|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
37-396 |
1.42e-70 |
|
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: 225.59 E-value: 1.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 37 VEKGDIVSLVSATGTINPVETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKSRAQYIQAEQ 116
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 117 DYKRVKYLVEQKVKSNSELDQAKASYEVAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANfsaPVL 196
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG---TPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 197 FQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVKQVRllPTTVQNVVNYSVVVEVENPGNVLLPGMT 276
Cdd:COG0845 160 FTIA-DLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFID--PAVDPATRTVRVRAELPNPDGLLRPGMF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 277 ATVDFITAKAEQVLKVPNgvlrfkattkmmetfrkrlaqrrgengaekgGALRNGNNGrrgegsplggslngngmakkiN 356
Cdd:COG0845 237 VRVRIVLGERENALLVPA-------------------------------SAVVRDGGG---------------------A 264
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1167106414 357 LLWYLDKKGELQATPVRLGATDGQMTEIRSDkIYEGMMVI 396
Cdd:COG0845 265 YVFVVDADGKVERRPVTLGRRDGDQVEVLSG-LKAGDRVV 303
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
8-293 |
3.35e-43 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 155.32 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 8 IAILAVVAGCVWWFYGREKSQEFSYQLVAVEKGDIVSLVSATGTINPVETVDVGTQVSGRIDKLYADYNDHVTKGQLVAT 87
Cdd:PRK11578 12 LIALVIVLAGGITLWRILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 88 LDRSLLENAVLDAESSLQKSRAQYIQAEQD-------YKRVKYLVEQKVKSNSELDQAKASYEVAK-------WNLKSQE 153
Cdd:PRK11578 92 IDPEQAENQIKEVEATLMELRAQRQQAEAElklarvtLSRQQRLAKTQAVSQQDLDTAATELAVKQaqigtidAQIKRNQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 154 SNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANFSAPVLFQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSY 233
Cdd:PRK11578 172 ASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLA-DMSTMLVKAQVSEADVIHLKPGQKAWFTVLGD 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 234 PDRTFMGKVKQVRLLPTTVQNVVNYSVVVEVENPGNVLLPGMTATVDFITAKAEQVLKVP 293
Cdd:PRK11578 251 PLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIP 310
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
34-293 |
2.64e-42 |
|
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: 151.70 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 34 LVAVEKGDIVSLVSATGTINPVETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKSRAQYIQ 113
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 114 AEQDYKRVKYLVEQKVKSNSELDQAKASYEVAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANfsa 193
Cdd:TIGR01730 83 AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 194 PVLFQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVKQVRllPTTVQNVVNYSVVVEVENPGNVLLP 273
Cdd:TIGR01730 160 QTLATIV-DLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFID--PRVDSGTGTVRVRATFPNPDGRLLP 236
|
250 260
....*....|....*....|
gi 1167106414 274 GMTATVDFITAKAEQVLKVP 293
Cdd:TIGR01730 237 GMFGRVTISLKVRSSAIVVP 256
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
46-277 |
1.56e-30 |
|
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: 116.84 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 46 VSATGTINPVET--VDVGTQVSGRIDKLYADYN-DHVTKGQLVATLDRSLLENAvldaesslqksRAQYIQAEQDYKrvk 122
Cdd:pfam16576 6 IRAVGRVAYDERrlAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYSPELVAA-----------QQEYLLALRSGD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 123 ylveqKVKSNSELDQAKASYEVakWNL-KSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAAnfsAPVLFQIAk 201
Cdd:pfam16576 72 -----ALSKSELLRAARQRLRL--LGMpEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQP---GDTLFTIA- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 202 DLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVK-------------QVRL-LPttvqnvvnysvvveveNP 267
Cdd:pfam16576 141 DLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDyiyptldpktrtvRVRIeLP----------------NP 204
|
250
....*....|
gi 1167106414 268 GNVLLPGMTA 277
Cdd:pfam16576 205 DGRLKPGMFA 214
|
|
| F-BAR_Rgd1 |
cd07652 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ... |
93-128 |
1.53e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153336 [Multi-domain] Cd Length: 234 Bit Score: 40.02 E-value: 1.53e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1167106414 93 LENAVLDAESSLQKSRAQYIQAEQDYKRVKYLVEQK 128
Cdd:cd07652 116 AEKKVQDAEAAAEKAKARYDSLADDLERVKTGDPGK 151
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
37-396 |
1.42e-70 |
|
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: 225.59 E-value: 1.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 37 VEKGDIVSLVSATGTINPVETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKSRAQYIQAEQ 116
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLAAAQAQLELAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 117 DYKRVKYLVEQKVKSNSELDQAKASYEVAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANfsaPVL 196
Cdd:COG0845 83 ELERYKALLKKGAVSQQELDQAKAALDQAQAALAAAQAALEQARANLAYTTIRAPFDGVVGERNVEPGQLVSAG---TPL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 197 FQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVKQVRllPTTVQNVVNYSVVVEVENPGNVLLPGMT 276
Cdd:COG0845 160 FTIA-DLDPLEVEFDVPESDLARLKVGQPVTVTLDAGPGKTFEGKVTFID--PAVDPATRTVRVRAELPNPDGLLRPGMF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 277 ATVDFITAKAEQVLKVPNgvlrfkattkmmetfrkrlaqrrgengaekgGALRNGNNGrrgegsplggslngngmakkiN 356
Cdd:COG0845 237 VRVRIVLGERENALLVPA-------------------------------SAVVRDGGG---------------------A 264
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1167106414 357 LLWYLDKKGELQATPVRLGATDGQMTEIRSDkIYEGMMVI 396
Cdd:COG0845 265 YVFVVDADGKVERRPVTLGRRDGDQVEVLSG-LKAGDRVV 303
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1-283 |
5.39e-49 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 169.46 E-value: 5.39e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 1 MRKVFVAIAILAVVAGCVWWFYGREKSQEfsyqlvavekgdivslVSATGTInPVETVDVGTQVSGRIDKLYADYNDHVT 80
Cdd:COG1566 6 KRRLLALVLLLLALGLALWAAGRNGPDEP----------------VTADGRV-EARVVTVAAKVSGRVTEVLVKEGDRVK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 81 KGQLVATLDRSLLENAVLDAESSLQKSRAQYIQ---------------------------AEQDYKRVKYLVEQKVKSNS 133
Cdd:COG1566 69 KGQVLARLDPTDLQAALAQAEAQLAAAEAQLARleaelgaeaeiaaaeaqlaaaqaqldlAQRELERYQALYKKGAVSQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 134 ELDQAKASYEVAKWNLKSQESNLSR---------------------------AKLNLSYASIFSPVDGIVIARNVNAGQT 186
Cdd:COG1566 149 ELDEARAALDAAQAQLEAAQAQLAQaqaglreeeelaaaqaqvaqaeaalaqAELNLARTTIRAPVDGVVTNLNVEPGEV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 187 VAANFSapvLFQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVKQVRLLPTTVQNVVNYSVVVEV-- 264
Cdd:COG1566 229 VSAGQP---LLTIV-PLDDLWVEAYVPETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNATGNVVQry 304
|
330 340
....*....|....*....|....*.
gi 1167106414 265 -------ENPGNVLLPGMTATVDFIT 283
Cdd:COG1566 305 pvrirldNPDPEPLRPGMSATVEIDT 330
|
|
| PRK11578 |
PRK11578 |
macrolide transporter subunit MacA; Provisional |
8-293 |
3.35e-43 |
|
macrolide transporter subunit MacA; Provisional
Pssm-ID: 183211 [Multi-domain] Cd Length: 370 Bit Score: 155.32 E-value: 3.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 8 IAILAVVAGCVWWFYGREKSQEFSYQLVAVEKGDIVSLVSATGTINPVETVDVGTQVSGRIDKLYADYNDHVTKGQLVAT 87
Cdd:PRK11578 12 LIALVIVLAGGITLWRILNAPVPTYQTLIVRPGDLQQSVLATGKLDALRKVDVGAQVSGQLKTLSVAIGDKVKKDQLLGV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 88 LDRSLLENAVLDAESSLQKSRAQYIQAEQD-------YKRVKYLVEQKVKSNSELDQAKASYEVAK-------WNLKSQE 153
Cdd:PRK11578 92 IDPEQAENQIKEVEATLMELRAQRQQAEAElklarvtLSRQQRLAKTQAVSQQDLDTAATELAVKQaqigtidAQIKRNQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 154 SNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANFSAPVLFQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSY 233
Cdd:PRK11578 172 ASLDTAKTNLDYTRIVAPMAGEVTQITTLQGQTVIAAQQAPNILTLA-DMSTMLVKAQVSEADVIHLKPGQKAWFTVLGD 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 234 PDRTFMGKVKQVRLLPTTVQNVVNYSVVVEVENPGNVLLPGMTATVDFITAKAEQVLKVP 293
Cdd:PRK11578 251 PLTRYEGVLKDILPTPEKVNDAIFYYARFEVPNPNGLLRLDMTAQVHIQLTDVKNVLTIP 310
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
34-293 |
2.64e-42 |
|
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: 151.70 E-value: 2.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 34 LVAVEKGDIVSLVSATGTINPVETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKSRAQYIQ 113
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 114 AEQDYKRVKYLVEQKVKSNSELDQAKASYEVAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANfsa 193
Cdd:TIGR01730 83 AQRSFERAERLVKRNAVSQADLDDAKAAVEAAQADLEAAKASLASAQLNLRYTEIRAPFDGTIGRRLVEVGAYVTAG--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 194 PVLFQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVKQVRllPTTVQNVVNYSVVVEVENPGNVLLP 273
Cdd:TIGR01730 160 QTLATIV-DLDPLEADFSVPERDLPQLRRGQTLTVELDALPGEEFKGKLRFID--PRVDSGTGTVRVRATFPNPDGRLLP 236
|
250 260
....*....|....*....|
gi 1167106414 274 GMTATVDFITAKAEQVLKVP 293
Cdd:TIGR01730 237 GMFGRVTISLKVRSSAIVVP 256
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
46-277 |
1.56e-30 |
|
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: 116.84 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 46 VSATGTINPVET--VDVGTQVSGRIDKLYADYN-DHVTKGQLVATLDRSLLENAvldaesslqksRAQYIQAEQDYKrvk 122
Cdd:pfam16576 6 IRAVGRVAYDERrlAHVHARVEGWIEKLYVNATgDPVKKGQPLAELYSPELVAA-----------QQEYLLALRSGD--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 123 ylveqKVKSNSELDQAKASYEVakWNL-KSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAAnfsAPVLFQIAk 201
Cdd:pfam16576 72 -----ALSKSELLRAARQRLRL--LGMpEAQIAELERTGKVQPTVTVYAPISGVVTELNVREGMYVQP---GDTLFTIA- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 202 DLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVK-------------QVRL-LPttvqnvvnysvvveveNP 267
Cdd:pfam16576 141 DLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGKVDyiyptldpktrtvRVRIeLP----------------NP 204
|
250
....*....|
gi 1167106414 268 GNVLLPGMTA 277
Cdd:pfam16576 205 DGRLKPGMFA 214
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
1-242 |
3.13e-26 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 108.13 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 1 MRKVFVAIAILAVVAGCV--WWFYGREKSQEFS-YQLVavekgDIvslvsatgtinpvETVDVGTQVSGRIDKLYADYND 77
Cdd:PRK03598 2 KKKVVIGLAVVVLAAAVAggWWWYQSRQDNGLTlYGNV-----DI-------------RTVNLGFRVGGRLASLAVDEGD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 78 HVTKGQLVATLDRSLLENAVLDAESSLQKSRAQ--------------------------YIQAEQDYKRVKYLVEQKVKS 131
Cdd:PRK03598 64 AVKAGQVLGELDAAPYENALMQAKANVSVAQAQldlmlagyrdeeiaqaraavkqaqaaYDYAQNFYNRQQGLWKSRTIS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 132 NSELDQAKAS-----------------YE---------VAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQ 185
Cdd:PRK03598 144 ANDLENARSSrdqaqatlksaqdklsqYRegnrpqdiaQAKASLAQAQAALAQAELNLQDTELIAPSDGTILTRAVEPGT 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167106414 186 TVAANFSAPVLfqiakDLSK-MQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKV 242
Cdd:PRK03598 224 MLNAGSTVFTL-----SLTRpVWVRAYVDERNLGQAQPGRKVLLYTDGRPDKPYHGQI 276
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
5-248 |
3.08e-16 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 80.22 E-value: 3.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 5 FVAIAILAVVAGCVWWFYGREKSQEFS-------------------------YQLVAVEKGDIVSLVSATGTINPVETVD 59
Cdd:PRK11556 10 VIVIVVVIAAIAAFWFWQGRSTSSSAApgaakqaqqspaggrrgmrsgplapVQAATATEQAVPRYLTGLGTVTAANTVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 60 VGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKSRAQYIQAEQDYKRVKYLVEQKVKSNSELDQAK 139
Cdd:PRK11556 90 VRSRVDGQLMALHFQEGQQVKAGDLLAEIDPRPFKVALAQAQGQLAKDQATLANARRDLARYQQLAKTNLVSRQELDAQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 140 ASYEVAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANFSAPVLfqIAKDLSKMQILANVDEGDVGQ 219
Cdd:PRK11556 170 ALVSETEGTIKADEASVASAQLQLDYSRITAPISGRVGLKQVDVGNQISSGDTTGIV--VITQTHPIDLVFTLPESDIAT 247
|
250 260 270
....*....|....*....|....*....|...
gi 1167106414 220 I----KEGQQVkfTVQSYpDRTFMGKVKQVRLL 248
Cdd:PRK11556 248 VvqaqKAGKPL--VVEAW-DRTNSKKLSEGTLL 277
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
46-190 |
1.47e-15 |
|
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: 77.08 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 46 VSATGTINPV-ETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKSRAQYIQAEQDYKRVKYL 124
Cdd:pfam00529 8 VEAPGRVVVSgNAKAVQPQVSGIVTRVLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQAL 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1167106414 125 VEQKVKSNSELDQAKASYEVAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAAN 190
Cdd:pfam00529 88 ESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQA 153
|
|
| PRK09859 |
PRK09859 |
multidrug transporter subunit MdtE; |
34-293 |
3.00e-14 |
|
multidrug transporter subunit MdtE;
Pssm-ID: 137559 [Multi-domain] Cd Length: 385 Bit Score: 73.98 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 34 LVAVEKGDIVSLVSATGTINPVETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKSRAQYIQ 113
Cdd:PRK09859 38 VVTLSPGSVNVLSELPGRTVPYEVAEIRPQVGGIIIKRNFIEGDKVNQGDSLYQIDPAPLQAELNSAKGSLAKALSTASN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 114 AEQDYKRVKYLVEQKVKSNSELDQAKASYEVAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANFSA 193
Cdd:PRK09859 118 ARITFNRQASLLKTNYVSRQDYDTARTQLNEAEANVTVAKAAVEQATINLQYANVTSPITGVSGKSSVTVGALVTANQAD 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 194 PV-----LFQIAKDLSK-----MQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVKQVRllPTTVQNVVNYSVVVE 263
Cdd:PRK09859 198 SLvtvqrLDPIYVDLTQsvqdfLRMKEEVASGQIKQVQGSTPVQLNLENGKRYSQTGTLKFSD--PTVDETTGSVTLRAI 275
|
250 260 270
....*....|....*....|....*....|
gi 1167106414 264 VENPGNVLLPGMTATVDFITAKAEQVLKVP 293
Cdd:PRK09859 276 FPNPNGDLLPGMYVTALVDEGSRQNVLLVP 305
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
56-242 |
3.02e-13 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 70.44 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 56 ETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQ----------------------------KS 107
Cdd:PRK10476 47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLAladaqimttqrsvdaersnaasaneqveRA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 108 RAQYIQAEQDYKRVKYLVEQKVKSNSELDQAK-----ASYEVAKWNLKSQ-------------------ESNLSRAKLNL 163
Cdd:PRK10476 127 RANAKLATRTLERLEPLLAKGYVSAQQVDQARtaqrdAEVSLNQALLQAQaaaaavggvdalvaqraarEAALAIAELHL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 164 SYASIFSPVDGIVIARNVNAGQTVAANFSAPVLFqiakDLSKMQILANVDEGDVGQIKEGQQVkfTVQSYPDR--TFMGK 241
Cdd:PRK10476 207 EDTTVRAPFDGRVVGLKVSVGEFAAPMQPIFTLI----DTDHWYAIANFRETDLKNIRVGDCA--TVYSMIDRgrPFEGK 280
|
.
gi 1167106414 242 V 242
Cdd:PRK10476 281 V 281
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
168-251 |
5.82e-10 |
|
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: 56.22 E-value: 5.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 168 IFSPVDGIVIARNVNAGQTVAAnfsAPVLFQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFMGKVkqVRL 247
Cdd:pfam13437 2 IRAPVDGVVAELNVEEGQVVQA---GDPLATIV-PPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGKV--VRI 75
|
....
gi 1167106414 248 LPTT 251
Cdd:pfam13437 76 SPTV 79
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
83-285 |
5.55e-09 |
|
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: 57.71 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 83 QLVATLDRSLLENAVLDAESSLQKSRAQYIQAEQDYKRVKYLVEQKVKSNSEldQAKASYEVAKWNLKSQESNLSRAKLN 162
Cdd:TIGR01843 191 GLVSRLELLELERERAEAQGELGRLEAELEVLKRQIDELQLERQQIEQTFRE--EVLEELTEAQARLAELRERLNKARDR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 163 LSYASIFSPVDGIV--IARN-----VNAGQTVAanfsapvlfQIAKDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPD 235
Cdd:TIGR01843 269 LQRLIIRSPVDGTVqsLKVHtvggvVQPGETLM---------EIVPEDDPLEIEAKLSPKDIGFVHVGQPAEIKFSAFPY 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167106414 236 RTF---MGKVK---------QVRLLPTTVQNVVNYSVVVEVENPGNVLLPGMTATVDFITAK 285
Cdd:TIGR01843 340 RRYgilNGKVKsispdtftdERGGGPYYRVRISIDQNTLGIGPKGLELSPGMPVTADIKTGE 401
|
|
| heterocyst_DevB |
TIGR02971 |
ABC exporter membrane fusion protein, DevB family; Members of this protein family are found ... |
97-248 |
1.04e-08 |
|
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: 56.37 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 97 VLDAESsLQKSRAQYIQAEQDYKRVKYLVEQKVKSNSeLDQAKASYEV--AKWNLKSQESNLSRAKLNLSYASIFSPVDG 174
Cdd:TIGR02971 136 DLDSKA-LKLRTAEEELEEALASRSEQIDGARAALAS-LAEEVRETDVdlAQAEVKSALEAVQQAEALLELTYVKAPIDG 213
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1167106414 175 IVIARNVNAGQTVAanfSAPVLfQIAkDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDrTFMGKVKQVRLL 248
Cdd:TIGR02971 214 RVLKIHAREGEVIG---SEGIL-EMG-DTSQMYAVAEVYETDINRVRVGQRATITSTALSG-PLRGTVRRIGSL 281
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
58-242 |
3.70e-08 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 55.09 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 58 VDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKS-RA---------QYI-----------QAEQ 116
Cdd:PRK15136 62 VQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSvRQthqlminskQYQanielqktalaQAQS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 117 DYKRVKYLVEQKVKSNSEL-------DQAKASYEVAKW------------NLKSQ------ESNLSRAKLNLSYASIFSP 171
Cdd:PRK15136 142 DLNRRVPLGNANLIGREELqhardavASAQAQLDVAIQqynanqamilntPLEDQpavqqaATEVRNAWLALQRTKIVSP 221
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1167106414 172 VDGIVIARNVNAGQTVAANfsAPVLFQIAKDlsKMQILANVDEGDVGQIKEGQQVKFTVQSY-PDRTFMGKV 242
Cdd:PRK15136 222 MTGYVSRRSVQVGAQISPT--TPLMAVVPAT--NLWVDANFKETQLANMRIGQPATITSDIYgDDVVYTGKV 289
|
|
| PRK09578 |
PRK09578 |
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit; |
2-175 |
1.22e-07 |
|
MexX/AxyX family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 169982 [Multi-domain] Cd Length: 385 Bit Score: 53.26 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 2 RKVFVAIAILAVVAGCVWWFYGREKSQEFSYQLVAVEKGDIVSLVSATGTINPVETVDVGTQVSGRIDKLYADYNDHVTK 81
Cdd:PRK09578 8 RLLLAALVALFVLAGCGKGDSDAAAAAPREATVVTVRPTSVPMTVELPGRLDAYRQAEVRARVAGIVTARTYEEGQEVKQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 82 GQLVATLDRSLLENAVLDAESSLQKSRAQYIQAEQDYKRVKYLVEQKVKSNSELDQAKASYEVAKWNLKSQESNLSRAKL 161
Cdd:PRK09578 88 GAVLFRIDPAPLKAARDAAAGALAKAEAAHLAALDKRRRYDDLVRDRAVSERDYTEAVADERQAKAAVASAKAELARAQL 167
|
170
....*....|....
gi 1167106414 162 NLSYASIFSPVDGI 175
Cdd:PRK09578 168 QLDYATVTAPIDGR 181
|
|
| PRK09783 |
PRK09783 |
copper/silver efflux system membrane fusion protein CusB; Provisional |
167-290 |
2.11e-07 |
|
copper/silver efflux system membrane fusion protein CusB; Provisional
Pssm-ID: 236625 [Multi-domain] Cd Length: 409 Bit Score: 52.95 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 167 SIFSPVDGIVIARNVNAGQTVAANfsaPVLFQIaKDLSKMQILANVDEGDVGQIKEGQQVKFTVQSYPDRTFmgKVKQVR 246
Cdd:PRK09783 211 TLKAPIDGVITAFDLRAGMNIAKD---NVVAKI-QGMDPVWVTAAIPESIAWLVKDASQFTLTVPARPDKTF--TIRKWT 284
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1167106414 247 LLPTTVQNVVNYSVVVEVENPGNVLLPGMTATVDFITAKAEQVL 290
Cdd:PRK09783 285 LLPSVDAATRTLQLRLEVDNADEALKPGMNAWLQLNTASEPMLL 328
|
|
| PRK15030 |
PRK15030 |
multidrug efflux RND transporter periplasmic adaptor subunit AcrA; |
50-187 |
4.94e-06 |
|
multidrug efflux RND transporter periplasmic adaptor subunit AcrA;
Pssm-ID: 184990 [Multi-domain] Cd Length: 397 Bit Score: 48.56 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 50 GTINPVETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQKSRAQYIQAEQDYKRVKYLVEQKV 129
Cdd:PRK15030 58 GRTSAYRIAEVRPQVSGIILKRNFKEGSDIEAGVSLYQIDPATYQATYDSAKGDLAKAQAAANIAQLTVNRYQKLLGTQY 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1167106414 130 KSNSELDQAKASYEVAKWNLKSQESNLSRAKLNLSYASIFSPVDGIVIARNVNAGQTV 187
Cdd:PRK15030 138 ISKQEYDQALADAQQANAAVTAAKAAVETARINLAYTKVTSPISGRIGKSNVTEGALV 195
|
|
| PRK10559 |
PRK10559 |
p-hydroxybenzoic acid efflux pump subunit AaeA; |
4-245 |
2.93e-05 |
|
p-hydroxybenzoic acid efflux pump subunit AaeA;
Pssm-ID: 182548 [Multi-domain] Cd Length: 310 Bit Score: 45.50 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 4 VFVAIAILAVVAgcVWWFYGRE---KSQEFSYQLVAvekgdivslvsatgtINPvetvdvgtQVSGRIDKLYADYNDHVT 80
Cdd:PRK10559 16 VLVILAFIAIFR--AWVFYTESpwtRDARFSADVVA---------------IAP--------DVSGLITQVNVHDNQLVK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 81 KGQLVATLDRSLLENAVLDAESSLQksraqYIQAEQDYKRVKYLVEQK----VKSNSELDQAKASYEVAKWNLKSQESNL 156
Cdd:PRK10559 71 KGQVLFTIDQPRYQKALAEAEADVA-----YYQVLAQEKRREAGRRNRlgvqAMSREEIDQANNVLQTVLHQLAKAQATR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1167106414 157 SRAKLNLSYASIFSPVDGIVIARNVNAGQTVAANFSAPVLfqIAKDlsKMQILANVDEGDVGQIKEGQQVKFTvqsyP-- 234
Cdd:PRK10559 146 DLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVAL--VKQN--SFYVLAYMEETKLEGVRPGYRAEIT----Plg 217
|
250
....*....|..
gi 1167106414 235 -DRTFMGKVKQV 245
Cdd:PRK10559 218 sNKVLKGTVDSV 229
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
56-105 |
7.33e-04 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 37.42 E-value: 7.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1167106414 56 ETVDVGTQVSGRIDKLYADYNDHVTKGQLVATLDRSLLENAVLDAESSLQ 105
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| F-BAR_Rgd1 |
cd07652 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ... |
93-128 |
1.53e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153336 [Multi-domain] Cd Length: 234 Bit Score: 40.02 E-value: 1.53e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1167106414 93 LENAVLDAESSLQKSRAQYIQAEQDYKRVKYLVEQK 128
Cdd:cd07652 116 AEKKVQDAEAAAEKAKARYDSLADDLERVKTGDPGK 151
|
|
| |
