|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
17-388 |
7.07e-115 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 340.13 E-value: 7.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 17 EVESADEETARKAKRKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKR 96
Cdd:PRK15136 6 ETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 97 GDILLRLDDTDAKLAVARAEAQLALTERKVRGLIATDSGLGAQIASRAAdqaradaqlaaargELDKARIDLQRREALVA 176
Cdd:PRK15136 86 GDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKT--------------ALAQAQSDLNRRVPLGN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 177 SGSVSGDELTTARNAHTTALAnvkAAEAARSQasanrltavgdRDANKALIADTTVENNPEVLAARTALDQARIDLDRTI 256
Cdd:PRK15136 152 ANLIGREELQHARDAVASAQA---QLDVAIQQ-----------YNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTG 336
Cdd:PRK15136 218 IVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTG 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1172344048 337 SAFAVVPAQNATGNWIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADIDLSN 388
Cdd:PRK15136 298 SAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTAN 349
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
31-384 |
1.97e-113 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 334.46 E-value: 1.97e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 31 RKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKL 110
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 111 AVARAEAQLALTERKVRGLIATDSGLGAQIASRAADQARADaqlaaarGELDKARIDLQRREALVASGSVSGDELTTARN 190
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAR-------EKLLQAELDLRRRVPLFKKGLISREELDHARK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 191 AHTTALANVkaaEAARSQASAnrltavgdrdANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSKRQV 270
Cdd:TIGR00998 154 ALLSAKAAL---NAAIQEQLN----------ANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 271 QVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTGSAFAVVPAQNATGN 350
Cdd:TIGR00998 221 QVGQVVSPGQPLMAVVPAEQMYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGN 300
|
330 340 350
....*....|....*....|....*....|....
gi 1172344048 351 WIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADI 384
Cdd:TIGR00998 301 WIKVVQRLPVRIKLDPKELDEHPLRIGLSAEVEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
28-386 |
7.46e-76 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 238.02 E-value: 7.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 28 KAKRKKGFTGLVAAVLLLGGGYYAYdYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTD 107
Cdd:COG1566 2 KALKKRRLLALVLLLLALGLALWAA-GRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 108 AKLAVARAEAQLALTERKVRGLIATdSGLGAQIASRAADQARADAqlaaargELDKARIDLQRREALVASGSVSGDELTT 187
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAE-LGAEAEIAAAEAQLAAAQA-------QLDLAQRELERYQALYKKGAVSQQELDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 188 ARNAHTTALANVKAAEAARSQASAnrltavgdrdanKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSK 267
Cdd:COG1566 153 ARAALDAAQAQLEAAQAQLAQAQA------------GLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 268 RQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDnVEYKGKVIGFSGGTGSAfavVPAQNA 347
Cdd:COG1566 221 LNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPD-RVFEGKVTSISPGAGFT---SPPKNA 296
|
330 340 350
....*....|....*....|....*....|....*....
gi 1172344048 348 TGNwikVVQRLPVRIALDPKQLaeHPLQVGLSMTADIDL 386
Cdd:COG1566 297 TGN---VVQRYPVRIRLDNPDP--EPLRPGMSATVEIDT 330
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
56-386 |
4.20e-54 |
|
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: 181.47 E-value: 4.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 56 VASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTERKV--------- 126
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVarlqaeldr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 127 -RGLIATDSGLGAQIASRAADQARADAQLAAARGELDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAA 205
Cdd:pfam00529 84 lQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 206 RSQASANrltAVGDRDANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSKRQVQV-GQRVSSGQTLMV 284
Cdd:pfam00529 164 LDQIYVQ---ITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 285 VVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNV--EYKGKVIGFSGGTGsafavvpaqnatgnwikvvqrlPVRI 362
Cdd:pfam00529 241 VVPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRV 298
|
330 340
....*....|....*....|....
gi 1172344048 363 ALDPKQLAEHPLQVGLSMTADIDL 386
Cdd:pfam00529 299 VVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
255-285 |
1.86e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 36.63 E-value: 1.86e-03
10 20 30
....*....|....*....|....*....|.
gi 1172344048 255 TIIRAPVDGIVSKRQVQVGQRVSSGQTLMVV 285
Cdd:cd06850 37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
17-388 |
7.07e-115 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 340.13 E-value: 7.07e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 17 EVESADEETARKAKRKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKR 96
Cdd:PRK15136 6 ETQTPQQPVKKKGKRKRALLLLTLLFIIIGVAYGIYWFLVLRHHQETDDAYVAGNQVQIMSQVSGSVTKVWADNTDFVKE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 97 GDILLRLDDTDAKLAVARAEAQLALTERKVRGLIATDSGLGAQIASRAAdqaradaqlaaargELDKARIDLQRREALVA 176
Cdd:PRK15136 86 GDVLVTLDPTDAEQAFEKAKTALANSVRQTHQLMINSKQYQANIELQKT--------------ALAQAQSDLNRRVPLGN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 177 SGSVSGDELTTARNAHTTALAnvkAAEAARSQasanrltavgdRDANKALIADTTVENNPEVLAARTALDQARIDLDRTI 256
Cdd:PRK15136 152 ANLIGREELQHARDAVASAQA---QLDVAIQQ-----------YNANQAMILNTPLEDQPAVQQAATEVRNAWLALQRTK 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTG 336
Cdd:PRK15136 218 IVSPMTGYVSRRSVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIGQPATITSDIYGDDVVYTGKVVGLDMGTG 297
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1172344048 337 SAFAVVPAQNATGNWIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADIDLSN 388
Cdd:PRK15136 298 SAFSLLPAQNATGNWIKVVQRLPVRIELDAKQLAQHPLRIGLSTLVTVDTAN 349
|
|
| 8a0101 |
TIGR00998 |
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, ... |
31-384 |
1.97e-113 |
|
efflux pump membrane protein (multidrug resistance protein A); [Transport and binding proteins, Other]
Pssm-ID: 273385 [Multi-domain] Cd Length: 334 Bit Score: 334.46 E-value: 1.97e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 31 RKKGFTGLVAAVLLLGGGYYAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKL 110
Cdd:TIGR00998 1 RKYFLLLLVVLLIVVAGAYAIYWFLVLRDYESTDDAYVKANQLQVSSQVSGSVIEVNVDDTDYVKQGDVLVRLDPTNAEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 111 AVARAEAQLALTERKVRGLIATDSGLGAQIASRAADQARADaqlaaarGELDKARIDLQRREALVASGSVSGDELTTARN 190
Cdd:TIGR00998 81 ALAKAEANLAALVRQTKQLEITVQQLQAKVESLKIKLEQAR-------EKLLQAELDLRRRVPLFKKGLISREELDHARK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 191 AHTTALANVkaaEAARSQASAnrltavgdrdANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSKRQV 270
Cdd:TIGR00998 154 ALLSAKAAL---NAAIQEQLN----------ANQALVRGTPLKKQPAVQEAKERLKTAWLALKRTVIRAPFDGYVARRFV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 271 QVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVEYKGKVIGFSGGTGSAFAVVPAQNATGN 350
Cdd:TIGR00998 221 QVGQVVSPGQPLMAVVPAEQMYVEANFKETQLKNVRIGQPVTIRSDLYGSDVVFEGKVTGISMGTGSAFSLLPAQNATGN 300
|
330 340 350
....*....|....*....|....*....|....
gi 1172344048 351 WIKVVQRLPVRIALDPKQLAEHPLQVGLSMTADI 384
Cdd:TIGR00998 301 WIKVVQRLPVRIKLDPKELDEHPLRIGLSAEVEI 334
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
28-386 |
7.46e-76 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 238.02 E-value: 7.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 28 KAKRKKGFTGLVAAVLLLGGGYYAYdYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTD 107
Cdd:COG1566 2 KALKKRRLLALVLLLLALGLALWAA-GRNGPDEPVTADGRVEARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 108 AKLAVARAEAQLALTERKVRGLIATdSGLGAQIASRAADQARADAqlaaargELDKARIDLQRREALVASGSVSGDELTT 187
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAE-LGAEAEIAAAEAQLAAAQA-------QLDLAQRELERYQALYKKGAVSQQELDE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 188 ARNAHTTALANVKAAEAARSQASAnrltavgdrdanKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSK 267
Cdd:COG1566 153 ARAALDAAQAQLEAAQAQLAQAQA------------GLREEEELAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVTN 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 268 RQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDnVEYKGKVIGFSGGTGSAfavVPAQNA 347
Cdd:COG1566 221 LNVEPGEVVSAGQPLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPD-RVFEGKVTSISPGAGFT---SPPKNA 296
|
330 340 350
....*....|....*....|....*....|....*....
gi 1172344048 348 TGNwikVVQRLPVRIALDPKQLaeHPLQVGLSMTADIDL 386
Cdd:COG1566 297 TGN---VVQRYPVRIRLDNPDP--EPLRPGMSATVEIDT 330
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
56-386 |
4.20e-54 |
|
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: 181.47 E-value: 4.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 56 VASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTERKV--------- 126
Cdd:pfam00529 4 LTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVarlqaeldr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 127 -RGLIATDSGLGAQIASRAADQARADAQLAAARGELDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAA 205
Cdd:pfam00529 84 lQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 206 RSQASANrltAVGDRDANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGIVSKRQVQV-GQRVSSGQTLMV 284
Cdd:pfam00529 164 LDQIYVQ---ITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVAFLSVTVdGGTVSAGLRLMF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 285 VVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNV--EYKGKVIGFSGGTGsafavvpaqnatgnwikvvqrlPVRI 362
Cdd:pfam00529 241 VVPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKtgRFTGVVVGISPDTG----------------------PVRV 298
|
330 340
....*....|....*....|....
gi 1172344048 363 ALDPKQLAEHPLQVGLSMTADIDL 386
Cdd:pfam00529 299 VVDKAQGPYYPLRIGLSAGALVRL 322
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
24-384 |
1.55e-40 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 146.71 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 24 ETARKAKRKKGFTGL--VAAVLLLGggyyAYDYFVASRHAVTDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILL 101
Cdd:PRK10476 2 ESTPKKSPRKKLPALaiVALAIVAL----VFVIWRTDSAPSTDDAYIDADVVHVASEVGGRIVELAVTENQAVKKGDLLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 102 RLDDTDAKLAVARAEAQLALTERKV----RGLIATDSglGAQIASRAADQARADaqlaaargeLDKARIDLQRREALVAS 177
Cdd:PRK10476 78 RIDPRPYELTVAQAQADLALADAQImttqRSVDAERS--NAASANEQVERARAN---------AKLATRTLERLEPLLAK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 178 GSVSGDELTTARNAHTTALANVKAAEAARSQASAnrltAVGDRDANKALIAdttvennpevlAARTALDQARIDLDRTII 257
Cdd:PRK10476 147 GYVSAQQVDQARTAQRDAEVSLNQALLQAQAAAA----AVGGVDALVAQRA-----------AREAALAIAELHLEDTTV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 258 RAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISdLYGDNVEYKGKVIGFSGGTGS 337
Cdd:PRK10476 212 RAPFDGRVVGLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYS-MIDRGRPFEGKVDSIGWGVLP 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1172344048 338 AFAV-----VPAQNATGNWIKVVQRLPVRIALD--PKQLaehpLQVGLSMTADI 384
Cdd:PRK10476 291 DDGGnvprgLPYVPRSINWVRVAQRFPVRIMLDkpDPEL----FRIGASAVVEL 340
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
71-387 |
7.27e-34 |
|
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: 128.14 E-value: 7.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 71 NVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTERkvrgliatdsglgaqiasraadqara 150
Cdd:COG0845 22 REVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQA-------------------------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 151 daqlaaargELDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAArsqasanrltavgdrdankaliadt 230
Cdd:COG0845 76 ---------QLELAKAELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAA------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 231 tvennpevlaartaLDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQS 310
Cdd:COG0845 122 --------------LEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLARLKVGQP 187
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172344048 311 VTLISDLYGDnVEYKGKVIgfsggtgsafAVVPAQNATgnwikvVQRLPVRIALDPkqlAEHPLQVGLSMTADIDLS 387
Cdd:COG0845 188 VTVTLDAGPG-KTFEGKVT----------FIDPAVDPA------TRTVRVRAELPN---PDGLLRPGMFVRVRIVLG 244
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
32-331 |
8.10e-24 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 100.81 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 32 KKGFTGLVAAVLLLGGGYYAYDYFvASRHAVTDNAYVGANVAQVTpL---IGGPVREVLVDDTQKVKRGDILLRLDDT-- 106
Cdd:PRK03598 2 KKKVVIGLAVVVLAAAVAGGWWWY-QSRQDNGLTLYGNVDIRTVN-LgfrVGGRLASLAVDEGDAVKAGQVLGELDAApy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 107 -----DAKLAVARAEAQLALTERKVRgliatdSGLGAQIASRAADQARadaqlaaargELDKARIDLQRREALVASGSVS 181
Cdd:PRK03598 80 enalmQAKANVSVAQAQLDLMLAGYR------DEEIAQARAAVKQAQA----------AYDYAQNFYNRQQGLWKSRTIS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 182 GDELTTARNAHTTALANVKAAEAARSQASA-NRltaVGDRDANKAliadttvennpEVLAARTALDQARIDLDRTIIRAP 260
Cdd:PRK03598 144 ANDLENARSSRDQAQATLKSAQDKLSQYREgNR---PQDIAQAKA-----------SLAQAQAALAQAELNLQDTELIAP 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1172344048 261 VDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVeYKGKvIGF 331
Cdd:PRK03598 210 SDGTILTRAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKP-YHGQ-IGF 278
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
68-328 |
8.98e-23 |
|
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: 97.39 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 68 VGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTErkvrgliatdsglgAQiasraadq 147
Cdd:TIGR01730 22 EAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAE--------------AQ-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 148 aradaqlaaargeLDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAArsqasanrltavgdrdankali 227
Cdd:TIGR01730 80 -------------LELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKAS---------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 228 adttvennpevlaartaLDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRP 307
Cdd:TIGR01730 125 -----------------LASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAGQTLATIVDLDPLEADFSVPERDLPQLRR 187
|
250 260
....*....|....*....|.
gi 1172344048 308 GQSVTLISDLYgDNVEYKGKV 328
Cdd:TIGR01730 188 GQTLTVELDAL-PGEEFKGKL 207
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
63-373 |
2.69e-17 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 81.71 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 63 TDNAYVGANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTERKVrgliatdsglgaqias 142
Cdd:PRK10559 38 TRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLA---------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 143 raadqaradaqlaaargelDKARIDLQRREALVASgSVSGDELTTARNAHTTALANVKAAEAARsqasanrltavgdrda 222
Cdd:PRK10559 102 -------------------QEKRREAGRRNRLGVQ-AMSREEIDQANNVLQTVLHQLAKAQATR---------------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 223 nkaliadttvennpevlaartalDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQL 302
Cdd:PRK10559 146 -----------------------DLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKL 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172344048 303 AKVRPGQSVTlISDLyGDNVEYKGKVIGFSGGTGSAFAVVPAQ-----NATGNWIKVVQRLPVRIALDPKQLAEHP 373
Cdd:PRK10559 203 EGVRPGYRAE-ITPL-GSNKVLKGTVDSVAAGVTNSSSTRDSKgmatiDSNLEWVRLAQRVPVRIRLDNQQGNLYP 276
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
71-384 |
9.14e-15 |
|
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: 75.43 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 71 NVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTD----------------AKLAVARAEA----------------- 117
Cdd:TIGR01843 42 NVKVVQHLEGGIVREILVREGDRVKAGQVLVELDATDveadaaelesqvlrleAEVARLRAEAdsqaaiefpddllsaed 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 118 ---------QLALTERKVRGLIATDSGLGAQIASRAADQARADAQLAAARGELDKARIDLQRREALVASGSVSGDELTTA 188
Cdd:TIGR01843 122 pavpelikgQQSLFESRKSTLRAQLELILAQIKQLEAELAGLQAQLQALRQQLEVISEELEARRKLKEKGLVSRLELLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 189 ---RNAHTTALANVKA-AEAARSQASANRLTAVGDRDANKALIADTTVENNPEVLAARTALDQARIDLDRTIIRAPVDGI 264
Cdd:TIGR01843 202 ereRAEAQGELGRLEAeLEVLKRQIDELQLERQQIEQTFREEVLEELTEAQARLAELRERLNKARDRLQRLIIRSPVDGT 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 265 V-SKRQVQVGQRVSSGQTLMVVVPV-QAAYVDANFKEVQLAKVRPGQSVTLISDLYgDNVEY---KGKVIGFSGGTgsaf 339
Cdd:TIGR01843 282 VqSLKVHTVGGVVQPGETLMEIVPEdDPLEIEAKLSPKDIGFVHVGQPAEIKFSAF-PYRRYgilNGKVKSISPDT---- 356
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1172344048 340 avVPAQNATGNWIKVVQRLPVR-IALDPKQLAEHPlqvGLSMTADI 384
Cdd:TIGR01843 357 --FTDERGGGPYYRVRISIDQNtLGIGPKGLELSP---GMPVTADI 397
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
257-337 |
8.17e-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: 58.53 E-value: 8.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDnVEYKGKVIGFSGGTG 336
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSD-YTLEGKVVRISPTVD 80
|
.
gi 1172344048 337 S 337
Cdd:pfam13437 81 P 81
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
70-297 |
1.03e-10 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 62.89 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 70 ANVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLALTErkvrgliATdsglgaqiasraadqar 149
Cdd:PRK11556 85 ANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQ-------AT----------------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 150 adaqlaaargeLDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAArsqasanrltavgdrdankaliad 229
Cdd:PRK11556 141 -----------LANARRDLARYQQLAKTNLVSRQELDAQQALVSETEGTIKADEAS------------------------ 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1172344048 230 ttvennpevlaartaLDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANF 297
Cdd:PRK11556 186 ---------------VASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIVVITQTHPIDLVF 238
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
184-329 |
5.27e-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: 58.67 E-value: 5.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 184 ELTTARNAHTTALANVKA-AEAARSQASANRLTAVGdrdANKALIAdttvennpevlaartALDQARIDLDRTIIRAPVD 262
Cdd:pfam16576 55 ELVAAQQEYLLALRSGDAlSKSELLRAARQRLRLLG---MPEAQIA---------------ELERTGKVQPTVTVYAPIS 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1172344048 263 GIVSKRQVQVGQRVSSGQTLMVVVPVQAAYVDANFKEVQLAKVRPGQSVTLISDLYGDNVeYKGKVI 329
Cdd:pfam16576 117 GVVTELNVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKT-FEGKVD 182
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
71-120 |
2.90e-08 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 49.36 E-value: 2.90e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1172344048 71 NVAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLA 120
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
185-280 |
3.84e-04 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 42.09 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 185 LTTARNAHTTALANVKAAEAA-----RSQASANRLTAVGDRDANKALIADTTVEnnPEVLAARTALDQARIDLDRTIIRA 259
Cdd:PRK09578 99 LKAARDAAAGALAKAEAAHLAaldkrRRYDDLVRDRAVSERDYTEAVADERQAK--AAVASAKAELARAQLQLDYATVTA 176
|
90 100
....*....|....*....|.
gi 1172344048 260 PVDGIVSKRQVQVGQRVSSGQ 280
Cdd:PRK09578 177 PIDGRARRALVTEGALVGQDQ 197
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
72-289 |
6.23e-04 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 41.62 E-value: 6.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 72 VAQVTPLIGGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLAlterkvrgliatdsglGAQIASraadqarad 151
Cdd:PRK09859 61 VAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLA----------------KALSTA--------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 152 aqlaaargelDKARIDLQRREALVASGSVSGDELTTARNAHTTALANVKAAEAARSQASANRLTA------VGDRDANKA 225
Cdd:PRK09859 116 ----------SNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYAnvtspiTGVSGKSSV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1172344048 226 LIADTTVENNPEVLAARTALDQARIDLDRTIirapvdgivsKRQVQVGQRVSSGQTLMV--VVPVQ 289
Cdd:PRK09859 186 TVGALVTANQADSLVTVQRLDPIYVDLTQSV----------QDFLRMKEEVASGQIKQVqgSTPVQ 241
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
68-309 |
7.69e-04 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 41.30 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 68 VGANVAqvtpligGPVREVLVDDTQKVKRGDILLRLDDTDAKLAVARAEAQLalterkvrgliatdSGLGAQIASRAAdq 147
Cdd:PRK11578 64 VGAQVS-------GQLKTLSVAIGDKVKKDQLLGVIDPEQAENQIKEVEATL--------------MELRAQRQQAEA-- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 148 aradaqlaaargELDKARIDLQRREALVASGSVSGDELTTARnahtTALAnVKAAEAARSQASANRltavgdrdaNKAli 227
Cdd:PRK11578 121 ------------ELKLARVTLSRQQRLAKTQAVSQQDLDTAA----TELA-VKQAQIGTIDAQIKR---------NQA-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 228 adttvennpevlaartALDQARIDLDRTIIRAPVDGIVSKRQVQVGQRVSSGQ---TLMVVVPVQAAYVDANFKEVQLAK 304
Cdd:PRK11578 173 ----------------SLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQqapNILTLADMSTMLVKAQVSEADVIH 236
|
....*
gi 1172344048 305 VRPGQ 309
Cdd:PRK11578 237 LKPGQ 241
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
187-294 |
1.46e-03 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 40.47 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1172344048 187 TARNAHTTALANVKAAEAARS--QASANRLTA------VGDRDANKALiADTTvENNPEVLAARTALDQARIDLDRTIIR 258
Cdd:PRK15030 100 TYQATYDSAKGDLAKAQAAANiaQLTVNRYQKllgtqyISKQEYDQAL-ADAQ-QANAAVTAAKAAVETARINLAYTKVT 177
|
90 100 110
....*....|....*....|....*....|....*...
gi 1172344048 259 APVDGIVSKRQVQVGQRVSSGQ--TLMVVVPVQAAYVD 294
Cdd:PRK15030 178 SPISGRIGKSNVTEGALVQNGQatALATVQQLDPIYVD 215
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
255-285 |
1.86e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 36.63 E-value: 1.86e-03
10 20 30
....*....|....*....|....*....|.
gi 1172344048 255 TIIRAPVDGIVSKRQVQVGQRVSSGQTLMVV 285
Cdd:cd06850 37 NEVTAPVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
257-312 |
1.94e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 36.24 E-value: 1.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVV------VPVQAAyVDANFKEVqlaKVRPGQSVT 312
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLeamkmeNEVTAP-VAGVVKEI---LVKEGDQVE 59
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
257-287 |
2.88e-03 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 39.83 E-value: 2.88e-03
10 20 30
....*....|....*....|....*....|.
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVVVP 287
Cdd:PRK09282 562 IQAPVDGTVKEILVKEGDRVNPGDVLMEIEP 592
|
|
| AccB |
COG0511 |
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier ... |
257-285 |
7.52e-03 |
|
Biotin carboxyl carrier protein [Lipid transport and metabolism]; Biotin carboxyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440277 [Multi-domain] Cd Length: 136 Bit Score: 36.41 E-value: 7.52e-03
10 20
....*....|....*....|....*....
gi 1172344048 257 IRAPVDGIVSKRQVQVGQRVSSGQTLMVV 285
Cdd:COG0511 107 IEAPVSGTVVEILVENGQPVEYGQPLFVI 135
|
|
|