVDANYKENQIAGMKPGMKAEIRADILKGEVFHGHIE 284
Cdd:COG0845 126 RANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVT 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446509668 285 SLSPAtgasfslipIENATGNFtkivqrvPVRIAFDDAkelKQLLRPGLSVTVSVD 340
Cdd:COG0845 206 FIDPA---------VDPATRTV-------RVRAELPNP---DGLLRPGMFVRVRIV 242
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
34-340 |
6.55e-41 |
|
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: 145.64 E-value: 6.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 34 IQTTDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIKSSKANLESIQATIAMQQSI 113
Cdd:pfam00529 8 VEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 114 I-----------------QSASETWQAVKHEEQKRLRDTERYEKLAQSAAISQQIIDNARFDYQQVAA--KERKAANDFL 174
Cdd:pfam00529 88 EselaisrqdydgataqlRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQAnlLATVAQLDQI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 175 ------VEKQRLAVLSAQEENVRASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHT-GSWVEGGTSLVSLVPVSEL 247
Cdd:pfam00529 168 yvqitqSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMFVVPEDNL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 248 WVDANYKENQIAGMKPGMKAEIRADIL---KGEVFHGHIESLSPATGasfslipienatgnftkivqrvPVRIAFDDAKE 324
Cdd:pfam00529 248 LVPGMFVETQLDQVRVGQPVLIPFDAFpqtKTGRFTGVVVGISPDTG----------------------PVRVVVDKAQG 305
|
330
....*....|....*.
gi 446509668 325 LKQLLRPGLSVTVSVD 340
Cdd:pfam00529 306 PYYPLRIGLSAGALVR 321
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
43-339 |
3.48e-36 |
|
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: 133.21 E-value: 3.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 43 GGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIKSSKANLESIQatiamqqsiiqsasetwq 122
Cdd:TIGR01730 23 AVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLELAQ------------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 123 avkheeqkrlRDTERYEKLAQSAAISQQIIDNARfdyqqvaakerkaandflvekqrlavlsAQEENVRASIEEVQAALT 202
Cdd:TIGR01730 85 ----------RSFERAERLVKRNAVSQADLDDAK----------------------------AAVEAAQADLEAAKASLA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 203 QALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTSLVSLVPVSELWVDANYKENQIAGMKPGMKAEIRADILKGEVFHGH 282
Cdd:TIGR01730 127 SAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGK 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446509668 283 IESLSPAtgasfslipIENATGNFtkivqrvPVRIAFDDAkelKQLLRPGLSVTVSV 339
Cdd:TIGR01730 207 LRFIDPR---------VDSGTGTV-------RVRATFPNP---DGRLLPGMFGRVTI 244
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
4-342 |
2.05e-31 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 120.45 E-value: 2.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 4 SKKQLIGVVAIGILLAGVVFFIWWvskgrFIQTTDDA-YIGGN--ITTV--ASKVSGYISAIEVRDNQSVKKGDIILRLD 78
Cdd:PRK03598 1 MKKKVVIGLAVVVLAAAVAGGWWW-----YQSRQDNGlTLYGNvdIRTVnlGFRVGGRLASLAVDEGDAVKAGQVLGELD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 79 DRDYRANVARLEAKIKSSKANLESIQATiAMQQSIIQSASETWQAvkheeQKRLRDTE----RYEKLAQSAAISQQIIDN 154
Cdd:PRK03598 76 AAPYENALMQAKANVSVAQAQLDLMLAG-YRDEEIAQARAAVKQA-----QAAYDYAQnfynRQQGLWKSRTISANDLEN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 155 ARFDYQQVAAKeRKAANDFLveKQRLAVLSAQE-ENVRASIEEVQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVE 233
Cdd:PRK03598 150 ARSSRDQAQAT-LKSAQDKL--SQYREGNRPQDiAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGTMLN 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 234 GGTSLVSLVPVSELWVDANYKENQIAGMKPGMKAEIRADILKGEVFHGHIESLSPAtgASFSLIPIEnaTGNF-TKIVQR 312
Cdd:PRK03598 227 AGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQIGFVSPT--AEFTPKTVE--TPDLrTDLVYR 302
|
330 340 350
....*....|....*....|....*....|
gi 446509668 313 vpVRIAFDDAKElkqLLRPGLSVTVSVDER 342
Cdd:PRK03598 303 --LRIVVTDADD---ALRQGMPVTVRFADE 327
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
2-322 |
9.74e-27 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 107.52 E-value: 9.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 2 IISKKQLIGVVAIGILLAGVVFFIWWVskgrFIQT---TDDAYIGGNITTVASKVSGYISAIEVRDNQSVKKGDIILRLD 78
Cdd:PRK10559 4 LIRKISRTAITLVLVILAFIAIFRAWV----FYTEspwTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 79 DRDYRanvarleakikssKAnLESIQATIAMQQSIIQsasetwqavkheeQKRlRDTERYEKLAQSaAISQQIIDNARFD 158
Cdd:PRK10559 80 QPRYQ-------------KA-LAEAEADVAYYQVLAQ-------------EKR-REAGRRNRLGVQ-AMSREEIDQANNV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 159 YQQVAAKERKAandflvekqrlavlsaqeenvrasieevQAALTQALLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTSL 238
Cdd:PRK10559 131 LQTVLHQLAKA----------------------------QATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 239 VSLVPVSELWVDANYKENQIAGMKPGMKAEIrADILKGEVFHGHIESL------SPATGASFSLIPIENATgNFTKIVQR 312
Cdd:PRK10559 183 VALVKQNSFYVLAYMEETKLEGVRPGYRAEI-TPLGSNKVLKGTVDSVaagvtnSSSTRDSKGMATIDSNL-EWVRLAQR 260
|
330
....*....|
gi 446509668 313 VPVRIAFDDA 322
Cdd:PRK10559 261 VPVRIRLDNQ 270
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
7-339 |
3.55e-19 |
|
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: 87.76 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 7 QLIGVVAIGILLAGVVFFIWW----------VSKGRFIQTtddayigGNITTVASKVSGYISAIEVRDNQSVKKGDIILR 76
Cdd:TIGR01843 1 SRFARLITWLIAGLVVIFFLWayfapldvvaTATGKVVPS-------GNVKVVQHLEGGIVREILVREGDRVKAGQVLVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 77 LDDRDYRANVARLEAKIKSSKANLESIQA------------------------TIAMQQSIIQSASETWQA--------V 124
Cdd:TIGR01843 74 LDATDVEADAAELESQVLRLEAEVARLRAeadsqaaiefpddllsaedpavpeLIKGQQSLFESRKSTLRAqlelilaqI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 125 KHEEQKRLRDTERYEKLAQSAAISQQIIDNAR--FDYQQVA--------AKERKAANDFLVEKQRLAVLSAQEENVRASI 194
Cdd:TIGR01843 154 KQLEAELAGLQAQLQALRQQLEVISEELEARRklKEKGLVSrlelleleRERAEAQGELGRLEAELEVLKRQIDELQLER 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 195 --------EEVQAALTQA---LLDLEYTL-----------VRAPIDGIVANRSAHT-GSWVEGGTSLVSLVPVSE-LWVD 250
Cdd:TIGR01843 234 qqieqtfrEEVLEELTEAqarLAELRERLnkardrlqrliIRSPVDGTVQSLKVHTvGGVVQPGETLMEIVPEDDpLEIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 251 ANYKENQIAGMKPGMKAEIRADILKGE---VFHGHIESLSPatgasfSLIPIENATGNFTKIVQRVPVRIAFDDAKELkq 327
Cdd:TIGR01843 314 AKLSPKDIGFVHVGQPAEIKFSAFPYRrygILNGKVKSISP------DTFTDERGGGPYYRVRISIDQNTLGIGPKGL-- 385
|
410
....*....|..
gi 446509668 328 LLRPGLSVTVSV 339
Cdd:TIGR01843 386 ELSPGMPVTADI 397
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
154-335 |
3.57e-15 |
|
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: 73.31 E-value: 3.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 154 NARFDYQQVAAKERKAANDFLVE--KQRLAVLSAQEENVRAsIE---EVQAALTqalldleytlVRAPIDGIVANRSAHT 228
Cdd:pfam16576 58 AAQQEYLLALRSGDALSKSELLRaaRQRLRLLGMPEAQIAE-LErtgKVQPTVT----------VYAPISGVVTELNVRE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 229 GSWVEGGTSLVSLVPVSELWVDANYKENQIAGMKPGMKAEIRADILKGEVFHGHIESLSPAtgasfslipIENATgnftk 308
Cdd:pfam16576 127 GMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYPT---------LDPKT----- 192
|
170 180
....*....|....*....|....*...
gi 446509668 309 ivqR-VPVRIAFDDAkelKQLLRPGLSV 335
Cdd:pfam16576 193 ---RtVRVRIELPNP---DGRLKPGMFA 214
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
49-267 |
1.16e-11 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 65.18 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 49 VASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIKSSKANLESIQATIAMQQSIIQsasetwqavkhee 128
Cdd:PRK11578 64 VGAQVSGQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLS------------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 129 qkrlrdteRYEKLAQSAAISQQIIDNARFDyqqvaakerkaandflvekqrLAVLSAQEENVRASIEEVQAALTQALLDL 208
Cdd:PRK11578 131 --------RQQRLAKTQAVSQQDLDTAATE---------------------LAVKQAQIGTIDAQIKRNQASLDTAKTNL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446509668 209 EYTLVRAPIDGIVANRSAHTGSWV---EGGTSLVSLVPVSELWVDANYKENQIAGMKPGMKA 267
Cdd:PRK11578 182 DYTRIVAPMAGEVTQITTLQGQTViaaQQAPNILTLADMSTMLVKAQVSEADVIHLKPGQKA 243
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
213-332 |
1.62e-11 |
|
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: 60.07 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 213 VRAPIDGIVANRSAHTGSWVEGGTSLVSLVPVSELWVDANYKENQIAGMKPGMKAEIRADILKGEVFHGHIESLSPATGA 292
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISPTVDP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 446509668 293 SfslipienatgnftkiVQRVPVRIAFDDAKELKqLLRPG 332
Cdd:pfam13437 82 D----------------TGVIPVRVSIENPKTPI-PLLPG 104
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
48-94 |
1.52e-10 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 55.91 E-value: 1.52e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 446509668 48 TVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIK 94
Cdd:pfam13533 4 KIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
45-237 |
1.80e-10 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 61.73 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 45 NITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRANVARLEAKIKSSKANLESIQatiamqqsiiqsasetwqav 124
Cdd:PRK11556 86 NTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANAR-------------------- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 125 kheeqkrlRDTERYEKLAQSAAISQQIIDNarfdyQQVAAKERKAandflvekqrlavlsaqeenvraSIEEVQAALTQA 204
Cdd:PRK11556 146 --------RDLARYQQLAKTNLVSRQELDA-----QQALVSETEG-----------------------TIKADEASVASA 189
|
170 180 190
....*....|....*....|....*....|...
gi 446509668 205 LLDLEYTLVRAPIDGIVANRSAHTGSWVEGGTS 237
Cdd:PRK11556 190 QLQLDYSRITAPISGRVGLKQVDVGNQISSGDT 222
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
46-307 |
7.25e-07 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 50.48 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 46 ITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYranvarlEAKIKSSKANLESIQATIAMQQSIIQsasetwqavk 125
Cdd:PRK15030 65 IAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATY-------QATYDSAKGDLAKAQAAANIAQLTVN---------- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 126 heeqkrlrdteRYEKLAQSAAISQQIIDNARFDYQQVAAkerkaandflvekqrlAVLSAQeenvrasieevqAALTQAL 205
Cdd:PRK15030 128 -----------RYQKLLGTQYISKQEYDQALADAQQANA----------------AVTAAK------------AAVETAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 206 LDLEYTLVRAPIDGIVANRSAHTGSWVEGG--TSLVSLVPVSELWVDANYKENQIAgmkpGMKAEIRADILKGEVFHGHI 283
Cdd:PRK15030 169 INLAYTKVTSPISGRIGKSNVTEGALVQNGqaTALATVQQLDPIYVDVTQSSNDFL----RLKQELANGTLKQENGKAKV 244
|
250 260 270
....*....|....*....|....*....|.
gi 446509668 284 ESLS------PATGA-SFSLIPIENATGNFT 307
Cdd:PRK15030 245 SLITsdgikfPQDGTlEFSDVTVDQTTGSIT 275
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
49-220 |
3.23e-05 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 45.17 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 49 VASKVSGYISAIEVRDNQSVKKGDIILRLDDRDYRAnvARLEAkiksskanlesiQATIAMQQSIIQSASEtwqavkhee 128
Cdd:PRK09578 66 VRARVAGIVTARTYEEGQEVKQGAVLFRIDPAPLKA--ARDAA------------AGALAKAEAAHLAALD--------- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 129 qKRlrdtERYEKLAQSAAISQQiidnarfDYQQVAAKERKAandflvekqRLAVLSAQeenvrasieevqAALTQALLDL 208
Cdd:PRK09578 123 -KR----RRYDDLVRDRAVSER-------DYTEAVADERQA---------KAAVASAK------------AELARAQLQL 169
|
170
....*....|..
gi 446509668 209 EYTLVRAPIDGI 220
Cdd:PRK09578 170 DYATVTAPIDGR 181
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
46-341 |
7.95e-04 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 40.85 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 46 ITTVASKVSGYISAIEVRDNQSVKKGDIILRLDDrdyranvARLEAKIKSSKANLesiqatiAMQQSIIQSASETWQavk 125
Cdd:PRK09859 61 VAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDP-------APLQAELNSAKGSL-------AKALSTASNARITFN--- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 126 heeqkrlrdteRYEKLAQSAAISQQIIDNARfdyqqvaakerkaandflvekqrlavlsAQEENVRASIEEVQAALTQAL 205
Cdd:PRK09859 124 -----------RQASLLKTNYVSRQDYDTAR----------------------------TQLNEAEANVTVAKAAVEQAT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 206 LDLEYTLVRAPIDGIVANRSAHTGSWVEG--GTSLVSLVPVSELWVDanykenqiagMKPGMKAEIRadiLKGEVFHGHI 283
Cdd:PRK09859 165 INLQYANVTSPITGVSGKSSVTVGALVTAnqADSLVTVQRLDPIYVD----------LTQSVQDFLR---MKEEVASGQI 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 284 ESLSPATGASFSLipiENA-----TGNFT-------KIVQRVPVRIAFDDAkelKQLLRPGLSVTVSVDE 341
Cdd:PRK09859 232 KQVQGSTPVQLNL---ENGkrysqTGTLKfsdptvdETTGSVTLRAIFPNP---NGDLLPGMYVTALVDE 295
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
83-209 |
9.62e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 9.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 83 RANVARLEAKIKSSKANLESIQATIAMQQ----SIIQSASETWQAVKHEEQKRLRDTERYEKLAQSAAISQQIIDNARFD 158
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQaeeyELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446509668 159 YQQVAAKERKAANDFLVEKQRLAVLSAQEENVRASIEEVQAALTQALLDLE 209
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
82-203 |
8.58e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.11 E-value: 8.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446509668 82 YRANVARLEAKIKSSKANLESIQATIAM---QQSIIQSASETWQAVKHEEQKRLRDT-ERYEKLAQSAAISQQIIDNARF 157
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALrKDLARLEAEVEQLEERIAQLSK 754
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90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446509668 158 DYQQVAAKERKAANDFLVEKQRLAVLSAQEENVRASIEEVQAALTQ 203
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
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