|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
3-369 |
0e+00 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 559.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 3 FFLTKKQGKIIAAILIFIAIGLFFFWPKEH--LPSYQTQKITRGELSKEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEG 80
Cdd:PRK11578 1 MKKRKKVKKRYLIALVIVLAGGITLWRILNapVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 81 DVVKKGDLLAIIDPKKAQNEVAESQETNNELTANLQQAKAELRLAQLTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARV 160
Cdd:PRK11578 81 DKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 161 ATYEAQIRKNQATLDTARTNLQYTRITAPMDGVVTFIKTLEGQTVIAAQEAPTILTLADLDTMLVKAEVSEADVIYLKPD 240
Cdd:PRK11578 161 GTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 241 LKASFTVLGAPDKAFNGKLKDILPTPEKINDAIFYYARFEVPNEQHLLRLQMTAQVKILLEHKKDILLVPLSALGEDVGI 320
Cdd:PRK11578 241 QKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGD 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490364890 321 NEYQVEVLVNGQPEKRVVKIGIRTDVYAEVISGLNENDDVILGEIAGES 369
Cdd:PRK11578 321 NRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIGEAKPGA 369
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
40-362 |
5.83e-83 |
|
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: 255.25 E-value: 5.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 40 KITRGELSKEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVAESQetnneltANLQQAK 119
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQ-------AQLAAAQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 120 AELRLAQLTYQRQLKLIGTHVIAQEELDRTktdvevkKARVATYEAQIRKNQATLDTARTNLQYTRITAPMDGVVTFIKT 199
Cdd:COG0845 75 AQLELAKAELERYKALLKKGAVSQQELDQA-------KAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 200 LEGQTVIAAQeapTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDILPTPEkiNDAIFYYARF 279
Cdd:COG0845 148 EPGQLVSAGT---PLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVD--PATRTVRVRA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 280 EVPNEQHLLRLQMTAQVKILLEHKKDILLVPLSALGEDVGinEYQVEVLV-NGQPEKRVVKIGIRTDVYAEVISGLNEND 358
Cdd:COG0845 223 ELPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGG--GAYVFVVDaDGKVERRPVTLGRRDGDQVEVLSGLKAGD 300
|
....
gi 490364890 359 DVIL 362
Cdd:COG0845 301 RVVV 304
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-362 |
7.49e-57 |
|
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: 188.29 E-value: 7.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 38 TQKITRGELSKEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAqnevaesQETNNELTANLQQ 117
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDY-------QLALQAALAQLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 118 AKAELRLAQLTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARVATYEAQirknqatLDTARTNLQYTRITAPMDGVVTFI 197
Cdd:TIGR01730 76 AEAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKAS-------LASAQLNLRYTEIRAPFDGTIGRR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 198 KTLEGQTVIAAQeapTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDILPTPEKINDAIFYYA 277
Cdd:TIGR01730 149 LVEVGAYVTAGQ---TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 278 RFevPNEQHLLRLQMTAQVKILLEHKKDILLVPLSALGEDvgINEYQVEVLVN-GQPEKRVVKIGIRTDVYAEVISGLNE 356
Cdd:TIGR01730 226 TF--PNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIED--LNGKYVYVVKNdGKVSKRPVEVGLRNGGYVEIESGLKA 301
|
....*.
gi 490364890 357 NDDVIL 362
Cdd:TIGR01730 302 GDQIVT 307
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
45-294 |
2.43e-25 |
|
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: 101.81 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 45 ELSKEVTATGKL--DAVRKVDVGAQVSGQLQTLYVK-EGDVVKKGDLLAIID-PK--KAQNEVAESQETNNELTAN--LQ 116
Cdd:pfam16576 1 PLSRTIRAVGRVayDERRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYsPElvAAQQEYLLALRSGDALSKSelLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 117 QAKAELRLAQLTyqrqlkligthviaqeeldrtktdvevkkarvatyEAQIrknqATLDTARTNLQYTRITAPMDGVVTF 196
Cdd:pfam16576 81 AARQRLRLLGMP-----------------------------------EAQI----AELERTGKVQPTVTVYAPISGVVTE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 197 IKTLEGQTVIAAQeapTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDILPTPEKINDAIfyY 276
Cdd:pfam16576 122 LNVREGMYVQPGD---TLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTV--R 196
|
250
....*....|....*...
gi 490364890 277 ARFEVPNEQHLLRLQMTA 294
Cdd:pfam16576 197 VRIELPNPDGRLKPGMFA 214
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
64-101 |
2.47e-04 |
|
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: 38.94 E-value: 2.47e-04
10 20 30
....*....|....*....|....*....|....*...
gi 490364890 64 VGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEV 101
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEV 39
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
3-369 |
0e+00 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 559.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 3 FFLTKKQGKIIAAILIFIAIGLFFFWPKEH--LPSYQTQKITRGELSKEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEG 80
Cdd:PRK11578 1 MKKRKKVKKRYLIALVIVLAGGITLWRILNapVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 81 DVVKKGDLLAIIDPKKAQNEVAESQETNNELTANLQQAKAELRLAQLTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARV 160
Cdd:PRK11578 81 DKVKKDQLLGVIDPEQAENQIKEVEATLMELRAQRQQAEAELKLARVTLSRQQRLAKTQAVSQQDLDTAATELAVKQAQI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 161 ATYEAQIRKNQATLDTARTNLQYTRITAPMDGVVTFIKTLEGQTVIAAQEAPTILTLADLDTMLVKAEVSEADVIYLKPD 240
Cdd:PRK11578 161 GTIDAQIKRNQASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLADMSTMLVKAQVSEADVIHLKPG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 241 LKASFTVLGAPDKAFNGKLKDILPTPEKINDAIFYYARFEVPNEQHLLRLQMTAQVKILLEHKKDILLVPLSALGEDVGI 320
Cdd:PRK11578 241 QKAWFTVLGDPLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIPLSALGDPVGD 320
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 490364890 321 NEYQVEVLVNGQPEKRVVKIGIRTDVYAEVISGLNENDDVILGEIAGES 369
Cdd:PRK11578 321 NRYKVKLLRNGETREREVTIGARNDTDVEIVKGLEAGDEVIIGEAKPGA 369
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
40-362 |
5.83e-83 |
|
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: 255.25 E-value: 5.83e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 40 KITRGELSKEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVAESQetnneltANLQQAK 119
Cdd:COG0845 2 KVERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQ-------AQLAAAQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 120 AELRLAQLTYQRQLKLIGTHVIAQEELDRTktdvevkKARVATYEAQIRKNQATLDTARTNLQYTRITAPMDGVVTFIKT 199
Cdd:COG0845 75 AQLELAKAELERYKALLKKGAVSQQELDQA-------KAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 200 LEGQTVIAAQeapTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDILPTPEkiNDAIFYYARF 279
Cdd:COG0845 148 EPGQLVSAGT---PLFTIADLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFIDPAVD--PATRTVRVRA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 280 EVPNEQHLLRLQMTAQVKILLEHKKDILLVPLSALGEDVGinEYQVEVLV-NGQPEKRVVKIGIRTDVYAEVISGLNEND 358
Cdd:COG0845 223 ELPNPDGLLRPGMFVRVRIVLGERENALLVPASAVVRDGG--GAYVFVVDaDGKVERRPVTLGRRDGDQVEVLSGLKAGD 300
|
....
gi 490364890 359 DVIL 362
Cdd:COG0845 301 RVVV 304
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
38-362 |
7.49e-57 |
|
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: 188.29 E-value: 7.49e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 38 TQKITRGELSKEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAqnevaesQETNNELTANLQQ 117
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDY-------QLALQAALAQLAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 118 AKAELRLAQLTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARVATYEAQirknqatLDTARTNLQYTRITAPMDGVVTFI 197
Cdd:TIGR01730 76 AEAQLELAQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKAS-------LASAQLNLRYTEIRAPFDGTIGRR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 198 KTLEGQTVIAAQeapTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDILPTPEKINDAIFYYA 277
Cdd:TIGR01730 149 LVEVGAYVTAGQ---TLATIVDLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTGTVRVRA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 278 RFevPNEQHLLRLQMTAQVKILLEHKKDILLVPLSALGEDvgINEYQVEVLVN-GQPEKRVVKIGIRTDVYAEVISGLNE 356
Cdd:TIGR01730 226 TF--PNPDGRLLPGMFGRVTISLKVRSSAIVVPTQAVIED--LNGKYVYVVKNdGKVSKRPVEVGLRNGGYVEIESGLKA 301
|
....*.
gi 490364890 357 NDDVIL 362
Cdd:TIGR01730 302 GDQIVT 307
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
47-301 |
2.25e-49 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 169.07 E-value: 2.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 47 SKEVTATGKLDAvRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVAESQ--------------------E 106
Cdd:COG1566 32 DEPVTADGRVEA-RVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEaqlaaaeaqlarleaelgaeA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 107 TNNELTANLQQAKAELRLAQLTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARV--------------------ATYEAQ 166
Cdd:COG1566 111 EIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLeaaqaqlaqaqaglreeeelAAAQAQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 167 IRKNQATLDTARTNLQYTRITAPMDGVVTFIKTLEGQTVIAAQeapTILTLADLDTMLVKAEVSEADVIYLKPDLKASFT 246
Cdd:COG1566 191 VAQAEAALAQAELNLARTTIRAPVDGVVTNLNVEPGEVVSAGQ---PLLTIVPLDDLWVEAYVPETDLGRVKPGQPVEVR 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490364890 247 VLGAPDKAFNGKLKDILPTPEKI--------NDAIFYYARFEVPNEQ-HLLRLQMTAQVKILLE 301
Cdd:COG1566 268 VDAYPDRVFEGKVTSISPGAGFTsppknatgNVVQRYPVRIRLDNPDpEPLRPGMSATVEIDTE 331
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
43-267 |
7.24e-26 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 106.20 E-value: 7.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 43 RGELSKEVTATGKLDaVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDP-------KKAQNEVAESQETNNELTAN- 114
Cdd:PRK03598 26 QSRQDNGLTLYGNVD-IRTVNLGFRVGGRLASLAVDEGDAVKAGQVLGELDAapyenalMQAKANVSVAQAQLDLMLAGy 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 115 -----------LQQAKAELRLAQLTYQRQLKLIGTHVIAQEELDRTKT-----DVEVKKAR--------------VATYE 164
Cdd:PRK03598 105 rdeeiaqaraaVKQAQAAYDYAQNFYNRQQGLWKSRTISANDLENARSsrdqaQATLKSAQdklsqyregnrpqdIAQAK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 165 AQIRKNQATLDTARTNLQYTRITAPMDGVVtFIKTLEGQTVIAAQEapTILTLADLDTMLVKAEVSEADVIYLKPDLKAS 244
Cdd:PRK03598 185 ASLAQAQAALAQAELNLQDTELIAPSDGTI-LTRAVEPGTMLNAGS--TVFTLSLTRPVWVRAYVDERNLGQAQPGRKVL 261
|
250 260
....*....|....*....|...
gi 490364890 245 FTVLGAPDKAFNGKLKDILPTPE 267
Cdd:PRK03598 262 LYTDGRPDKPYHGQIGFVSPTAE 284
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
45-294 |
2.43e-25 |
|
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: 101.81 E-value: 2.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 45 ELSKEVTATGKL--DAVRKVDVGAQVSGQLQTLYVK-EGDVVKKGDLLAIID-PK--KAQNEVAESQETNNELTAN--LQ 116
Cdd:pfam16576 1 PLSRTIRAVGRVayDERRLAHVHARVEGWIEKLYVNaTGDPVKKGQPLAELYsPElvAAQQEYLLALRSGDALSKSelLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 117 QAKAELRLAQLTyqrqlkligthviaqeeldrtktdvevkkarvatyEAQIrknqATLDTARTNLQYTRITAPMDGVVTF 196
Cdd:pfam16576 81 AARQRLRLLGMP-----------------------------------EAQI----AELERTGKVQPTVTVYAPISGVVTE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 197 IKTLEGQTVIAAQeapTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDILPTPEKINDAIfyY 276
Cdd:pfam16576 122 LNVREGMYVQPGD---TLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDYIYPTLDPKTRTV--R 196
|
250
....*....|....*...
gi 490364890 277 ARFEVPNEQHLLRLQMTA 294
Cdd:pfam16576 197 VRIELPNPDGRLKPGMFA 214
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
33-361 |
7.89e-23 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 98.71 E-value: 7.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 33 LPSYQTQKITRGELSKEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVAESQetnnelt 112
Cdd:PRK11556 59 LAPVQAATATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQ------- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 113 ANLQQAKAELRLAQLTYQRQLKLIGTHVIAQEELDrtktdveVKKARVATYEAQIRKNQATLDTARTNLQYTRITAPMDG 192
Cdd:PRK11556 132 GQLAKDQATLANARRDLARYQQLAKTNLVSRQELD-------AQQALVSETEGTIKADEASVASAQLQLDYSRITAPISG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 193 VVTfIKTLEGQTVIAAQEAPTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTV-LGAPDKAFNGKLKD--ILPTPEKI 269
Cdd:PRK11556 205 RVG-LKQVDVGNQISSGDTTGIVVITQTHPIDLVFTLPESDIATVVQAQKAGKPLvVEAWDRTNSKKLSEgtLLSLDNQI 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 270 NDA---IFYYARFevPNEQHLLRLQMTAQVKILLEHKKDILLVPLSALgeDVGINEYQVEVL-VNGQPEKRVVKIGIRTD 345
Cdd:PRK11556 284 DATtgtIKLKARF--NNQDDALFPNQFVNARMLVDTLQNAVVIPTAAL--QMGNEGHFVWVLnDENKVSKHLVTPGIQDS 359
|
330
....*....|....*.
gi 490364890 346 VYAEVISGLNENDDVI 361
Cdd:PRK11556 360 QKVVISAGLSAGDRVV 375
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
43-362 |
1.60e-22 |
|
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: 96.72 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 43 RGELSKEVTATGKLDAVRKVD-VGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVAESQetnneltANLQQAKAE 121
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKaVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAE-------AQLAKAQAQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 122 LRLAQLTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARVATYEAQirknqatLDTARTNLQYTRITAPMDGVVTFIKTLE 201
Cdd:pfam00529 74 VARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQ-------LAQAQIDLARRRVLAPIGGISRESLVTA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 202 GQTVIAAQ-----------------EAPTILTLADLDTMLVKAE--VSEADVIYLKPDLKASFTVLGAPdkaFNGKLKDI 262
Cdd:pfam00529 147 GALVAQAQanllatvaqldqiyvqiTQSAAENQAEVRSELSGAQlqIAEAEAELKLAKLDLERTEIRAP---VDGTVAFL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 263 LPTPEKINDAIFYYARFEVPnEQHLLRLQMTAQVKILLEHKKDILLVPLSALGEDVGINEYQVEVLVNGQPEKRVVKIGI 342
Cdd:pfam00529 224 SVTVDGGTVSAGLRLMFVVP-EDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRVVVDK 302
|
330 340
....*....|....*....|
gi 490364890 343 RTDVYAEVISGLNENDDVIL 362
Cdd:pfam00529 303 AQGPYYPLRIGLSAGALVRL 322
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
61-262 |
1.15e-21 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 94.71 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 61 KVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPK---------KAQNEVAESQ----------ETNNELTANLQ--QAK 119
Cdd:PRK10476 48 VVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRpyeltvaqaQADLALADAQimttqrsvdaERSNAASANEQveRAR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 120 AELRLAQLTYQRQLKLIGTHVIAQEELDRTKT-----DVEVKKAR------------VATYEAQIRKNQATLDTARTNLQ 182
Cdd:PRK10476 128 ANAKLATRTLERLEPLLAKGYVSAQQVDQARTaqrdaEVSLNQALlqaqaaaaavggVDALVAQRAAREAALAIAELHLE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 183 YTRITAPMDGVVTFIKTLEGQTVIAAQeapTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDI 262
Cdd:PRK10476 208 DTTVRAPFDGRVVGLKVSVGEFAAPMQ---PIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYSMIDRGRPFEGKVDSI 284
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
54-310 |
2.17e-18 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 85.92 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 54 GKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPkkaqnevAESQETNNELTANLQQAKAELRLAQLTYQRQL 133
Cdd:PRK15030 58 GRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDP-------ATYQATYDSAKGDLAKAQAAANIAQLTVNRYQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 134 KLIGTHVIAQEELDRTKTDVEVKKARVATYEAQIrknqatlDTARTNLQYTRITAPMDGVVTFIKTLEGQTVIAAQeAPT 213
Cdd:PRK15030 131 KLLGTQYISKQEYDQALADAQQANAAVTAAKAAV-------ETARINLAYTKVTSPISGRIGKSNVTEGALVQNGQ-ATA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 214 ILTLADLDTMLVKAEVSEADVIYLKPDLkASFTVlgapdKAFNGKLKDILPTPEKI---NDAIFYYARFEV--------- 281
Cdd:PRK15030 203 LATVQQLDPIYVDVTQSSNDFLRLKQEL-ANGTL-----KQENGKAKVSLITSDGIkfpQDGTLEFSDVTVdqttgsitl 276
|
250 260 270
....*....|....*....|....*....|...
gi 490364890 282 ----PNEQHLLRLQMTAQVKILLEHKKDILLVP 310
Cdd:PRK15030 277 raifPNPDHTLLPGMFVRARLEEGLNPNAILVP 309
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
33-310 |
3.86e-15 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 75.91 E-value: 3.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 33 LPSYQTQKITRGELSKEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVaesqetnNELT 112
Cdd:PRK09859 33 TPEVGVVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAEL-------NSAK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 113 ANLQQAKAELRLAQLTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARVATYEAQIRknQATLdtartNLQYTRITAPMDG 192
Cdd:PRK09859 106 GSLAKALSTASNARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVE--QATI-----NLQYANVTSPITG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 193 VVTFIKTLEGQTVIAAQeAPTILTLADLDTMLVKAEVSEADVIYLKPDLKAS--FTVLGAPDKAFN----------GKLK 260
Cdd:PRK09859 179 VSGKSSVTVGALVTANQ-ADSLVTVQRLDPIYVDLTQSVQDFLRMKEEVASGqiKQVQGSTPVQLNlengkrysqtGTLK 257
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490364890 261 DILPTPEKINDAIFYYARFEVPNEQHLLRLQMTAqvkiLLEH--KKDILLVP 310
Cdd:PRK09859 258 FSDPTVDETTGSVTLRAIFPNPNGDLLPGMYVTA----LVDEgsRQNVLLVP 305
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
61-195 |
1.30e-13 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 71.26 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 61 KVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDP-------KKAQNEVAESQETNNELTANLQQAKA-------ELRLAQ 126
Cdd:PRK15136 61 QVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPtdaeqafEKAKTALANSVRQTHQLMINSKQYQAnielqktALAQAQ 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 127 LTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARVATYEAQIRKNQAT-LDT-----------------ARTNLQYTRITA 188
Cdd:PRK15136 141 SDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAIQQYNANQAMiLNTpledqpavqqaatevrnAWLALQRTKIVS 220
|
....*..
gi 490364890 189 PMDGVVT 195
Cdd:PRK15136 221 PMTGYVS 227
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
185-289 |
2.67e-12 |
|
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: 62.76 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 185 RITAPMDGVVTFIKTLEGQTVIAAQEaptILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDILP 264
Cdd:pfam13437 1 TIRAPVDGVVAELNVEEGQVVQAGDP---LATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKVVRISP 77
|
90 100
....*....|....*....|....*
gi 490364890 265 TPEKINDAIFYYARFEVPNEQHLLR 289
Cdd:pfam13437 78 TVDPDTGVIPVRVSIENPKTPIPLL 102
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
57-262 |
2.78e-12 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 66.69 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 57 DAVRKVDVGA---QVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVAESQETNNELTANLQQAKAElrlaqltYQRQL 133
Cdd:PRK10559 40 DARFSADVVAiapDVSGLITQVNVHDNQLVKKGQVLFTIDQPRYQKALAEAEADVAYYQVLAQEKRRE-------AGRRN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 134 KLiGTHVIAQEELDRTKTDVEvkkarvaTYEAQIRKNQATLDTARTNLQYTRITAPMDGVVTFIKTLEGQTViaaQEAPT 213
Cdd:PRK10559 113 RL-GVQAMSREEIDQANNVLQ-------TVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFI---TRGST 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490364890 214 ILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGApDKAFNGKLKDI 262
Cdd:PRK10559 182 AVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGS-NKVLKGTVDSV 229
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
72-262 |
5.06e-12 |
|
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. DevB from Anabaena sp. strain PCC 7120 is partially characterized as a membrane fusion protein of the DevBCA ABC exporter, probably a glycolipid exporter, required for heterocyst formation. Most Cyanobacteria have one member only, but Nostoc sp. PCC 7120 has seven members.
Pssm-ID: 213754 [Multi-domain] Cd Length: 327 Bit Score: 66.00 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 72 LQTLYVKEGDVVKKGDLLAIID--PKKAQN-EVAESQ---------------------------------ETNNELTANL 115
Cdd:TIGR02971 27 IKKLLVAEGDRVQAGQVLAELDsrPERTAElDVARTQldeakarlaqvragakkgeiaaqraaraaaklfKDVAAQQATL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 116 QQAKAELRLAQLTYQR-------------------------QLKLIGTHVIAQEELDRTK-----TDVEVKKARVATYEA 165
Cdd:TIGR02971 107 NRLEAELETAQREVDRyrslfrdgavsasdldskalklrtaEEELEEALASRSEQIDGARaalasLAEEVRETDVDLAQA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 166 QIRKNQATLDTARTNLQYTRITAPMDGVVTFIKTLEGQTViaAQEAptILTLADLDTMLVKAEVSEADVIYLKPDLKASF 245
Cdd:TIGR02971 187 EVKSALEAVQQAEALLELTYVKAPIDGRVLKIHAREGEVI--GSEG--ILEMGDTSQMYAVAEVYETDINRVRVGQRATI 262
|
250
....*....|....*..
gi 490364890 246 TVLGAPDKAfNGKLKDI 262
Cdd:TIGR02971 263 TSTALSGPL-RGTVRRI 278
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
49-243 |
5.15e-12 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 66.36 E-value: 5.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 49 EVTATGKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPK--KAQNEVAESQetnneltanLQQAKAELRLAQ 126
Cdd:PRK09578 51 TVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQGAVLFRIDPAplKAARDAAAGA---------LAKAEAAHLAAL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 127 LTYQRQLKLIGTHVIAQEELDRTKTDVEVKKARVATYEAQirknqatLDTARTNLQYTRITAPMDGVVTFIKTLEGQTVi 206
Cdd:PRK09578 122 DKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAE-------LARAQLQLDYATVTAPIDGRARRALVTEGALV- 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 490364890 207 aAQEAPTILTLAD-LDTMLVKAEVSEADVIYLKPDLKA 243
Cdd:PRK09578 194 -GQDQATPLTTVEqLDPIYVNFSQPAADVEALRRAVKS 230
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
60-105 |
2.29e-07 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 47.05 E-value: 2.29e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490364890 60 RKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDP--KKAQNEVAESQ 105
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSpeLQLQLQQAEAQ 48
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
37-361 |
3.96e-07 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 51.41 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 37 QTQKITRGEL--SKEVTATGKLDAVRKVDVGAQVSGQLQTLY-VKEGDVVKKGDLL---AIIDPKKAQNEVAESQETNNE 110
Cdd:PRK09783 97 KTATVTRGPLtfAQTFPANVSYNEYQYAIVQARAAGFIDKVYpLTVGDKVQKGTPLldlTIPDWVEAQSEYLLLRETGGT 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 111 LTaNLQQAKAELRLAQLTyqrqlkligthviaqeeldrtktdvevkkarvatyEAQIRKNQATldtARTNLQYTrITAPM 190
Cdd:PRK09783 177 AT-QTEGILERLRLAGMP-----------------------------------EADIRRLIAT---RKIQTRFT-LKAPI 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 191 DGVVTFIKTLEGQTViaaQEAPTILTLADLDTMLVKAEVSEADVIYLKPDLKASFTVLGAPDKAFNGKLKDILPTPEKIN 270
Cdd:PRK09783 217 DGVITAFDLRAGMNI---AKDNVVAKIQGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTFTIRKWTLLPSVDAAT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 271 DAIfyYARFEVPNEQHLLRLQMTAQVKiLLEHKKDILLVPLSALgEDVGINEYQVEVLVNGQPEKRVVKIGIRTDVYAEV 350
Cdd:PRK09783 294 RTL--QLRLEVDNADEALKPGMNAWLQ-LNTASEPMLLIPSQAL-IDTGSEQRVITVDADGRFVPKRVAVFQESQGVTAI 369
|
330
....*....|.
gi 490364890 351 ISGLNENDDVI 361
Cdd:PRK09783 370 RSGLAEGEKVV 380
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
44-182 |
9.86e-07 |
|
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: 50.39 E-value: 9.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 44 GELSKEVTATGKLDAV--RKVdVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVAESQETNNELTANLQQAKAE 121
Cdd:TIGR01843 25 APLDVVATATGKVVPSgnVKV-VQHLEGGIVREILVREGDRVKAGQVLVELDATDVEADAAELESQVLRLEAEVARLRAE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490364890 122 LRLAQLTYQRQLKLIGT-----HVIAQEE--LDRTKTdveVKKARVATYEAQIRKNQATLDTARTNLQ 182
Cdd:TIGR01843 104 ADSQAAIEFPDDLLSAEdpavpELIKGQQslFESRKS---TLRAQLELILAQIKQLEAELAGLQAQLQ 168
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
48-92 |
2.94e-05 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 46.28 E-value: 2.94e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 490364890 48 KEVTATGKldAVRKVD------VGAQVSGQLQTLYVKEGDVVKKGDLLAII 92
Cdd:PRK12999 1059 RSVKSTVA--AREKADpgnpghVGAPMPGSVVTVLVKEGDEVKAGDPLAVI 1107
|
|
| PRK09282 |
PRK09282 |
pyruvate carboxylase subunit B; Validated |
48-101 |
2.47e-04 |
|
pyruvate carboxylase subunit B; Validated
Pssm-ID: 236449 [Multi-domain] Cd Length: 592 Bit Score: 42.91 E-value: 2.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 490364890 48 KEVTATGKLDAVRKVDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEV 101
Cdd:PRK09282 509 KEIVVGGRPRASAPGAVTSPMPGTVVKVKVKEGDKVKAGDTVLVLEAMKMENEI 562
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
64-101 |
2.47e-04 |
|
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: 38.94 E-value: 2.47e-04
10 20 30
....*....|....*....|....*....|....*...
gi 490364890 64 VGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEV 101
Cdd:cd06850 2 VTAPMPGTVVKVLVKEGDKVEAGQPLAVLEAMKMENEV 39
|
|
| PRK11855 |
PRK11855 |
dihydrolipoamide acetyltransferase; Reviewed |
62-205 |
4.57e-04 |
|
dihydrolipoamide acetyltransferase; Reviewed
Pssm-ID: 237000 [Multi-domain] Cd Length: 547 Bit Score: 42.12 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 62 VDVGAQVSGQLQTLYVKEGDVVKKGDLLAIIDPKKAQNEVAESQETNNELTANLQQAKAELRLAQLTYQ------RQLKL 135
Cdd:PRK11855 45 MEIPSPAAGVVKEIKVKVGDTVSVGGLLAVIEAAGAAAAAAAPAAAAAPAAAAAAAPAPAAAAPAAAAAaagggvVEVKV 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490364890 136 --IGTHViaqeeldrtktDVEVKKARVATYEaQIRKNQ--ATLDTARTNLQytrITAPMDGVVTFIKTLEGQTV 205
Cdd:PRK11855 125 pdIGEIT-----------EVEVIEWLVKVGD-TVEEDQslITVETDKATME---IPSPVAGVVKEIKVKVGDKV 183
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
51-92 |
6.95e-04 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 41.60 E-value: 6.95e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 490364890 51 TATGKLDAVRKVD------VGAQVSGQLQTLYVKEGDVVKKGDLLAII 92
Cdd:COG1038 1060 SVKVTVASREKADpgnpghIGAPMPGTVVKVLVKEGDEVKKGDPLLTI 1107
|
|
| type_I_sec_TolC |
TIGR01844 |
type I secretion outer membrane protein, TolC family; Members of this model are outer membrane ... |
111-187 |
1.93e-03 |
|
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: 40.05 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 111 LTANLQQAKAELRLAQL-TYQRQLKLigthviAQEELDR---TKTDVEVKKARVATYEAQIRKNQATLDTARTnlQYTRI 186
Cdd:TIGR01844 120 MEVLRAQEILALAEANLaALKEQLDL------ARARFDVglgTRTDVLQAEARYASARAQLIQAQNNLDDAKA--QLRRL 191
|
.
gi 490364890 187 T 187
Cdd:TIGR01844 192 V 192
|
|
| sucB |
TIGR01347 |
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This ... |
62-185 |
2.85e-03 |
|
2-oxoglutarate dehydrogenase complex dihydrolipoamide succinyltransferase (E2 component); This model describes the TCA cycle 2-oxoglutarate system E2 component, dihydrolipoamide succinyltransferase. It is closely related to the pyruvate dehydrogenase E2 component, dihydrolipoamide acetyltransferase. The seed for this model includes mitochondrial and Gram-negative bacterial forms. Mycobacterial candidates are highly derived, differ in having and extra copy of the lipoyl-binding domain at the N-terminus. They score below the trusted cutoff, but above the noise cutoff and above all examples of dihydrolipoamide acetyltransferase. [Energy metabolism, TCA cycle]
Pssm-ID: 273565 [Multi-domain] Cd Length: 403 Bit Score: 39.33 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490364890 62 VDVGAQVSGQLQTLYVKEGDVVKKGDLLAII----DPKKAQNEVA-ESQETNNELTANLQQAKAELRLAQLTYQRqlKLI 136
Cdd:TIGR01347 44 LEVPSPADGVLQEILFKEGDTVESGQVLAILeegnDATAAPPAKSgEEKEETPAASAAAAPTAAANRPSLSPAAR--RLA 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490364890 137 GTHVIAQEELDRTKTDVEVKKARVATYEAQIRKNQ--ATLDTARTNLQYTR 185
Cdd:TIGR01347 122 KEHGIDLSAVPGTGVTGRVTKEDIIKKTEAPASAQppAAAAAAAAPAAATR 172
|
|
| CARDB |
pfam07705 |
CARDB; Cell adhesion related domain found in bacteria. |
76-113 |
2.97e-03 |
|
CARDB; Cell adhesion related domain found in bacteria.
Pssm-ID: 400172 [Multi-domain] Cd Length: 101 Bit Score: 36.87 E-value: 2.97e-03
10 20 30
....*....|....*....|....*....|....*...
gi 490364890 76 YVKEGDVvkkgDLLAIIDPkkaQNEVAESQETNNELTA 113
Cdd:pfam07705 71 PPTEGSY----TLTVVVDP---DNTVAESNETNNELTK 101
|
|
| AceF |
COG0508 |
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component ... |
62-92 |
3.21e-03 |
|
Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component [Energy production and conversion]; Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide acyltransferase (E2) component is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440274 [Multi-domain] Cd Length: 77 Bit Score: 36.20 E-value: 3.21e-03
10 20 30
....*....|....*....|....*....|.
gi 490364890 62 VDVGAQVSGQLQTLYVKEGDVVKKGDLLAII 92
Cdd:COG0508 46 MEVPAPAAGVLLEILVKEGDTVPVGAVIAVI 76
|
|
| biotinyl_domain |
cd06850 |
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all ... |
66-92 |
8.61e-03 |
|
The biotinyl-domain or biotin carboxyl carrier protein (BCCP) domain is present in all biotin-dependent enzymes, such as acetyl-CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, methylcrotonyl-CoA carboxylase, geranyl-CoA carboxylase, oxaloacetate decarboxylase, methylmalonyl-CoA decarboxylase, transcarboxylase and urea amidolyase. This domain functions in transferring CO2 from one subsite to another, allowing carboxylation, decarboxylation, or transcarboxylation. During this process, biotin is covalently attached to a specific lysine.
Pssm-ID: 133459 [Multi-domain] Cd Length: 67 Bit Score: 34.70 E-value: 8.61e-03
10 20
....*....|....*....|....*..
gi 490364890 66 AQVSGQLQTLYVKEGDVVKKGDLLAII 92
Cdd:cd06850 41 APVAGVVKEILVKEGDQVEAGQLLVVI 67
|
|
| |
