|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-248 |
1.42e-137 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 386.75 E-value: 1.42e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD----GADQQMGFVF 81
Cdd:COG1116 8 LELRGVSKRF-PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 82 QDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPF 161
Cdd:COG1116 87 QEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 162 GALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSARPGRVKEMVEIDLPRPRGEATRNDPKFTEYNK 241
Cdd:COG1116 167 GALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPRPRDRELRTSPEFAALRA 246
|
....*..
gi 1472203387 242 YLRGIIG 248
Cdd:COG1116 247 EILDLLR 253
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-222 |
8.06e-116 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 330.20 E-value: 8.06e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEdTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD----GADQQMGFVF 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGepvtGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 82 QDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPF 161
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 162 GALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSARPGRVKEMVEIDL 222
Cdd:cd03293 160 SALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-247 |
2.55e-86 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 257.10 E-value: 2.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNLlKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEyRDG-------ADQqmGF 79
Cdd:COG4525 5 TVRHVSVRYPGG-GQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT-LDGvpvtgpgADR--GV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 80 VFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 160 PFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSARPGRVKEMVEIDLPR--PRGEATR---NDP 234
Cdd:COG4525 161 PFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSRrfLAGEDARaikSDP 240
|
250
....*....|...
gi 1472203387 235 KFTEYNKYLRGII 247
Cdd:COG4525 241 AFIALREELLDII 253
|
|
| ABC_ATP_SaoA |
NF040729 |
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC ... |
5-247 |
2.82e-83 |
|
ABC transporter ATP-binding protein SaoA; SaoA is the ATP-binding subunit of an ABC transporter in which both the permease subunit SaoP, and the substrate-binding protein SaoB, are nearly always selenoproteins that were unrecognized as such until recently (2022). The SAO system is found in Clostridium difficile and various other anaerobic heterotrophs.
Pssm-ID: 468693 [Multi-domain] Cd Length: 248 Bit Score: 248.89 E-value: 2.82e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNLLKEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI----EYRDGADQQMGFV 80
Cdd:NF040729 1 KLKIQNISKTFINNKKENEV-LKDISFDVEEGEFVSLLGPSGCGKTTLLTIIAGFQNATSGEIlvngNEVTKPGPDRGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 81 FQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:NF040729 80 FQNYALFPWMTVKENIEYPMKQQKMPKQEREKRLNELLEMAQLTGKENLYPHQISGGMKQRTAVIRALACKPEVLLMDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 161 FGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSARPGRVKEMVEIDLPRPRgeaTRNDPKFTEYN 240
Cdd:NF040729 160 LGAVDFQMRQILQEELESIWLKDKTTVLMVTHDVDEAVYLSDRVIVMSRDKGKILEDLKIDLPRPR---NRESEKYLEYK 236
|
....*..
gi 1472203387 241 KYLRGII 247
Cdd:NF040729 237 DHLTNIL 243
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-214 |
7.33e-79 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 236.26 E-value: 7.33e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGADQQ--------M 77
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI-LIDGRDVTgvpperrnI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNE--GRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-214 |
2.13e-78 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 240.00 E-value: 2.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGADQ----- 75
Cdd:COG3842 1 MAMPALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL-DGRDVtglpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 ---QMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:COG3842 75 ekrNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 153 PLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMND--GRI 214
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-236 |
4.20e-74 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 225.04 E-value: 4.20e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY------RDGADQQMgfVFQDSVLLPWKNVRQNAEFP 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILegkqitEPGPDRMV--VFQNYSLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 100 L--VIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELL 177
Cdd:TIGR01184 79 VdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 178 KIWQKTKKTVIFVTHSIEEATFLSDRVLVMSARPG-RVKEMVEIDLPRPRG-EATRNDPKF 236
Cdd:TIGR01184 159 QIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAaNIGQILEVPFPRPRDrLEVVEDPSY 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
6-216 |
7.22e-73 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 221.46 E-value: 7.22e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:COG1136 5 LELRNLTKSY-GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLI-DGQDisslserelar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ---QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYD 151
Cdd:COG1136 83 lrrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 152 APLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFlSDRVLVMsaRPGRVKE 216
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRL--RDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-208 |
2.14e-72 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 220.05 E-value: 2.14e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:cd03255 1 IELKNLSKTY-GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRV-DGTDisklsekelaa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ---QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYD 151
Cdd:cd03255 79 frrRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 152 APLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEAtFLSDRVLVMS 208
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELR 214
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-214 |
3.63e-72 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 222.66 E-value: 3.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQ 76
Cdd:COG1125 3 EFENVTKRYPD----GTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILI-DGEDirdldpvelrRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGL--SEFKTALPRELSGGMKQRVSIVRALSYDAPL 154
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 155 LLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRI 215
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-214 |
7.37e-69 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 215.71 E-value: 7.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSeySVELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDG-------- 72
Cdd:COG3839 1 MA--SLELENVSKSYG-----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI-GGrdvtdlpp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 73 ADQQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:COG3839 73 KDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 153 PLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND--GRI 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-243 |
2.61e-68 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 211.10 E-value: 2.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR----DGADQQMGFVFQDSVLLPWKNVRQNAEFPL 100
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvEGPGAERGVVFQNEGLLPWRNVQDNVAFGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 101 VIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIW 180
Cdd:PRK11248 96 QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLW 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 181 QKTKKTVIFVTHSIEEATFLSDRVLVMSARPGRVKEMVEIDLPR--PRGEATR---NDPKFTEYNKYL 243
Cdd:PRK11248 176 QETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARrfVAGESSRsikSDPQFIAMREYV 243
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-214 |
1.47e-67 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 212.31 E-value: 1.47e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------Q 75
Cdd:COG1118 2 SIEVRNISKRFGS-----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL-NGRDlftnlppreR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLL 155
Cdd:COG1118 76 RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 156 LMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG1118 156 LLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ--GRI 212
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
6-214 |
3.33e-67 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 212.66 E-value: 3.33e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSN-------LLKE------------DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGT 66
Cdd:COG4175 4 IEVRNLYKIFGKrperalkLLDQgkskdeilektgQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 67 IEYrDGAD--------------QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPR 132
Cdd:COG4175 84 VLI-DGEDitklskkelrelrrKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 133 ELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPG 212
Cdd:COG4175 163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLGDRIAIM--KDG 240
|
..
gi 1472203387 213 RV 214
Cdd:COG4175 241 RI 242
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-207 |
7.27e-65 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 201.76 E-value: 7.27e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------Q 75
Cdd:cd03295 1 IEFENVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI-FIDGEDireqdpvelrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGL--SEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:cd03295 76 KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 154 LLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-217 |
8.50e-65 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 201.31 E-value: 8.50e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD--------QQM 77
Cdd:cd03300 1 IELENVSKFYG-----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL-DGKDitnlpphkRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEM 217
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNK--GKIQQI 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-231 |
2.10e-64 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 208.60 E-value: 2.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF-DGKDltklsrrslre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQD--SVLLPWKNVRQNAEFPLVIQKKQT-EENEKKLDELLELAGLS-EFKTALPRELSGGMKQRVSIVRAL 148
Cdd:COG1123 340 lrRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSrAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 149 SYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMVEID--LPRPR 226
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYD--GRIVEDGPTEevFANPQ 497
|
....*
gi 1472203387 227 GEATR 231
Cdd:COG1123 498 HPYTR 502
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
23-224 |
2.18e-63 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 199.02 E-value: 2.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 23 TVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD--------------QQMGFVFQDSVLLP 88
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLI-DGQDiaamsrkelrelrrKKISMVFQSFALLP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 WKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALT 168
Cdd:cd03294 116 HRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 169 RDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVkemVEIDLPR 224
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM--KDGRL---VQVGTPE 246
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-207 |
1.85e-61 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 196.80 E-value: 1.85e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYsVELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD------ 74
Cdd:TIGR03265 1 SSPY-LSIDNIRKRF-----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTI-YQGGRDitrlpp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:TIGR03265 74 qkRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 153 PLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:TIGR03265 154 GLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVM 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-216 |
5.10e-61 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 191.64 E-value: 5.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEdTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:cd03258 2 IELKNVSKVFGDTGGK-VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-DGTDltllsgkelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:cd03258 80 arRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 153 PLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEK--GEVVE 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
6-214 |
5.14e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 191.82 E-value: 5.14e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------QQ 76
Cdd:COG1131 1 IEVRGLTKRYG-----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV-LGEDvardpaevrRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLL 156
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 157 MDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDK--GRI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-216 |
1.06e-59 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 188.70 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 4 YSVELKGLNKVYSNLlkedtVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY-------RDGADQQ 76
Cdd:cd03296 1 MSIEVRNVSKRFGDF-----VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdVPVQERN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENE----KKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:cd03296 76 VGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEaeirAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 153 PLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNK--GRIEQ 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-232 |
2.39e-59 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 190.67 E-value: 2.39e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLlKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:COG1135 2 IELENLSKTFPTK-GGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLV-DGVDltalserelra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:COG1135 80 arRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 153 PLLLMDEPFGALD-ALTRDHLneELLK-IWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEM---VEIdLPRPRG 227
Cdd:COG1135 160 KVLLCDEATSALDpETTRSIL--DLLKdINRELGLTIVLITHEMDVVRRICDRVAVLEN--GRIVEQgpvLDV-FANPQS 234
|
....*
gi 1472203387 228 EATRN 232
Cdd:COG1135 235 ELTRR 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-216 |
2.67e-59 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 186.94 E-value: 2.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLlKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD----GADQQM---- 77
Cdd:cd03257 2 LEVKNLSVSFPTG-GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 ----GFVFQD--SVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGL---SEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:cd03257 81 rkeiQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 149 SYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYA--GKIVE 226
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-224 |
2.71e-59 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 187.49 E-value: 2.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD------ 74
Cdd:COG1127 1 MSEPMIEVRNLTKSF-----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV-DGQDitglse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 -------QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKL-DELLELAGLSEFKTALPRELSGGMKQRVSIVR 146
Cdd:COG1127 75 kelyelrRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELvLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 147 ALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSAR----PGRVKEMVEIDL 222
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGkiiaEGTPEELLASDD 234
|
..
gi 1472203387 223 PR 224
Cdd:COG1127 235 PW 236
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-209 |
3.58e-59 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 185.08 E-value: 3.58e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILI-DGEDltdledelppl 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 -QQMGFVFQDSVLLPWKNVRQNAEFPLviqkkqteenekkldellelaglsefktalprelSGGMKQRVSIVRALSYDAP 153
Cdd:cd03229 75 rRRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 154 LLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSA 209
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-207 |
2.88e-58 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 184.00 E-value: 2.88e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDG--------ADQQM 77
Cdd:cd03301 1 VELENVTKRF-----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRI-YIGGrdvtdlppKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-226 |
2.37e-56 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 180.01 E-value: 2.37e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:cd03261 1 IELRGLTKSF-----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI-DGEDisglseaelyr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQDSVLLPWKNVRQNAEFPLviqKKQTEENEKKLDEL----LELAGLSEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:cd03261 75 lrRRMGMLFQSGALFDSLTVFENVAFPL---REHTRLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 149 SYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSAR----PGRVKEMVEIDLPR 224
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGkivaEGTPEELRASDDPL 231
|
..
gi 1472203387 225 PR 226
Cdd:cd03261 232 VR 233
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-231 |
5.37e-55 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 176.92 E-value: 5.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------Q 75
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPV-LKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTF-DGRPvtrrrrkafrR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQD--SVLLPWKNVRQNAEFPLVIQKKQteENEKKLDELLELAGL-SEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:COG1124 80 RVQMVFQDpyASLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 153 PLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMVEIDLPR--PRGEAT 230
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN--GRIVEELTVADLLagPKHPYT 235
|
.
gi 1472203387 231 R 231
Cdd:COG1124 236 R 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-231 |
9.22e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 175.95 E-value: 9.22e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:COG1126 2 IEIENLHKSFG-----DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITV-DGEDltdskkdinkl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 -QQMGFVFQDSVLLPWKNVRQN-AEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:COG1126 76 rRKVGMVFQQFNLFPHLTVLENvTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 153 PLLLMDEPFGALD-ALTRDHLN--EELlkiwQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVkemVEIDLPR----- 224
Cdd:COG1126 156 KVMLFDEPTSALDpELVGEVLDvmRDL----AKEGMTMVVVTHEMGFAREVADRVVFMDG--GRI---VEEGPPEeffen 226
|
....*..
gi 1472203387 225 PRGEATR 231
Cdd:COG1126 227 PQHERTR 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
8-226 |
1.45e-54 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 176.02 E-value: 1.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 8 LKGLNKVYSnllkEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI--------EYRDgaDQQMgf 79
Cdd:PRK11247 15 LNAVSKRYG----ERTV-LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagtaplaEARE--DTRL-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 80 VFQDSVLLPWKNVRQNAEFPLVIQKKQTEEnekkldELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGLKGQWRDAAL------QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 160 PFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMVEIDLPRPR 226
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE--GKIGLDLTVDLPRPR 224
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-214 |
3.47e-54 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 174.06 E-value: 3.47e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------Q 75
Cdd:COG1122 1 IELENLSFSYPG----GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV-DGKDitkknlrelrR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDsvllPW-----KNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSY 150
Cdd:COG1122 76 KVGLVFQN----PDdqlfaPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 151 DAPLLLMDEPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRREL-LELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDD--GRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-208 |
4.94e-54 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 173.04 E-value: 4.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQ 76
Cdd:cd03225 1 ELKNLSFSYPD---GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV-DGKDltklslkelrRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDS---VLLPwkNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:cd03225 77 VGLVFQNPddqFFGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 154 LLLMDEPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:cd03225 155 ILLLDEPTAGLDPAGRREL-LELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-195 |
3.72e-53 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 171.39 E-value: 3.72e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:COG2884 2 IRFENVSKRYPG----GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV-NGQDlsrlkrreipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:COG2884 77 lrRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1472203387 153 PLLLMDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIE 195
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE 198
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
6-207 |
2.36e-52 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 168.86 E-value: 2.36e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLlkedtVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:cd03262 1 IEIKNLHKSFGDF-----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIII-DGLKltddkkninel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 -QQMGFVFQDSVLLPWKNVRQN-AEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:cd03262 75 rQKVGMVFQQFNLFPHLTVLENiTLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 153 PLLLMDEPFGALDAltrdHLNEELLKIWQ---KTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:cd03262 155 KVMLFDEPTSALDP----ELVGEVLDVMKdlaEEGMTMVVVTHEMGFAREVADRVIFM 208
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-224 |
1.14e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 172.05 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD--------QQM 77
Cdd:PRK09452 15 VELRGISKSF-----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI-MLDGQDithvpaenRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKemvEIDLPR 224
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM--RDGRIE---QDGTPR 230
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
6-228 |
1.26e-51 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 171.03 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllKEdtVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD--------QQM 77
Cdd:NF040840 2 IRIENLSKDW----KE--FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKI-YLDGKDitnlppekRGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:NF040840 75 AYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM-SARPGRVKEMVEIdLPRPRGE 228
Cdd:NF040840 155 DEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMlNGRLSQVGDVREV-FRRPKNE 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
26-209 |
5.18e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.37 E-value: 5.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI-------------EYRdgadQQMGFVFQDSVLLPwKNV 92
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIyldgkplsampppEWR----RQVAYVPQEPALWG-GTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 93 RQNAEFPLVIQKKQTeeNEKKLDELLELAGLSE-FKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDH 171
Cdd:COG4619 91 RDNLPFPFQLRERKF--DRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1472203387 172 LNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSA 209
Cdd:COG4619 169 VEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
5-208 |
1.93e-50 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 168.34 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD-------GADQQM 77
Cdd:PRK10851 2 SIEIANIKKSFGR-----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVI----QKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 154 LLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-221 |
2.00e-50 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 165.03 E-value: 2.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------QQM 77
Cdd:COG4555 3 EVENLSKKYG-----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILI-DGEDvrkeprearRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 158 DEPFGALDALTRDHLNEELLKiWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMVEID 221
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHK--GKVVAQGSLD 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
6-217 |
3.08e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 167.29 E-value: 3.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEdTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------- 74
Cdd:PRK11153 2 IELKNISKVFPQGGRT-IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV-LVDGQDltalsekelrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDA 152
Cdd:PRK11153 80 arRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 153 PLLLMDEPFGALD-ALTRDHLneELLK-IWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEM 217
Cdd:PRK11153 160 KVLLCDEATSALDpATTRSIL--ELLKdINRELGLTIVLITHEMDVVKRICDRVAVIDA--GRLVEQ 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-217 |
6.75e-50 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 163.28 E-value: 6.75e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLlkedtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD--------QQM 77
Cdd:cd03299 1 LKVENLSKDWKEF------KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-LLNGKDitnlppekRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKEM 217
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM--LNGKLIQV 211
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-214 |
1.22e-49 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 162.08 E-value: 1.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIR---PGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGA-------------DQQMGFVFQDSVLLPW 89
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqQRKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLviqkKQTEENEKKL--DELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAL 167
Cdd:cd03297 90 LNVRENLAFGL----KRKRNREDRIsvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1472203387 168 TRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVM--EDGRL 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
6-214 |
1.52e-48 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 157.56 E-value: 1.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------QQ 76
Cdd:cd03230 1 IEVRNLSKRYG-----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV-LGKDikkepeevkRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPWKNVRQNAEfplviqkkqteenekkldellelaglsefktalpreLSGGMKQRVSIVRALSYDAPLLL 156
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 157 MDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNN--GRI 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
6-214 |
1.76e-46 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 154.10 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIE--------YRDGA---- 73
Cdd:cd03292 1 IEFINVTKTYPN----GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdLRGRAipyl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 74 DQQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 154 LLLMDEPFGALDAltrDHLNE--ELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:cd03292 157 ILIADEPTGNLDP---DTTWEimNLLKKINKAGTTVVVATHAKELVDTTRHRVIAL--ERGKL 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-207 |
2.36e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.48 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD----GADQQ 76
Cdd:COG1121 2 MMMPAIELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLlpwknvrqNAEFPL----VIQ----------KKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRV 142
Cdd:COG1121 77 IGYVPQRAEV--------DWDFPItvrdVVLmgrygrrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 143 SIVRALSYDAPLLLMDEPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATEEAL-YELLRELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
7-211 |
2.43e-46 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 153.46 E-value: 2.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGADQQM-----GFVF 81
Cdd:cd03235 1 EVEDLTVSYGG-----HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV-FGKPLEKerkriGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 82 QDSVLlpwknvrqNAEFPL--------------VIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRA 147
Cdd:cd03235 75 QRRSI--------DRDFPIsvrdvvlmglyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 148 LSYDAPLLLMDEPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSARP 211
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDI-YELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
25-209 |
1.42e-45 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 151.63 E-value: 1.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD-------------QQMGFVFQDSVLLPWKN 91
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRI-AGEDvnrlrgrqlpllrRRIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDaltrDH 171
Cdd:TIGR02673 96 VYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLD----PD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1472203387 172 LNEELLKIWQKTKK---TVIFVTHSIEEATFLSDRVLVMSA 209
Cdd:TIGR02673 172 LSERILDLLKRLNKrgtTVIVATHDLSLVDRVAHRVIILDD 212
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-215 |
5.08e-45 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 150.35 E-value: 5.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLlkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI--------EYRDGADQQM 77
Cdd:cd03263 1 LQIRNLTKTYKKG---TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAyingysirTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIwqKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVK 215
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSD--GKLR 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
5-217 |
5.30e-45 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 160.00 E-value: 5.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------- 74
Cdd:COG2274 473 DIELENVSFRYPG---DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILI-DGIDlrqidpaslr 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDSVLLPwKNVRQNaefpLVIQKKQTeeNEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVS 143
Cdd:COG2274 549 RQIGVVLQDVFLFS-GTIREN----ITLGDPDA--TDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 144 IVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQktKKTVIFVTH---SIEEAtflsDRVLVMSArpGRVKEM 217
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHrlsTIRLA----DRIIVLDK--GRIVED 690
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-216 |
5.88e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 157.37 E-value: 5.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-IIGNLDKP--TSGTIEYrDGAD-------- 74
Cdd:COG1123 5 LEVRDLSVRYPG---GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGgrISGEVLL-DGRDllelseal 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQD--SVLLPWKNVRQNAEfPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSY 150
Cdd:COG1123 81 rgRRIGMVFQDpmTQLNPVTVGDQIAE-ALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 151 DAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKE 216
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM--DDGRIVE 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-214 |
2.02e-44 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 148.41 E-value: 2.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 28 DINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI-------EYRDGADQQMGFVFQDSVLLPWKNVRQNAEFPL 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVlingvdvTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 101 VIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIW 180
Cdd:cd03298 96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|....
gi 1472203387 181 QKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDN--GRI 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-207 |
3.28e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 146.24 E-value: 3.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDgadqqmgfvfQDSVL 86
Cdd:cd00267 1 EIENLSFRY-----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG----------KDIAK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 87 LPWKNVRQNAEFplVIQkkqteenekkldellelaglsefktalpreLSGGMKQRVSIVRALSYDAPLLLMDEPFGALDA 166
Cdd:cd00267 66 LPLEELRRRIGY--VPQ------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDP 113
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1472203387 167 LTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:cd00267 114 ASRERL-LELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-214 |
6.55e-44 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 151.72 E-value: 6.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDG--------ADQQ 76
Cdd:PRK11000 3 SVTLRNVTKAYG-----DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL-FIGEkrmndvppAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLD---ELLELAGLSEFKtalPRELSGGMKQRVSIVRALSYDAP 153
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNqvaEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 154 LLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDA--GRV 212
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
6-216 |
7.88e-44 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 147.33 E-value: 7.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNL-----DKPTSGTIEYrDGAD------ 74
Cdd:cd03260 1 IELRDLNVYY-----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLL-DGKDiydldv 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ------QQMGFVFQDSVLLPwKNVRQNAEFPLVIQKKQTEENEKKLDE-LLELAGLS-EFKTAL-PRELSGGMKQRVSIV 145
Cdd:cd03260 75 dvlelrRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWdEVKDRLhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 146 RALSYDAPLLLMDEPFGALDALTRDHLnEELLKiWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKI-EELIA-ELKKEYTIVIVTHNMQQAARVADRTAFLLN--GRLVE 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-214 |
1.61e-43 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 150.38 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDG--------ADQQ 76
Cdd:PRK11650 3 GLKLQAVRKSYDG----KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGrvvnelepADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDE---LLELAGLSEFKtalPRELSGGMKQRVSIVRALSYDAP 153
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarILELEPLLDRK---PRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 154 LLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:PRK11650 155 VFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNG--GVA 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-207 |
2.20e-43 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 146.34 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 9 KGLNKVYSNLlKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD-------------- 74
Cdd:TIGR02211 5 ENLGKRYQEG-KLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLF-NGQSlsklssneraklrn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPL 154
Cdd:TIGR02211 83 KKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 155 LLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLsDRVLVM 207
Cdd:TIGR02211 163 VLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEM 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-209 |
4.20e-43 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 146.29 E-value: 4.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:TIGR02315 2 LEVENLSKVYPN----GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILL-EGTDitklrgkklrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQ--------TEENEKKLDELLELAGLSEFktALPR--ELSGGMKQRV 142
Cdd:TIGR02315 77 lrRRIGMIFQHYNLIERLTVLENVLHGRLGYKPTwrsllgrfSEEDKERALSALERVGLADK--AYQRadQLSGGQQQRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 143 SIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSA 209
Cdd:TIGR02315 155 AIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKA 221
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-216 |
5.88e-43 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 152.99 E-value: 5.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------- 74
Cdd:COG4988 336 SIELEDVSFSYP----GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI-NGVDlsdldpaswr 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDSVLLPWkNVRQNaefplvIQKKQTEENEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVS 143
Cdd:COG4988 411 RQIAWVPQNPYLFAG-TIREN------LRLGRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 144 IVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQktKKTVIFVTHSIEEATFlSDRVLVMSArpGRVKE 216
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDD--GRIVE 551
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-205 |
6.92e-43 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 144.30 E-value: 6.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 8 LKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADQQ----------- 76
Cdd:TIGR03608 1 LKNISKKFG-----DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlnskkaskfrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 --MGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPL 154
Cdd:TIGR03608 76 ekLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 155 LLMDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATfLSDRVL 205
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVAK-QADRVI 204
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-224 |
8.32e-43 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 147.64 E-value: 8.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 41 IIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD--------QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEK 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIML-DGEDvtnvpphlRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 113 KLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTH 192
Cdd:TIGR01187 80 RVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTH 159
|
170 180 190
....*....|....*....|....*....|..
gi 1472203387 193 SIEEATFLSDRVLVMsaRPGRVkemVEIDLPR 224
Cdd:TIGR01187 160 DQEEAMTMSDRIAIM--RKGKI---AQIGTPE 186
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-214 |
1.16e-42 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 145.02 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD------------GAD 74
Cdd:cd03256 2 EVENLSKTYPN----GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQ--------TEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVR 146
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENVLSGRLGRRSTwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 147 ALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKD--GRI 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
6-214 |
2.17e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.43 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:COG3638 3 LELRNLSKRYPG----GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILV-DGQDvtalrgralrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQD-------SVL-------LP----WKNVRQNaeFPlviqkkqTEENEKKLdELLELAGLSEFKTALPREL 134
Cdd:COG3638 78 lrRRIGMIFQQfnlvprlSVLtnvlagrLGrtstWRSLLGL--FP-------PEDRERAL-EALERVGLADKAYQRADQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 135 SGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD--GRV 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-214 |
2.33e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 143.74 E-value: 2.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNLLKEdtvalkdINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDG-------ADQQMGF 79
Cdd:COG3840 3 RLDDLTYRYGDFPLR-------FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppAERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 80 VFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 160 PFGALD-ALTRDHLNeeLLK-IWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG3840 156 PFSALDpALRQEMLD--LVDeLCRERGLTVLMVTHDPEDAARIADRVLLVAD--GRI 208
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-220 |
2.79e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 145.97 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnlLKEDTV-ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKP---TSGTIEYrDGAD------- 74
Cdd:COG0444 2 LEVRNLKVYFP--TRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILF-DGEDllklsek 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 -------QQMGFVFQD--SVLLPWKNVRQNAEFPLVIQKKQT-EENEKKLDELLELAGLS---EFKTALPRELSGGMKQR 141
Cdd:COG0444 79 elrkirgREIQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSkAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 142 VSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVkemVEI 220
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYA--GRI---VEE 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-161 |
4.24e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 140.48 E-value: 4.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGAD---------QQMGFVFQDSVLLPWKNVRQNA 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderkslrKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 97 EFPLVIQKKQTEENEKKLDELLELAGLSEFK----TALPRELSGGMKQRVSIVRALSYDAPLLLMDEPF 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-216 |
4.86e-42 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 142.96 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSNLLKEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD------ 74
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTI-LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL-AGQDlfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --------QQMGFVFQDSVLLPWKNVRQNAEFPLVIqkKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVR 146
Cdd:COG4181 82 dararlraRHVGFVFQSFQLLPTLTALENVMLPLEL--AGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 147 ALSYDAPLLLMDEPFGALDALTRDH-------LNEEllkiwQKTkkTVIFVTHSIEEATfLSDRVLVMSArpGRVKE 216
Cdd:COG4181 160 AFATEPAILFADEPTGNLDAATGEQiidllfeLNRE-----RGT--TLVLVTHDPALAA-RCDRVLRLRA--GRLVE 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-214 |
5.52e-42 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 143.65 E-value: 5.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------Q 75
Cdd:COG1120 2 LEAENLSVGYG-----GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLL-DGRDlaslsrrelaR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQ-----------DSVLL---PWKNVRQNAefplviqkkqTEENEKKLDELLELAGLSEFKTALPRELSGGMKQR 141
Cdd:COG1120 76 RIAYVPQeppapfgltvrELVALgryPHLGLFGRP----------SAEDREAVEEALERTGLEHLADRPVDELSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 142 VSIVRALSYDAPLLLMDEPFGALDaltrdhLN--EELL----KIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLD------LAhqLEVLellrRLARERGRTVVMVLHDLNLAARYADRLVLL--KDGRI 216
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-207 |
9.16e-42 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 140.21 E-value: 9.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------Q 75
Cdd:cd03228 1 IEFKNVSFSYPG---RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-DGVDlrdldleslrK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDSVLLPwKNVRQNaefplvIqkkqteenekkldellelaglsefktalpreLSGGMKQRVSIVRALSYDAPLL 155
Cdd:cd03228 77 NIAYVPQDPFLFS-GTIREN------I-------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 156 LMDEPFGALDALTRDHLNEELLKIwqKTKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIR-DADRIIVL 167
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-214 |
3.71e-41 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 142.21 E-value: 3.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------- 74
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTI-DGRDitakkkkklkd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQ--------DSVLlpwKNVrqnaEFPLVIQKKQTEENEKKLDELLELAGLSE-FKTALPRELSGGMKQRVS 143
Cdd:TIGR04521 80 lrKKVGLVFQfpehqlfeETVY---KDI----AFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 144 IVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHK--GKI 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-208 |
4.11e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 144.59 E-value: 4.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD--------QQM 77
Cdd:PRK11607 20 LEIRNLTKSF-----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLDGVDlshvppyqRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-215 |
6.49e-41 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 143.32 E-value: 6.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 28 DINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR-----DGADQQM--------GFVFQDSVLLPWKNVRQ 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSARGIFlpphrrriGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 95 NAEFPLviqkKQTEENEKKLD-----ELLELAGLSEFKtalPRELSGGMKQRVSIVRAL-SydAP-LLLMDEPFGALDAL 167
Cdd:COG4148 97 NLLYGR----KRAPRAERRISfdevvELLGIGHLLDRR---PATLSGGERQRVAIGRALlS--SPrLLLMDEPLAALDLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1472203387 168 TRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVK 215
Cdd:COG4148 168 RKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQ--GRVV 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-216 |
7.68e-41 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 140.23 E-value: 7.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGT-----IEYRDGA------D 74
Cdd:PRK09493 2 IEFKNVSKHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdgLKVNDPKvderliR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDSVLLPWKNVRQNAEF-PLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 154 LLLMDEPFGALDAltrdHLNEELLKIWQKTKK---TVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:PRK09493 157 LMLFDEPTSALDP----ELRHEVLKVMQDLAEegmTMVIVTHEIGFAEKVASRLIFIDK--GRIAE 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-207 |
1.19e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 142.55 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD------QQ--M 77
Cdd:PRK11432 7 VVLKNITKRFGS-----NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI-FIDGEDvthrsiQQrdI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-207 |
1.99e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 139.87 E-value: 1.99e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------- 74
Cdd:TIGR04520 1 IEVENVSFSYPE---SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKV-TVDGLDtldeenlweir 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDsvllPwKN------VRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:TIGR04520 77 KKVGMVFQN----P-DNqfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 149 SYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVM 209
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
6-207 |
1.11e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 137.57 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllKEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD-------------- 71
Cdd:PRK11264 4 IEVKNLVKKF----HGQTV-LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDitidtarslsqqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 72 ---GADQQMGFVFQDSVLLPWKNVRQNA-EFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRA 147
Cdd:PRK11264 79 lirQLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 148 LSYDAPLLLMDEPFGALDAltrDHLNEELLKIWQ--KTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaQEKRTMVIVTHEMSFARDVADRAIFM 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
16-210 |
1.14e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.07 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 16 SNLLKE--DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY--------RDGADQQMGFVFQDSV 85
Cdd:COG4133 6 ENLSCRrgERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWngepirdaREDYRRRLAYLGHADG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 86 LLPWKNVRQNAEFplVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:COG4133 86 LKPELTVRENLRF--WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1472203387 166 ALTRDHLnEELLKIWQKTKKTVIFVTHsiEEATFLSDRVLVMSAR 210
Cdd:COG4133 164 AAGVALL-AELIAAHLARGGAVLLTTH--QPLELAAARVLDLGDF 205
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-192 |
9.99e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 142.17 E-value: 9.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNLlKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGT--IEYRDGAD---------- 74
Cdd:PRK10535 6 ELKDIRRSYPSG-EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTyrVAGQDVATldadalaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 -QQMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:PRK10535 85 rEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1472203387 154 LLLMDEPFGALDAltrdHLNEELLKIWQKTKK---TVIFVTH 192
Cdd:PRK10535 165 VILADEPTGALDS----HSGEEVMAILHQLRDrghTVIIVTH 202
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-208 |
1.49e-38 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 133.65 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY------RDGAD--QQM 77
Cdd:cd03265 1 IEVENLVKKYG-----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvREPREvrRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-216 |
2.61e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 140.30 E-value: 2.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLPwK 90
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI-DGVDirdltleslrRQIGVVPQDTFLFS-G 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 91 NVRQNaefplvI---QKKQTEEnekKLDELLELAGLSEFKTALP-----------RELSGGMKQRVSIVRALSYDAPLLL 156
Cdd:COG1132 429 TIREN------IrygRPDATDE---EVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 157 MDEPFGALDALT----RDHLnEELLKiwqktKKTVIFVTH---SIEEAtflsDRVLVMSArpGRVKE 216
Cdd:COG1132 500 LDEATSALDTETealiQEAL-ERLMK-----GRTTIVIAHrlsTIRNA----DRILVLDD--GRIVE 554
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
5-244 |
3.38e-38 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 133.60 E-value: 3.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIE-------YRDGAD--- 74
Cdd:COG4161 2 SIQLKNINCFYGS-----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqfdFSQKPSeka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 -----QQMGFVFQDSVLLPWKNVRQN-AEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:COG4161 77 irllrQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 149 SYDAPLLLMDEPFGALD-ALTrdhlNE--ELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMveidlprp 225
Cdd:COG4161 157 MMEPQVLLFDEPTAALDpEIT----AQvvEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEK--GRIIEQ-------- 222
|
250 260
....*....|....*....|
gi 1472203387 226 rGEATR-NDPKFTEYNKYLR 244
Cdd:COG4161 223 -GDASHfTQPQTEAFAHYLS 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
5-243 |
5.57e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.13 E-value: 5.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGA----------- 73
Cdd:PRK11124 2 SIQLNGINCFYGA-----HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfsktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 74 ----DQQMGFVFQDSVLLPWKNVRQN-AEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:PRK11124 77 irelRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 149 SYDAPLLLMDEPFGALDAltrdHLNEELLKI---WQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMveidlprp 225
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDP----EITAQIVSIireLAETGITQVIVTHEVEVARKTASRVVYMEN--GHIVEQ-------- 222
|
250
....*....|....*....
gi 1472203387 226 rGEATR-NDPKFTEYNKYL 243
Cdd:PRK11124 223 -GDASCfTQPQTEAFKNYL 240
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
22-214 |
6.69e-37 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 127.94 E-value: 6.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQdsvllpwkn 91
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL-DGKDlaslspkelaRKIAYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 vrqnaefplviqkkqteenekkldeLLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDH 171
Cdd:cd03214 81 -------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1472203387 172 LNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD--GRI 176
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
25-216 |
8.72e-37 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 136.05 E-value: 8.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLDkPTSGTIEYrDGAD----------QQMGFVFQDSVLLpwkN-- 91
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLD-PQSGSITL-GGVDlrdldeddlrRRIAVVPQRPHLF---Dtt 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNaefpLVIQKKQTEENEkkLDELLELAGLSEFKTALP-----------RELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:COG4987 425 LREN----LRLARPDATDEE--LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDEP 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 161 FGALDALTRDHLNEELLKIWQktKKTVIFVTHSIEEATfLSDRVLVMSArpGRVKE 216
Cdd:COG4987 499 TEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLE-RMDRILVLED--GRIVE 549
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-215 |
2.29e-36 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 131.39 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 28 DINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI--------EYRDGAD-----QQMGFVFQDSVLLPWKNVRQ 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfDSRKGIFlppekRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 95 NAEFPLviQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNE 174
Cdd:TIGR02142 95 NLRYGM--KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1472203387 175 ELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVK 215
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVL--EDGRVA 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-246 |
2.29e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 132.46 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 23 TVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI-------------EYRDGADQQMGFVFQDSVLLPW 89
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVlidgvdiakisdaELREVRRKKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTR 169
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 170 DHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpgrvKEMVEIDLPrprgEATRNDPKFTEYNKYLRGI 246
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQN-----GEVVQVGTP----DEILNNPANDYVRTFFRGV 268
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-214 |
4.25e-36 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 127.55 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------QQMGFV--FQDSVLLPWKNV 92
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLF-DGEDitglppheiARLGIGrtFQIPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 93 RQNAEFPLVIQKKQT----------EENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:cd03219 93 LENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 163 ALDALTRDHLNEELLKIWQKtKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03219 173 GLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQ--GRV 221
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-220 |
6.67e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 129.85 E-value: 6.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNK---VYSNLL--KEDTV-ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD 74
Cdd:COG4608 3 MAEPLLEVRDLKKhfpVRGGLFgrTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF-DGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 -------------QQMGFVFQD--SVLLPWKNVRQNAEFPLVIQKKQT-EENEKKLDELLELAGLS-EFKTALPRELSGG 137
Cdd:COG4608 82 itglsgrelrplrRRMQMVFQDpyASLNPRMTVGDIIAEPLRIHGLASkAERRERVAELLELVGLRpEHADRYPHEFSGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 138 MKQRVSIVRALSYDAPLLLMDEPFGALDA--------LTRDhLNEEL-LkiwqktkkTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:COG4608 162 QRQRIGIARALALNPKLIVCDEPVSALDVsiqaqvlnLLED-LQDELgL--------TYLFISHDLSVVRHISDRVAVMY 232
|
250
....*....|..
gi 1472203387 209 ArpGRvkeMVEI 220
Cdd:COG4608 233 L--GK---IVEI 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-216 |
6.97e-36 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 126.75 E-value: 6.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLPwK 90
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-EGEDistlkpeiyrQQVSYCAQTPTLFG-D 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 91 NVRQNAEFPLVIQKKQTEenEKKLDELLELAGLSEfkTALPR---ELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAL 167
Cdd:PRK10247 96 TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALPD--TILTKniaELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1472203387 168 TRDHLNEELLKIWQKTKKTVIFVTHSIEEATFlSDRVLVMSARPGRVKE 216
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQPHAGEMQE 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
7-214 |
1.33e-35 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 127.08 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNLlkedtVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------QQM 77
Cdd:COG0411 6 EVRGLTKRFGGL-----VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF-DGRDitglpphriARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFV--FQDSVLLPWKNVRQN---------------AEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQ 140
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENvlvaaharlgrgllaALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 141 RVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF--GRV 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-216 |
2.64e-35 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 125.70 E-value: 2.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 23 TVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR-------------DGADQQMGFVFQDSVLLPW 89
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaELRNQKLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTR 169
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1472203387 170 DHLNEELLKIWQKTKKTVIFVTHSIEEATFLSdRVLVMsaRPGRVKE 216
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEM--RDGRLTA 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
6-214 |
2.81e-35 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 125.97 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSG-TI----EYRDGAD-----Q 75
Cdd:COG1119 4 LELRNVTVRR-----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVrlfgERRGGEDvwelrK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFV---------------------FQDSVLLpWKNVrqnaefplviqkkqTEENEKKLDELLELAGLSEFKTALPREL 134
Cdd:COG1119 79 RIGLVspalqlrfprdetvldvvlsgFFDSIGL-YREP--------------TDEQRERARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 135 SGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEE--ATFlsDRVLVMsaRPG 212
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEipPGI--THVLLL--KDG 219
|
..
gi 1472203387 213 RV 214
Cdd:COG1119 220 RV 221
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
5-214 |
4.72e-35 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 124.62 E-value: 4.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------- 74
Cdd:cd03245 2 RIEFRNVSFSYPN---QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-DGTDirqldpadlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDSVLLpWKNVRQNaefplvIQKKQTEENEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVS 143
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDN------ITLGAPLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 144 IVRALSYDAPLLLMDEPFGALDALTRDHLNEElLKIWQKTkKTVIFVTHsieEATFLS--DRVLVMSArpGRV 214
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKER-LRQLLGD-KTLIIITH---RPSLLDlvDRIIVMDS--GRI 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
5-207 |
8.06e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.93 E-value: 8.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD---------- 74
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKI-IIDGVDitdkkvklsd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMGFVFQ-DSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLS--EFKTALPRELSGGMKQRVSIVRALS 149
Cdd:PRK13637 81 irKKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 150 YDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-215 |
1.06e-34 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 123.43 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 30 NLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGA-------DQQMGFVFQDSVLLPWKNVRQNAEFPLVI 102
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQShtglapyQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 103 QKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQK 182
Cdd:TIGR01277 98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177
|
170 180 190
....*....|....*....|....*....|...
gi 1472203387 183 TKKTVIFVTHSIEEATFLSDRVLVMSArpGRVK 215
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQ--GKIK 208
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-248 |
1.33e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.38 E-value: 1.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 2 SEYSVELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-------IIGNLDkpTSGTIEYrDGAD 74
Cdd:COG1117 8 LEPKIEVRNLNVYYG-----DKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILL-DGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ------------QQMGFVFQDSVLLPwKNVRQNAEFPLVIQKKQteeNEKKLDEL----LELAGL-SEFKTAL---PREL 134
Cdd:COG1117 80 iydpdvdvvelrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIK---SKSELDEIveesLRKAALwDEVKDRLkksALGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 135 SGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLnEELlkIWQ-KTKKTVIFVTHSIEEATFLSDRVLVMSArpGr 213
Cdd:COG1117 156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKI-EEL--ILElKKDYTIVIVTHNMQQAARVSDYTAFFYL--G- 229
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1472203387 214 vkEMVEIDLP-----RPRGEATRNdpkfteynkYLRGIIG 248
Cdd:COG1117 230 --ELVEFGPTeqiftNPKDKRTED---------YITGRFG 258
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-207 |
2.01e-34 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 122.58 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-IIGNLDKpTSGTIEYRDGadqqMGFVFQdsvlLPW-KN--VRQNA 96
Cdd:cd03250 16 ETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS----IAYVSQ----EPWiQNgtIRENI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 97 EFPLviqkkqtEENEKKLDELLELAGLSEFKTALPR-------E----LSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:cd03250 87 LFGK-------PFDEERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1472203387 166 ALTRDHLNEE-LLKIWQKtKKTVIFVTHSIEeatFLS--DRVLVM 207
Cdd:cd03250 160 AHVGRHIFENcILGLLLN-NKTRILVTHQLQ---LLPhaDQIVVL 200
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
22-226 |
3.25e-34 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 124.81 E-value: 3.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGT--------IEYRDGADQQMGFVFQ----DSVLLPW 89
Cdd:TIGR01188 5 DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTarvagydvVREPRKVRRSIGIVPQyasvDEDLTGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFpLVIQKKqteENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTR 169
Cdd:TIGR01188 85 ENLEMMGRL-YGLPKD---EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 170 DHLNEELLKIwQKTKKTVIFVTHSIEEATFLSDRVLVMS-------ARPGRVKEMVEIDLPRPR 226
Cdd:TIGR01188 161 RAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDhgriiaeGTPEELKRRLGKDTLESR 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-206 |
3.76e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.77 E-value: 3.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 30 NLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGADQQ--------MGFVFQDSVLLPWKNVRQNAEFPLV 101
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TLNGQDHTttppsrrpVSMLFQENNLFSHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 102 IQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQ 181
Cdd:PRK10771 98 PGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180
....*....|....*....|....*
gi 1472203387 182 KTKKTVIFVTHSIEEATFLSDRVLV 206
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-214 |
3.86e-34 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 122.09 E-value: 3.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLlKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------QQ 76
Cdd:cd03266 2 ITADALTKRFRDV-KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATV-DGFDvvkepaearRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLL 156
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 157 MDEPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03266 160 LDEPTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHR--GRV 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
5-207 |
1.10e-33 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 127.02 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY---------RDGADQ 75
Cdd:TIGR02857 321 SLEFSGVSVAYPG----RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVngvpladadADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDSVLLPwKNVRQNaefplvIQKKQTEENEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVSI 144
Cdd:TIGR02857 397 QIAWVPQHPFLFA-GTIAEN------IRLARPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 145 VRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQktKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
6-214 |
1.49e-33 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 119.07 E-value: 1.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIE----------YRDGADQ 75
Cdd:cd03216 1 LELRGITKRFGG-----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILvdgkevsfasPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQdsvllpwknvrqnaefplviqkkqteenekkldellelaglsefktalpreLSGGMKQRVSIVRALSYDAPLL 155
Cdd:cd03216 76 GIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 156 LMDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVL--RDGRV 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-234 |
3.10e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.52 E-value: 3.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 2 SEYSVELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD------- 74
Cdd:COG1129 1 AEPLLEMRGISKSFGG-----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL-DGEPvrfrspr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 --QQMG--FVFQDSVLLPWKNVRQN-------AEFPLVIQKKQTEENEKKLDELlelaGLSEFKTALPRELSGGMKQRVS 143
Cdd:COG1129 75 daQAAGiaIIHQELNLVPNLSVAENiflgrepRRGGLIDWRAMRRRARELLARL----GLDIDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 144 IVRALSYDAPLLLMDEPFGALDALTRDHLNeELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGR---------- 213
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLF-RIIRRLKAQGVAIIYISHRLDEVFEIADRVTVL--RDGRlvgtgpvael 227
|
250 260
....*....|....*....|....*...
gi 1472203387 214 -----VKEMV--EIDLPRPRGEATRNDP 234
Cdd:COG1129 228 tedelVRLMVgrELEDLFPKRAAAPGEV 255
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
20-207 |
4.52e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 118.90 E-value: 4.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD-------QQMGFVFQDS-VLLPWKN 91
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL-NGKPikakerrKSIGYVMQDVdYQLFTDS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRqnAEfpLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDaltRDH 171
Cdd:cd03226 89 VR--EE--LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD---YKN 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 1472203387 172 LNE--ELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:cd03226 162 MERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
26-232 |
7.35e-32 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 117.60 E-value: 7.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR-------DGA-------DQQMgfVFQDSV--LLPW 89
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqdlyqlDRKqrrafrrDVQL--VFQDSPsaVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLV-IQKKQTEENEKKLDELLELAGL-SEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAL 167
Cdd:TIGR02769 105 MTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 168 TRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGR-VKEMVEIDLPRPRGEATRN 232
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK--GQiVEECDVAQLLSFKHPAGRN 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-234 |
7.50e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.67 E-value: 7.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSNLlkedtVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGADQQM--- 77
Cdd:COG3845 1 MMPPALELRGITKRFGGV-----VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI-DGKPVRIrsp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 --------GFVFQDSVLLPWKNVRQN----AE--FPLVIQKKQTeenEKKLDELLELAGLSEFKTALPRELSGGMKQRVS 143
Cdd:COG3845 75 rdaialgiGMVHQHFMLVPNLTVAENivlgLEptKGGRLDRKAA---RARIRELSERYGLDVDPDAKVEDLSVGEQQRVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 144 IVRALSYDAPLLLMDEP------------FGALDALTRDHlneellkiwqktkKTVIFVTHSIEEATFLSDRVLVMsaRP 211
Cdd:COG3845 152 ILKALYRGARILILDEPtavltpqeadelFEILRRLAAEG-------------KSIIFITHKLREVMAIADRVTVL--RR 216
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1472203387 212 GRV---------------KEMV--EIDLPRPRGEATRNDP 234
Cdd:COG3845 217 GKVvgtvdtaetseeelaELMVgrEVLLRVEKAPAEPGEV 256
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-216 |
3.67e-31 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 114.55 E-value: 3.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 2 SEYSVELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEyRDGA-----DQQ 76
Cdd:cd03220 14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT-VRGRvssllGLG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFvfqdsvlLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLL 156
Cdd:cd03220 93 GGF-------NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 157 MDEPFGALDALTRDHLNEELLKIWQKTkKTVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEK--GKIRF 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
6-215 |
6.77e-31 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 113.44 E-value: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkedTVALKDINLQIRPGeFISIIGPSGCGKSTLLRIIGNLDKPTSGTIE--------YRDGADQQM 77
Cdd:cd03264 1 LQLENLTKRYGK-----KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRidgqdvlkQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIwqKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVK 215
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNK--GKLV 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-207 |
8.19e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 112.71 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGAdqQMGFVFQDSVL---LPwKNVRQNAE 97
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA--RVAYVPQRSEVpdsLP-LTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 98 F----PLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLN 173
Cdd:NF040873 80 MgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|....
gi 1472203387 174 eELLKIWQKTKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:NF040873 160 -ALLAEEHARGATVVVVTHDLELVR-RADPCVLL 191
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
26-170 |
2.26e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 112.19 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLR-IIGNLDKP--TSGTIeYRDGAD--------QQMGFVFQDSVLLPWKNVRQ 94
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEV-LLNGRRltalpaeqRRIGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 95 NAEF--PLVIQKKQTEEnekKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRD 170
Cdd:COG4136 96 NLAFalPPTIGRAQRRA---RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-216 |
2.39e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.87 E-value: 2.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEySVELKGLNKVY-----------------SNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPT 63
Cdd:COG1134 1 MSS-MIEVENVSKSYrlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 64 SGTIEyRDGA-----DQQMGFVFQDSvllpwknVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEF-----KTalpre 133
Cdd:COG1134 80 SGRVE-VNGRvsallELGAGFHPELT-------GRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFidqpvKT----- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 134 LSGGMKQRV--SIvrALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTkKTVIFVTHSIEEATFLSDRVLVMSArp 211
Cdd:COG1134 147 YSSGMRARLafAV--ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEK-- 221
|
....*
gi 1472203387 212 GRVKE 216
Cdd:COG1134 222 GRLVM 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-225 |
2.48e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.06 E-value: 2.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------Q 75
Cdd:PRK13650 5 IEVKNLTFKYKE--DQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQI-IIDGDLlteenvwdirH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQ--DSVLLPwKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:PRK13650 82 KIGMVFQnpDNQFVG-ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 154 LLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATfLSDRVLVM-------SARP----GRVKEMVEIDL 222
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMkngqvesTSTPrelfSRGNDLLQLGL 239
|
...
gi 1472203387 223 PRP 225
Cdd:PRK13650 240 DIP 242
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-197 |
6.31e-30 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 111.41 E-value: 6.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI------------EYRDGAD-QQMGFVFQDSVLLPWKNV 92
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVslvgqplhqmdeEARAKLRaKHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 93 RQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHL 172
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|....*
gi 1472203387 173 NEELLKIWQKTKKTVIFVTHSIEEA 197
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-207 |
1.61e-29 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 110.06 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD-----GADQQMGFV 80
Cdd:cd03269 1 LEVENVTKRFG-----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkpldiAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 81 FQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1472203387 161 FGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:cd03269 156 FSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLL 201
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
26-231 |
2.40e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.93 E-value: 2.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR-------DGADQ-------QMgfVFQDSV--LLPW 89
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRgeplaklNRAQRkafrrdiQM--VFQDSIsaVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLV-IQKKQTEENEKKLDELLELAGLS-EFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAL 167
Cdd:PRK10419 106 KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 168 TRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEmveidlPRPRGEATR 231
Cdd:PRK10419 186 LQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDN--GQIVE------TQPVGDKLT 241
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
22-207 |
3.28e-29 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 115.18 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLPwKN 91
Cdd:TIGR02204 352 DQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL-DGVDlrqldpaelrARMALVPQDPVLFA-AS 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNAEFplviqkKQTEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:TIGR02204 430 VMENIRY------GRPDATDEEVEAAARAAHAHEFISALPEgydtylgergvTLSGGQRQRIAIARAILKDAPILLLDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 161 FGALDALTRDHLN---EELLKiwqktKKTVIFVTHSIeeATFLS-DRVLVM 207
Cdd:TIGR02204 504 TSALDAESEQLVQqalETLMK-----GRTTLIIAHRL--ATVLKaDRIVVM 547
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-207 |
4.17e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 107.69 E-value: 4.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------QQ 76
Cdd:cd03246 2 EVENVSFRYPG---AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-RLDGADisqwdpnelgDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPwKNVRQNAefplviqkkqteenekkldellelaglsefktalpreLSGGMKQRVSIVRALSYDAPLLL 156
Cdd:cd03246 78 VGYLPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 157 MDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLA-SADRILVL 168
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
25-208 |
7.55e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 108.42 E-value: 7.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD-------------QQMGFVFQDSVLLPWKN 91
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF-SGHDitrlknrevpflrRQIGMIFQDHHLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDaltrDH 171
Cdd:PRK10908 96 VYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1472203387 172 LNEELLKIWQKTKK---TVIFVTHSIEEATFLSDRVLVMS 208
Cdd:PRK10908 172 LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLS 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-216 |
9.91e-29 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 108.47 E-value: 9.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLPw 89
Cdd:cd03251 12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGHDvrdytlaslrRQIGLVSQDVFLFN- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNaefplvIQKKQTEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMD 158
Cdd:cd03251 90 DTVAEN------IAYGRPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 159 EPFGALDALTRDHLNEELLKIWQktKKTVIFVTH---SIEEAtflsDRVLVMSArpGRVKE 216
Cdd:cd03251 164 EATSALDTESERLVQAALERLMK--NRTTFVIAHrlsTIENA----DRIVVLED--GKIVE 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
26-214 |
3.72e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 105.71 E-value: 3.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLDKP-TSGTIEYrDGADQ-------QMGFVFQDSVLLPWKNVRQNA 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALaGRRTGLgVSGEVLI-NGRPLdkrsfrkIIGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 97 EFplviqkkqteenekkldellelaglsefkTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTrDHLNEEL 176
Cdd:cd03213 104 MF-----------------------------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS-ALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 1472203387 177 LKIWQKTKKTVIFVTHSI-EEATFLSDRVLVMSarPGRV 214
Cdd:cd03213 154 LRRLADTGRTIICSIHQPsSEIFELFDKLLLLS--QGRV 190
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-215 |
8.99e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 108.42 E-value: 8.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 28 DINLQIrPGEFIS-IIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD----GADQQ---------MGFVFQDSVLLPWKNVR 93
Cdd:PRK11144 16 TVNLTL-PAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfDAEKGiclppekrrIGYVFQDARLFPHYKVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNAEFPLviqkkqTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDaLTRDHln 173
Cdd:PRK11144 95 GNLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKR-- 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1472203387 174 eELLKIWQKTKKTV----IFVTHSIEEATFLSDRVLVMSArpGRVK 215
Cdd:PRK11144 166 -ELLPYLERLAREInipiLYVSHSLDEILRLADRVVVLEQ--GKVK 208
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
25-207 |
1.10e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.03 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD-----GAD--------QQMGFVFQ--DSVLLPw 89
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitaGKKnkklkplrKKVGIVFQfpEHQLFE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEF-PLVIQKKQtEENEKKLDELLELAGLSE-FKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAL 167
Cdd:PRK13634 101 ETVEKDICFgPMNFGVSE-EDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1472203387 168 TRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-193 |
1.86e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 109.76 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGADQQ----------MGFVFQDSVLLPwKN 91
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTL-DGVPVSsldqdevrrrVSVCAQDAHLFD-TT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNaefpLVIQKKQTEENEkkLDELLELAGLSEFKTALP-----------RELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:TIGR02868 425 VREN----LRLARPDATDEE--LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498
|
170 180 190
....*....|....*....|....*....|...
gi 1472203387 161 FGALDALTRDHLNEELLKIwqKTKKTVIFVTHS 193
Cdd:TIGR02868 499 TEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-209 |
1.91e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.61 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD--------G 72
Cdd:PRK13536 37 MSTVAIDLAGVSKSYG-----DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 73 ADQQMGFVFQDSVLLPWKNVRQNaefpLVIQKK----QTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:PRK13536 112 ARARIGVVPQFDNLDLEFTVREN----LLVFGRyfgmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 149 SYDAPLLLMDEPFGALDALTRdHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSA 209
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHAR-HLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEA 247
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-208 |
2.11e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.84 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 11 LNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDG----------ADQQMGFV 80
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGitiskenlkeIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 81 FQ--DSVLLPwKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMD 158
Cdd:PRK13632 89 FQnpDNQFIG-ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1472203387 159 EPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATfLSDRVLVMS 208
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFS 216
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
26-217 |
2.19e-27 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 105.00 E-value: 2.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLPwKNVRQN 95
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-DGQDirevtldslrRAIGVVPQDTVLFN-DTIGYN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 aefplvIQKKQTEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:cd03253 95 ------IRYGRPDATDEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDEATSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 165 DALTRDHLNEELLKIwqKTKKTVIFVTHSIEEATFlSDRVLVMSArpGRVKEM 217
Cdd:cd03253 169 DTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKD--GRIVER 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-203 |
2.37e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 105.24 E-value: 2.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNkVYSNLLKedtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIG--------------------NLD 60
Cdd:PRK14239 1 MTEPILQVSDLS-VYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmndlnpevtitgsivynghNIY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 61 KPTSGTIEYRdgadQQMGFVFQDSVLLPWkNVRQNAEFPLVIQKkqtEENEKKLDELLE--LAGLS---EFKTALPRE-- 133
Cdd:PRK14239 76 SPRTDTVDLR----KEIGMVFQQPNPFPM-SIYENVVYGLRLKG---IKDKQVLDEAVEksLKGASiwdEVKDRLHDSal 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 134 -LSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIwqKTKKTVIFVTHSIEEATFLSDR 203
Cdd:PRK14239 148 gLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-216 |
4.09e-27 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.48 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD------ 74
Cdd:PRK13635 1 MKEEIIRVEHISFRYPD---AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVlseetv 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ----QQMGFVFQDSvllpwKN------VRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSI 144
Cdd:PRK13635 77 wdvrRQVGMVFQNP-----DNqfvgatVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 145 VRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFlSDRVLVMsaRPGRVKE 216
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVM--NKGEILE 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-207 |
4.65e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 103.45 E-value: 4.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllKEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADQ-------QMG 78
Cdd:cd03268 1 LKTNDLTKTY----GKKRV-LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQkniealrRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 79 FVFQDSVLLPWKNVRQNaefpLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMD 158
Cdd:cd03268 76 ALIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1472203387 159 EPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:cd03268 152 EPTNGLDPDGIKEL-RELILSLRDQGITVLISSHLLSEIQKVADRIGII 199
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-207 |
4.90e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 4.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI--------EYRDG 72
Cdd:PRK13537 3 MSVAPIDFRNVEKRYG-----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIslcgepvpSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 73 ADQQMGFVFQDSVLLPWKNVRQNaefpLVIQKK----QTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVREN----LLVFGRyfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 149 SYDAPLLLMDEPFGALDALTRdHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQAR-HLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVI 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-217 |
1.04e-26 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 107.91 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeyR-DGAD----------QQMGFVFQDSVLLPw 89
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV--RlDGADlsqwdreelgRHIGYLPQDVELFD- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQN-AEFPlviqkkqtEENEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVSIVRALsYDAP-LLL 156
Cdd:COG4618 420 GTIAENiARFG--------DADPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARAL-YGDPrLVV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 157 MDEPFGALDALTRDHLNeELLKIWQKTKKTVIFVTH--SIEEATflsDRVLVMsaRPGRVKEM 217
Cdd:COG4618 491 LDEPNSNLDDEGEAALA-AAIRALKARGATVVVITHrpSLLAAV---DKLLVL--RDGRVQAF 547
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-217 |
1.26e-26 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 102.69 E-value: 1.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------QQMGFVFQDSVLLPw 89
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-LIDGIDirdisrkslrSMIGVVLQDTFLFS- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNaefplvIQKKQTEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMD 158
Cdd:cd03254 91 GTIMEN------IRLGRPNATDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILILD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 159 EPFGALDALTRDHLNEELLKIwqKTKKTVIFVTH---SIEEAtflsDRVLVMsaRPGRVKEM 217
Cdd:cd03254 165 EATSNIDTETEKLIQEALEKL--MKGRTSIIIAHrlsTIKNA----DKILVL--DDGKIIEE 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-248 |
1.33e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 103.71 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 2 SEYSVELKGLNKVYSNLLkedtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDK--PT---SGTIEYRD----- 71
Cdd:PRK14243 7 TETVLRTENLNVYYGSFL-----AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGknlya 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 72 -GAD-----QQMGFVFQDSVLLPwKNVRQNAEFPLVIQKKQTEenekkLDELLEL----AGL-SEFKTALPRE---LSGG 137
Cdd:PRK14243 82 pDVDpvevrRRIGMVFQKPNPFP-KSIYDNIAYGARINGYKGD-----MDELVERslrqAALwDEVKDKLKQSglsLSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 138 MKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLnEELLKIWqKTKKTVIFVTHSIEEATFLSDRVLVMSARP----GR 213
Cdd:PRK14243 156 QQQRLCIARAIAVQPEVILMDEPCSALDPISTLRI-EELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNVELteggGR 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1472203387 214 VKEMVEIDlprpRGEATRNDPKFTEYNKYLRGIIG 248
Cdd:PRK14243 234 YGYLVEFD----RTEKIFNSPQQQATRDYVSGRFG 264
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-207 |
2.49e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.24 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD-----------QQMGFVFQ--DSVLL 87
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKV-YVDGLDtsdeenlwdirNKAGMVFQnpDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 88 PwKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAL 167
Cdd:PRK13633 100 A-TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1472203387 168 TRDHLNEELLKIWQKTKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:PRK13633 179 GRREVVNTIKELNKKYGITIILITHYMEEAV-EADRIIVM 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-214 |
4.23e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.88 E-value: 4.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD------QQMG 78
Cdd:COG4152 1 MLELKGLTKRFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW-DGEPldpedrRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 79 FVFQDSVLLPWKNVRQNAEFpLV----IQKKqteENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPL 154
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVY-LArlkgLSKA---EAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 155 LLMDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTH---SIEEatfLSDRVLVMSArpGRV 214
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHqmeLVEE---LCDRIVIINK--GRK 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
8-208 |
5.32e-26 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 101.25 E-value: 5.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 8 LKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI--------EYRDGADQQMGF 79
Cdd:cd03267 19 LIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrvaglvpwKRRKKFLRRIGV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 80 VFQDSVLLPWK-NVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMD 158
Cdd:cd03267 99 VFGQKTQLWWDlPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1472203387 159 EPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVID 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-216 |
9.78e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSnllkEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY--------RDG 72
Cdd:PRK10619 1 MSENKLNVIDLHKRYG----EHEV-LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvRDK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 73 ADQ--------------QMGFVFQDSVLLPWKNVRQNA-EFPLVIQKKQTEENEKKLDELLELAGLSE-FKTALPRELSG 136
Cdd:PRK10619 76 DGQlkvadknqlrllrtRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 137 GMKQRVSIVRALSYDAPLLLMDEPFGALDAltrdHLNEELLKIWQKTK---KTVIFVTHSIEEATFLSDRVLVMsaRPGR 213
Cdd:PRK10619 156 GQQQRVSIARALAMEPEVLLFDEPTSALDP----ELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFL--HQGK 229
|
...
gi 1472203387 214 VKE 216
Cdd:PRK10619 230 IEE 232
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
6-214 |
1.47e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 100.54 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------Q 75
Cdd:COG4604 2 IEIKNVSKRYG-----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLV-DGLDvattpsrelaK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDSVLLPWKNVRQnaefpLVI-------QKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:COG4604 76 RLAILRQENHINSRLTVRE-----LVAfgrfpysKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 149 SYDAPLLLMDEPFGALD--------ALTRdHLNEELlkiwqktKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDmkhsvqmmKLLR-RLADEL-------GKTVVIVLHDINFASCYADHIVAM--KDGRV 214
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
5-207 |
2.18e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIE---YRDGAD------- 74
Cdd:PRK13641 2 SIKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagYHITPEtgnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ---QQMGFVFQDSVLLPWKN-VRQNAEF-PLVIQKKQTEENEKKLdELLELAGLSE-FKTALPRELSGGMKQRVSIVRAL 148
Cdd:PRK13641 82 klrKKVSLVFQFPEAQLFENtVLKDVEFgPKNFGFSEDEAKEKAL-KWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 149 SYDAPLLLMDEPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEM-MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVL 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-207 |
2.51e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 103.75 E-value: 2.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 2 SEYSVELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI--------EYRDGA 73
Cdd:PRK11160 335 DQVSLTLNNVSFTYPD---QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIllngqpiaDYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 74 -DQQMGFVFQdSVLLPWKNVRQNaefpLVIQKKQteENEKKLDELLELAGLS---EFKTALP-------RELSGGMKQRV 142
Cdd:PRK11160 412 lRQAISVVSQ-RVHLFSATLRDN----LLLAAPN--ASDEALIEVLQQVGLEkllEDDKGLNawlgeggRQLSGGEQRRL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 143 SIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQktKKTVIFVTHsieEATFLS--DRVLVM 207
Cdd:PRK11160 485 GIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITH---RLTGLEqfDRICVM 546
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
28-231 |
4.12e-25 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 98.98 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 28 DINLQIRPGEFISIIGPSGCGKS-TLLRIIGNLDK---PTSGTIeYRDGAD--------QQMGFVFQD--SVLLPWKNVR 93
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPgltQTSGEI-LLDGRPllplsirgRHIATIMQNprTAFNPLFTMG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTAL---PRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRD 170
Cdd:TIGR02770 83 NHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 171 HLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEM--VEIDLPRPRGEATR 231
Cdd:TIGR02770 163 RVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD--GRIVERgtVKEIFYNPKHETTR 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-214 |
4.45e-25 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 98.66 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD------QQ---- 76
Cdd:cd03224 2 EVENLNAGY-----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF-DGRDitglppHErara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 -MGFVFQDSVLLPWKNVRQNAEfpLVIQKKQTEENEKKLDELLEL-AGLSEFKTALPRELSGGMKQRVSIVRALSYDAPL 154
Cdd:cd03224 76 gIGYVPEGRRIFPELTVEENLL--LGAYARRRAKRKARLERVYELfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 155 LLMDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLER--GRV 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-214 |
4.87e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 99.32 E-value: 4.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGA-----DQQMGfvfQDSVLLPWK------ 90
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlsSRQLA---RRLALLPQHhltpeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 91 -NVRQNAEF---P-LVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:PRK11231 91 iTVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 166 altrdhLNE--ELLKIWQKTK---KTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:PRK11231 171 ------INHqvELMRLMRELNtqgKTVVTVLHDLNQASRYCDHLVVLAN--GHV 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
24-216 |
5.11e-25 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 98.71 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------QQMGFVFQDSVLLPwKNVR 93
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-LVDGHDlaladpawlrRQVGVVLQENVLFN-RSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNaefplvIQKKQTEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:cd03252 94 DN------IALADPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 163 ALDALTRDHLNEELLKIWQktKKTVIFVTHSIeEATFLSDRVLVMSArpGRVKE 216
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA--GRTVIIIAHRL-STVKNADRIIVMEK--GRIVE 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-231 |
5.16e-25 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 102.84 E-value: 5.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTL----LRIIgnldkPTSGTIEYrDGAD-------------QQMGFVFQ 82
Cdd:COG4172 296 VGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRF-DGQDldglsrralrplrRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 83 D--SVLLPWKNVRQNAEFPLVIQKKQT--EENEKKLDELLELAGLS-EFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:COG4172 370 DpfGSLSPRMTVGQIIAEGLRVHGPGLsaAERRARVAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKEMVEID--LPRPRGEATR 231
Cdd:COG4172 450 DEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVM--KDGKVVEQGPTEqvFDAPQHPYTR 523
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
26-214 |
6.18e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.08 E-value: 6.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLdKPTSGTIEYrDGAD-----------------QQ--MGFVFqdSV 85
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRL-NGRPladwspaelarrravlpQHssLSFPF--TV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 86 -------LLPWKNVRQNAEfPLViqkkqteenekklDELLELAGLSEFKTALPRELSGGMKQRVSIVRAL------SYDA 152
Cdd:PRK13548 94 eevvamgRAPHGLSRAEDD-ALV-------------AAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 153 PLLLMDEPFGALDaLTRDHLNEELLKiwQKTKK---TVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:PRK13548 160 RWLLLDEPTSALD-LAHQHHVLRLAR--QLAHErglAVIVVLHDLNLAARYADRIVLLHQ--GRL 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
24-209 |
6.97e-25 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 98.28 E-value: 6.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLdKPTSGTIEYRDG---------ADQQM--------GFVFQDSV 85
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIyGNY-LPDSGSILVRHDggwvdlaqaSPREIlalrrrtiGYVSQFLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 86 LLPwknvRQNAE----FPLVIQKKQTEENEKKLDELLELAGLSEfktAL----PRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:COG4778 104 VIP----RVSALdvvaEPLLERGVDREEARARARELLARLNLPE---RLwdlpPATFSGGEQQRVNIARGFIADPPLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 158 DEPFGALDALTRDHLNEELLKiwqktKK----TVIFVTHSIEEATFLSDRVLVMSA 209
Cdd:COG4778 177 DEPTASLDAANRAVVVELIEE-----AKargtAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-217 |
1.10e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 99.65 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYS---NLLK-EDTV-ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD- 74
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPvkrGLFKpERLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY-QGQDl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ------------QQMGFVFQD--SVLLPWKNVRQNAEFPLVIQKKQT-EENEKKLDELLELAGL-SEFKTALPRELSGGM 138
Cdd:PRK11308 80 lkadpeaqkllrQKIQIVFQNpyGSLNPRKKVGQILEEPLLINTSLSaAERREKALAMMAKVGLrPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 139 KQRVSIVRALSYDAPLLLMDEPFGALDALTRDH-LNeeLLKIWQKTKKTV-IFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQvLN--LMMDLQQELGLSyVFISHDLSVVEHIADEVMVMYL--GRCVE 235
|
.
gi 1472203387 217 M 217
Cdd:PRK11308 236 K 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
26-231 |
1.11e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGAdqQMGFVFQDSVLLPWKNVRQNAE--FPLVIQ 103
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--RIGYLPQEPPLDDDLTVLDTVLdgDAELRA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 104 KKQ-----------TEENEKKLDELLE-----------------LAGLsEFKTALP----RELSGGMKQRVSIVRALSYD 151
Cdd:COG0488 92 LEAeleeleaklaePDEDLERLAELQEefealggweaearaeeiLSGL-GFPEEDLdrpvSELSGGWRRRVALARALLSE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 152 APLLLMDEPFGALDALTRDHLnEELLKiwqKTKKTVIFVTHsieEATFLsDRVlvmsarpgrVKEMVEIDlprpRGEATR 231
Cdd:COG0488 171 PDLLLLDEPTNHLDLESIEWL-EEFLK---NYPGTVLVVSH---DRYFL-DRV---------ATRILELD----RGKLTL 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-207 |
1.51e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.84 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLdKPTSGTI--------EYRDGADQQMGFVFQdSVLLPWKN 91
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLtGDL-KPQQGEItldgvpvsDLEKALSSLISVLNQ-RPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNaefplviqkkqteenekkldellelaglsefktaLPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDH 171
Cdd:cd03247 91 LRNN----------------------------------LGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 1472203387 172 LNEELLKiwQKTKKTVIFVTH---SIEEAtflsDRVLVM 207
Cdd:cd03247 137 LLSLIFE--VLKDKTLIWITHhltGIEHM----DKILFL 169
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-217 |
2.33e-24 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 97.23 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------Q 75
Cdd:cd03249 1 IEFKNVSFRYPS--RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILL-DGVDirdlnlrwlrS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDSVLLPwKNVRQNAEFPLviqKKQTEENEkklDELLELAGLSEFKTALPR-----------ELSGGMKQRVSI 144
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENIRYGK---PDATDEEV---EEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 145 VRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIwqKTKKTVIFVTH---SIEEAtflsDRVLVMSarPGRVKEM 217
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRA--MKGRTTIVIAHrlsTIRNA----DLIAVLQ--NGQVVEQ 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-226 |
3.78e-24 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 97.14 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNkvysnLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDG------------- 72
Cdd:PRK11831 8 VDMRGVS-----FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF-DGenipamsrsrlyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 73 ADQQMGFVFQDSVLLPWKNVRQNAEFPLviqKKQTEENEKKLDEL----LELAGLSEFKTALPRELSGGMKQRVSIVRAL 148
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAYPL---REHTQLPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 149 SYDAPLLLMDEPFGALDALTR-------DHLNEELlkiwqktKKTVIFVTHSIEEATFLSDRVLVMSAR----PGRVKEM 217
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMgvlvkliSELNSAL-------GVTCVVVSHDVPEVLSIADHAYIVADKkivaHGSAQAL 231
|
....*....
gi 1472203387 218 VEIDLPRPR 226
Cdd:PRK11831 232 QANPDPRVR 240
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-207 |
6.41e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.92 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-IIGNLdkPTSGT-----IEYR--DGAD--QQMGFVFQDSvLLPWK 90
Cdd:PRK11174 361 DGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSlkingIELRelDPESwrKHLSWVGQNP-QLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 91 NVRQNaefplvIQKKQTEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:PRK11174 438 TLRDN------VLLGNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDE 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1472203387 160 PFGALDALTRDHLNEELLKIWQktKKTVIFVTHSIEEATFLsDRVLVM 207
Cdd:PRK11174 512 PTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVM 556
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-217 |
6.70e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.65 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLPwKNVRQ 94
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILI-DGTDirtvtraslrRNIAVVFQDAGLFN-RSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 95 NaefplvIQKKQTEENEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVSIVRALSYDAPLLLMDEPFGA 163
Cdd:PRK13657 428 N------IRVGRPDATDEEMRAAAERAQAHDFIERKPdgydtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSA 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 164 LDALTRDHLNEELLKIWQktKKTVIFVTH---SIEEAtflsDRVLVMSArpGRVKEM 217
Cdd:PRK13657 502 LDVETEAKVKAALDELMK--GRTTFIIAHrlsTVRNA----DRILVFDN--GRVVES 550
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
10-216 |
8.27e-24 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 96.05 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 10 GLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY--RDGADQQM---------- 77
Cdd:TIGR02323 8 GLSKSYGG-----GKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimRSGAELELyqlseaerrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 ------GFVFQDsvllPWKNVRQN-------AEFPLVIQKKQ----TEENEKKLDEL-LELAGLSEfktaLPRELSGGMK 139
Cdd:TIGR02323 83 lmrtewGFVHQN----PRDGLRMRvsaganiGERLMAIGARHygniRATAQDWLEEVeIDPTRIDD----LPRAFSGGMQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 140 QRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKE 216
Cdd:TIGR02323 155 QRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM--QQGRVVE 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
9-216 |
1.00e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 95.76 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 9 KGLNKVYSNLlkedtVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY--RDGADQQM--------- 77
Cdd:PRK11701 10 RGLTKLYGPR-----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmRDGQLRDLyalseaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 -------GFVFQDS------------------VLLPWK---NVRQNAEFPLviqkKQTEENEKKLDELlelaglsefkta 129
Cdd:PRK11701 85 rllrtewGFVHQHPrdglrmqvsaggnigerlMAVGARhygDIRATAGDWL----ERVEIDAARIDDL------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 130 lPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDA--------LTRDHLNEELLkiwqktkkTVIFVTHSIEEATFLS 201
Cdd:PRK11701 149 -PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVsvqarlldLLRGLVRELGL--------AVVIVTHDLAVARLLA 219
|
250
....*....|....*
gi 1472203387 202 DRVLVMsaRPGRVKE 216
Cdd:PRK11701 220 HRLLVM--KQGRVVE 232
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
5-216 |
1.37e-23 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 94.48 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNLLKedtVALKDINLQIRPGEFISIIGPSGCGKST----LLRIIgnldKPTSGTIEYrDGAD------ 74
Cdd:cd03244 2 DIEFKNVSLRYRPNLP---PVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILI-DGVDiskigl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ----QQMGFVFQDSVLLPwKNVRQNAEfPLviqkkqTEENEKKLDELLELAGLSEFKTALP-----------RELSGGMK 139
Cdd:cd03244 74 hdlrSRISIIPQDPVLFS-GTIRSNLD-PF------GEYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 140 QRVSIVRALSYDAPLLLMDEPFGALDALTrDHLNEELLKIWQKtKKTVIFVTHSIEeaTFL-SDRVLVMSArpGRVKE 216
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPET-DALIQKTIREAFK-DCTVLTIAHRLD--TIIdSDRILVLDK--GRVVE 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
26-219 |
1.56e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.73 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADqqMGFVFQDSvLLPWKNVRQNAEFPlviqkk 105
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGAR--VLFLPQRP-YLPLGTLREALLYP------ 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 106 QTEEN--EKKLDELLELAGLSEFKTAL------PRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELL 177
Cdd:COG4178 450 ATAEAfsDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR 529
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1472203387 178 KIWQKTkkTVIFVTHSiEEATFLSDRVLVMSARPGRVKEMVE 219
Cdd:COG4178 530 EELPGT--TVISVGHR-STLAAFHDRVLELTGDGSWQLLPAE 568
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
26-214 |
1.99e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.18 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLdKPTSGTIEYrDGAD----------QQMGFVFQDSVL-LPWkNVR 93
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRL-NGRPlaawspwelaRRRAVLPQHSSLaFPF-TVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRAL-----SYDAP--LLLMDEPFGALDa 166
Cdd:COG4559 94 EVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwePVDGGprWLFLDEPTSALD- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1472203387 167 LTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG4559 173 LAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQ--GRL 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-214 |
2.42e-23 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 94.15 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDG----------ADQ 75
Cdd:cd03218 1 LRAENLSKRYGK-----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLL 155
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 156 LMDEPFGALDALTRdhlnEELLKIWQ--KTKKTVIFVT-HSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03218 156 LLDEPFAGVDPIAV----QDIQKIIKilKDRGIGVLITdHNVRETLSITDRAYIIYE--GKV 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-224 |
3.09e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 95.30 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD------ 74
Cdd:PRK13636 1 MEDYILKVEELNYNYS----DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPidysrk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ------QQMGFVFQD-SVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRA 147
Cdd:PRK13636 76 glmklrESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 148 LSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV------------K 215
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKE--GRVilqgnpkevfaeK 233
|
250
....*....|..
gi 1472203387 216 EM---VEIDLPR 224
Cdd:PRK13636 234 EMlrkVNLRLPR 245
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-216 |
3.57e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 94.47 E-value: 3.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 3 EYSVELKGLNKVY---SNLLKEDTV-ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI-------EYRD 71
Cdd:PRK15112 2 ETLLEVRNLSKTFryrTGWFRRQTVeAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 72 GA--DQQMGFVFQDSV--LLPWKNVRQNAEFPLVIQKK-QTEENEKKLDELLELAGL-SEFKTALPRELSGGMKQRVSIV 145
Cdd:PRK15112 82 YSyrSQRIRMIFQDPStsLNPRQRISQILDFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 146 RALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQ--GEVVE 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-192 |
4.97e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 90.97 E-value: 4.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrdGADQQMGFVFQdsv 85
Cdd:cd03221 1 IELENLSKTY-----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW--GSTVKIGYFEQ--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 86 llpwknvrqnaefplviqkkqteenekkldellelaglsefktalpreLSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:cd03221 71 ------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180
....*....|....*....|....*..
gi 1472203387 166 ALTRDHLNEELlkiwQKTKKTVIFVTH 192
Cdd:cd03221 103 LESIEALEEAL----KEYPGTVILVSH 125
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
25-216 |
5.69e-23 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 97.09 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLP---WKN 91
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL-DGHDladytlaslrRQVALVSQDVVLFNdtiANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNAefplviqkkQTEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:TIGR02203 426 IAYGR---------TEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 161 FGALDALTRDHLNEELLKIWQktKKTVIFVTH---SIEEAtflsDRVLVMSArpGRVKE 216
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQ--GRTTLVIAHrlsTIEKA----DRIVVMDD--GRIVE 547
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-208 |
8.70e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 8.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSG-------TIEYRD----GADQQMGFVFQ---DSVL 86
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGevlikgePIKYDKksllEVRKTVGIVFQnpdDQLF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 87 LPwkNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDA 166
Cdd:PRK13639 93 AP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1472203387 167 LTRDHLNeELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:PRK13639 171 MGASQIM-KLLYDLNKEGITIIISTHDVDLVPVYADKVYVMS 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-208 |
1.25e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 92.33 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLD---KPTSGTIEY------RDGADQQMGFVFQDSVLLPWKNVRQNA 96
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFngqprkPDQFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 97 EF--PLVIQKKQTEENEKKLDE--LLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHL 172
Cdd:cd03234 103 TYtaILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1472203387 173 NeELLKIWQKTKKTVIFVTHSIEEATF-LSDRVLVMS 208
Cdd:cd03234 183 V-STLSQLARRNRIVILTIHQPRSDLFrLFDRILLLS 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-207 |
1.88e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.94 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR---------DGADQQ 76
Cdd:PRK13652 4 IETRDLCYSYSG----SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRgepitkeniREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQ---DSVLLPwkNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:PRK13652 80 VGLVFQnpdDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 154 LLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-208 |
2.18e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 95.58 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY---------RDGADQQMGFVFQDSVLLPwKNVRQN 95
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfslkdidRHTLRQFINYLPQEPYIFS-GSILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 aefpLVIQKKQTEENEKkLDELLELAGLSE--------FKTALPRE---LSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:TIGR01193 568 ----LLLGAKENVSQDE-IWAACEIAEIKDdienmplgYQTELSEEgssISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1472203387 165 DALTRDHLNEELLKIwqkTKKTVIFVTHSIEEATfLSDRVLVMS 208
Cdd:TIGR01193 643 DTITEKKIVNNLLNL---QDKTIIFVAHRLSVAK-QSDKIIVLD 682
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-206 |
2.26e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 93.23 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIE--YRDGADQQMG----- 78
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEwiFKDEKNKKKTkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 79 ----FVFQDSVLLPWKNVR----------QNAEFPL---VIQKK----------QTEENEKKLDELLELAGLSE-FKTAL 130
Cdd:PRK13651 83 vlekLVIQKTRFKKIKKIKeirrrvgvvfQFAEYQLfeqTIEKDiifgpvsmgvSKEEAKKRAAKYIELVGLDEsYLQRS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 131 PRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAltrdHLNEELLKIWQ---KTKKTVIFVTHSIEEATFLSDRVLV 206
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDP----QGVKEILEIFDnlnKQGKTIILVTHDLDNVLEWTKRTIF 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-214 |
3.56e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 91.69 E-value: 3.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLdKPTSGTIEYrDGAD---------- 74
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIaGSL-PPDSGSILI-DGKDvtklpeykra 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDSVL--LPWKNVRQN--------AEFPLVIQKKQTEENEKKldELLELAGLS-----EFKTALpreLSGGMK 139
Cdd:COG1101 80 KYIGRVFQDPMMgtAPSMTIEENlalayrrgKRRGLRRGLTKKRRELFR--ELLATLGLGlenrlDTKVGL---LSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 140 QRVSIVRALSYDAPLLLMDEPFGALD--------ALTRdhlneellKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArp 211
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDpktaalvlELTE--------KIVEENNLTTLMVTHNMEQALDYGNRLIMMHE-- 224
|
...
gi 1472203387 212 GRV 214
Cdd:COG1101 225 GRI 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-214 |
4.17e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 93.75 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGT-------IEYRDG--ADQQMGFVFQDSVLLPWKNV 92
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTvlvagddVEALSAraASRRVASVPQDTSLSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 93 RQNAEFPLVIQKKQ----TEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDaLT 168
Cdd:PRK09536 95 RQVVEMGRTPHRSRfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD-IN 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1472203387 169 RDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLAD--GRV 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-208 |
4.78e-22 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 94.70 E-value: 4.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGT-------IEYR-DGADQQMGFVFQDSVLLPWKNVRQNA 96
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTvlvggkdIETNlDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 97 EFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEEL 176
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|..
gi 1472203387 177 LKIwqKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:TIGR01257 1105 LKY--RSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
25-214 |
7.24e-22 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 89.03 E-value: 7.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY----------RDGADQQMGFVFQD---SVLLPWKN 91
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgkpvtrrspRDAIRAGIAYVPEDrkrEGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNAefplviqkkqteenekkldellelaglsefktALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDH 171
Cdd:cd03215 95 VAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1472203387 172 LNEELLKIWQKtKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:cd03215 143 IYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYE--GRI 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-248 |
8.90e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.67 E-value: 8.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 3 EYSVELKGLNKVYSNllkedTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-------------------IIG-NLDKP 62
Cdd:PRK14267 2 KFAIETVNLRVYYGS-----NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrllelneearvegevrLFGrNIYSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 63 TSGTIEYRdgadQQMGFVFQDSVLLPWKNVRQNAEFPLVIQK--KQTEENEKKLDELLELAGL-SEFKTAL---PRELSG 136
Cdd:PRK14267 77 DVDPIEVR----REVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwDEVKDRLndyPSNLSG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 137 GMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIwqKTKKTVIFVTHSIEEATFLSDRVLVMSarpgrVKE 216
Cdd:PRK14267 153 GQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLY-----LGK 225
|
250 260 270
....*....|....*....|....*....|..
gi 1472203387 217 MVEIDLPRPRGEatrnDPKFTEYNKYLRGIIG 248
Cdd:PRK14267 226 LIEVGPTRKVFE----NPEHELTEKYVTGALG 253
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-216 |
1.17e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 93.21 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKS-TLLRIIGNLDKP---TSGTIEYrDGAD--------------QQMGFVF 81
Cdd:COG4172 20 GGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILF-DGQDllglserelrrirgNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 82 QD--SVLLPWKNV-RQNAEfPLVIQKKQT-EENEKKLDELLELAGLSEFKT---ALPRELSGGMKQRVSIVRALSYDAPL 154
Cdd:COG4172 99 QEpmTSLNPLHTIgKQIAE-VLRLHRGLSgAAARARALELLERVGIPDPERrldAYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 155 LLMDEPFGALDALTR----DHLNEelLKiwQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKE 216
Cdd:COG4172 178 LIADEPTTALDVTVQaqilDLLKD--LQ--RELGMALLLITHDLGVVRRFADRVAVM--RQGEIVE 237
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-207 |
1.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD-------------GADQQMGFVFQ--DSVLLPw 89
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikPVRKKVGVVFQfpESQLFE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLS-EFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALT 168
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1472203387 169 RDhlneELLKIWQ---KTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK13643 180 RI----EMMQLFEsihQSGQTVVLVTHLMDDVADYADYVYLL 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-207 |
1.22e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.99 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD-------------GADQQMGFVFQ--DSVLLP 88
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirPVRKRIGMVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 wKNVRQNAEF-PLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAL 167
Cdd:PRK13646 101 -DTVEREIIFgPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1472203387 168 TRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVM 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-216 |
1.75e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrdGADQQMGFVFQD-S 84
Cdd:COG0488 316 LELEGLSKSY-----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--GETVKIGYFDQHqE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 85 VLLPWKNVRQNaefplvIQKKQTEENEKKLDELLELAGLSE---FKTAlpRELSGGMKQRVSIVRALSYDAPLLLMDEPF 161
Cdd:COG0488 389 ELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSGddaFKPV--GVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 162 GALDALTRDHLnEELLKIWqktKKTVIFVTHSIEeatFLS---DRVLVMsaRPGRVKE 216
Cdd:COG0488 461 NHLDIETLEAL-EEALDDF---PGTVLLVSHDRY---FLDrvaTRILEF--EDGGVRE 509
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-207 |
3.43e-21 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 90.54 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI-------------EYRDG-ADQQMgfVFQDSV--LLP 88
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdllgmkddEWRAVrSDIQM--IFQDPLasLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 WKNVRQNAEFPLVI--QKKQTEENEKKLDELLELAGL-SEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:PRK15079 114 RMTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1472203387 166 -ALTRDHLNeeLLKIWQKTKK-TVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK15079 194 vSIQAQVVN--LLQQLQREMGlSLIFIAHDLAVVKHISDRVLVM 235
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
7-165 |
4.74e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.16 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYsnllKEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD-----------Q 75
Cdd:COG1137 5 EAENLVKSY----GKRTV-VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL-DGEDithlpmhkrarL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQD-SVLlpWK-NVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAP 153
Cdd:COG1137 79 GIGYLPQEaSIF--RKlTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170
....*....|..
gi 1472203387 154 LLLMDEPFGALD 165
Cdd:COG1137 157 FILLDEPFAGVD 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-214 |
5.04e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.40 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDG------------- 72
Cdd:TIGR03269 280 IKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGdewvdmtkpgpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 73 ---ADQQMGFVFQDSVLLPWKNVRQN------AEFP-------LVIQKKQTEENEKKLDELLElaglsefktALPRELSG 136
Cdd:TIGR03269 360 rgrAKRYIGILHQEYDLYPHRTVLDNlteaigLELPdelarmkAVITLKMVGFDEEKAEEILD---------KYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 137 GMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALM--RDGKI 506
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
12-225 |
1.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 88.23 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 12 NKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVF 81
Cdd:PRK13642 9 NLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELltaenvwnlrRKIGMVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 82 QD-SVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:PRK13642 88 QNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDES 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 161 FGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFlSDRVLVM-------SARPGRV----KEMVEIDLPRP 225
Cdd:PRK13642 168 TSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMkageiikEAAPSELfatsEDMVEIGLDVP 242
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-192 |
1.06e-20 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 90.38 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 2 SEYSVELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGtiEYRDGADQQMGFVF 81
Cdd:TIGR03719 1 AQYIYTMNRVSKVVPP----KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--EARPQPGIKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 82 QDSVLLPWKNVRQNAEFPL-VIQKKQTEENE-------------------KKLDELLELAGLSEFKTALPR--------- 132
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVaEIKDALDRFNEisakyaepdadfdklaaeqAELQEIIDAADAWDLDSQLEIamdalrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 133 ------ELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELlkiwQKTKKTVIFVTH 192
Cdd:TIGR03719 155 wdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTH 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-172 |
1.17e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 86.26 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 23 TVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADQQMGFVFQDS------------VLLPWK 90
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilylghlpglkpELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 91 NVRQNAEFplviqkKQTEENEkkLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALD----- 165
Cdd:TIGR01189 93 NLHFWAAI------HGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDkagva 164
|
170
....*....|
gi 1472203387 166 ---ALTRDHL 172
Cdd:TIGR01189 165 llaGLLRAHL 174
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-206 |
1.85e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 88.22 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVY-------------SNLLK---EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY 69
Cdd:COG4586 2 IEVENLSKTYrvyekepglkgalKGLFRreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 70 rdgadqqMGFVfqdsvllPWKNVRQNA-EFPLVI-QKKQ---------------------TEENEKKLDELLELAGLSEF 126
Cdd:COG4586 82 -------LGYV-------PFKRRKEFArRIGVVFgQRSQlwwdlpaidsfrllkaiyripDAEYKKRLDELVELLDLGEL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 127 KTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLV 206
Cdd:COG4586 148 LDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
26-216 |
2.77e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.78 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGN--LDKPTSGTIEYRDGAdqqmgfVFQDSVLLpwKNVRQNAEFPLVIq 103
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQ------FGREASLI--DAIGRKGDFKDAV- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 104 kkqteenekkldELLELAGLSE--FKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEpFGA-LDALTRDHLNEELLKIW 180
Cdd:COG2401 117 ------------ELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCShLDRQTAKRVARNLQKLA 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 1472203387 181 QKTKKTVIFVTHSIEEATFLSDRVLVMSARPGRVKE 216
Cdd:COG2401 184 RRAGITLVVATHHYDVIDDLQPDLLIFVGYGGVPEE 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-216 |
4.47e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 88.72 E-value: 4.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------QQMGFVFQDSVLLpwkN--VR 93
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI-LIDGQDirdvtqaslrAAIGIVPQDTVLF---NdtIA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNaefplvIQKKQTEENEKKLDELLELAGLSEFKTALP---------R--ELSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:COG5265 450 YN------IAYGRPDASEEEVEAAARAAQIHDFIESLPdgydtrvgeRglKLSGGEKQRVAIARTLLKNPPILIFDEATS 523
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 163 ALDALTRDHLNEELLKIWQktKKTVIFVTH---SIEEAtflsDRVLVMSArpGRVKE 216
Cdd:COG5265 524 ALDSRTERAIQAALREVAR--GRTTLVIAHrlsTIVDA----DEILVLEA--GRIVE 572
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
26-217 |
4.62e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.63 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLPwKNVRQN 95
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPlvqydhhylhRQVALVGQEPVLFS-GSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 AEFPLviqkKQTEENEkkLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:TIGR00958 575 IAYGL----TDTPDEE--IMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 165 DALTrdhlnEELLKIWQKTK-KTVIFVTH---SIEEAtflsDRVLVMsaRPGRVKEM 217
Cdd:TIGR00958 649 DAEC-----EQLLQESRSRAsRTVLLIAHrlsTVERA----DQILVL--KKGSVVEM 694
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-216 |
5.77e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 5.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKST----LLRIIgnldkPTSGTIEYRDGADQQ------------MGFVFQD--SV 85
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNlnrrqllpvrhrIQVVFQDpnSS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 86 LLPWKNVRQNAEFPLVIQKKQ--TEENEKKLDELLELAGLS-EFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 163 ALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKE 216
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL--RQGEVVE 506
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-214 |
7.38e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.94 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 3 EYSVELKGLNKVYsnllKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI---------EYRDGA 73
Cdd:PRK13647 2 DNIIEVEDLHFRY----KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkvmgrevnaENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 74 DQQMGFVFQD--------SVllpWKNVrqnaEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIV 145
Cdd:PRK13647 78 RSKVGLVFQDpddqvfssTV---WDDV----AFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 146 RALSYDAPLLLMDEPFGALDALTRDHLNeELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLM-EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKE--GRV 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-232 |
1.08e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 85.14 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 19 LKEDTVALKDINLQIRPGEFISIIGPSGCGKStlLRIIGNLD------KPTSGTIEYrDGADQ--------QMGFVFQD- 83
Cdd:PRK10418 12 LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLL-DGKPVapcalrgrKIATIMQNp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 84 -SVLLPWKNVRQNAEFPLVIQKKQTeeNEKKLDELLELAGLSEFKTAL---PRELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:PRK10418 89 rSAFNPLHTMHTHARETCLALGKPA--DDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 160 PFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEM--VEIDLPRPRGEATRN 232
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSH--GRIVEQgdVETLFNAPKHAVTRS 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-230 |
1.35e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.58 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNL----DKPTSGTIEYRDGAD----------QQMGFVFQDSVLL 87
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielyPEARVSGEVYLDGQDifkmdvielrRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 88 PWKNVRQNAEFPLVIQK--KQTEENEKKLDELLELAGL-SEFKTAL---PRELSGGMKQRVSIVRALSYDAPLLLMDEPF 161
Cdd:PRK14247 95 PNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 162 GALDALTRDHLNEELLKIwqKTKKTVIFVTHSIEEATFLSDRVLVMS----ARPGRVKEMveidLPRPRGEAT 230
Cdd:PRK14247 175 ANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYkgqiVEWGPTREV----FTNPRHELT 241
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-212 |
1.36e-19 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 84.38 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 33 IRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEyrdgadqqmgfVFQDSVllpwknvrqnAEFPLVIQKKQTEENEK 112
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIE-----------IELDTV----------SYKPQYIKADYEGTVRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 113 KLDELLELAG-LSEFKTAL--P-----------RELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLK 178
Cdd:cd03237 81 LLSSITKDFYtHPYFKTEIakPlqieqildrevPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190
....*....|....*....|....*....|....
gi 1472203387 179 IWQKTKKTVIFVTHSIEEATFLSDRVLVMSARPG 212
Cdd:cd03237 161 FAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-214 |
1.67e-19 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 84.06 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGA----------DQ 75
Cdd:cd03248 12 VKFQNVTFAYPT--RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-LLDGKpisqyehkylHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 QMGFVFQDSVLLPwKNVRQNAEFPLviQKKQTEenekKLDELLELAGLSEFKTALPRE-----------LSGGMKQRVSI 144
Cdd:cd03248 89 KVSLVGQEPVLFA-RSLQDNIAYGL--QSCSFE----CVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 145 VRALSYDAPLLLMDEPFGALDALTRdHLNEELLKIWQkTKKTVIFVTH---SIEEAtflsDRVLVMSArpGRV 214
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESE-QQVQQALYDWP-ERRTVLVIAHrlsTVERA----DQILVLDG--GRI 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
23-207 |
1.70e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 23 TVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR----------DGADQQMGFVFQD-SVLLPWKN 91
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklQGIRKLVGIVFQNpETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDH 171
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 1472203387 172 LNEELLKIWQKtKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:PRK13644 175 VLERIKKLHEK-GKTIVYITHNLEELH-DADRIIVM 208
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-195 |
2.08e-19 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 83.53 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLL-RIIGNLDKpTSGTIEYRDGADQQMGFVFQDS---------VLLPW-- 89
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSrnrysvayaAQKPWll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 -KNVRQNAEF--PLVIQKKQTEENEKKLDELLELAGLSEFKTALPR--ELSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:cd03290 92 nATVEENITFgsPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|..
gi 1472203387 165 DALTRDHLNEE-LLKIWQKTKKTVIFVTHSIE 195
Cdd:cd03290 172 DIHLSDHLMQEgILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-200 |
2.69e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVaLKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGaDQQMGFVFQDSVLLPWKN-------VR 93
Cdd:PRK13539 14 GRVL-FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-DIDDPDVAEACHYLGHRNamkpaltVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNAEFPLVIQKkqteENEKKLDELLELAGLSEFkTALP-RELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTrDHL 172
Cdd:PRK13539 92 ENLEFWAAFLG----GEELDIAAALEAVGLAPL-AHLPfGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA-VAL 165
|
170 180 190
....*....|....*....|....*....|.
gi 1472203387 173 NEELLKIWQKTKKTVIFVTHS---IEEATFL 200
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATHIplgLPGAREL 196
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
12-207 |
3.37e-19 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 84.14 E-value: 3.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 12 NKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrdgaDQQMGFVFQDSVLLPwKN 91
Cdd:cd03291 39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH----SGRISFSSQFSWIMP-GT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNAEFPL---------VIQKKQTEENEKKLDE----LLELAGLSefktalpreLSGGMKQRVSIVRALSYDAPLLLMD 158
Cdd:cd03291 114 IKENIIFGVsydeyryksVVKACQLEEDITKFPEkdntVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1472203387 159 EPFGALDALTRDHLNEE-LLKIwqKTKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:cd03291 185 SPFGYLDVFTEKEIFEScVCKL--MANKTRILVTSKMEHLK-KADKILIL 231
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
25-207 |
3.59e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.29 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLDKPTSGTI--EYRDGAD-----------QQMGFVFQ-DSVLLPW 89
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGQTIvgDYAIPANlkkikevkrlrKEIGLVFQfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLVIQKKQTEENEKKLDELLELAGL-SEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALT 168
Cdd:PRK13645 106 ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 1472203387 169 RDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK13645 186 EEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-166 |
5.84e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.77 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 16 SNL--LKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADQQMGFVFQ----------- 82
Cdd:PRK13538 5 RNLacERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHqdllylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 83 -DSVLLPWKNVRqnaeFPLVIQKKQTEEnekKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPF 161
Cdd:PRK13538 85 iKTELTALENLR----FYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
....*
gi 1472203387 162 GALDA 166
Cdd:PRK13538 158 TAIDK 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-217 |
6.16e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 6.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 17 NLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR--------DGADQ----QMGFVFQD- 83
Cdd:PRK10261 331 NRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNgqridtlsPGKLQalrrDIQFIFQDp 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 84 -SVLLPWKNVRQNAEFPLVIQK-KQTEENEKKLDELLELAGL-SEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:PRK10261 411 yASLDPRQTVGDSIMEPLRVHGlLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 161 FGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEM 217
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYL--GQIVEI 545
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
25-207 |
7.18e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.88 E-value: 7.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGA---------DQQMGFVFQDSvllpwKN---- 91
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAitddnfeklRKHIGIVFQNP-----DNqfvg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 --VRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTR 169
Cdd:PRK13648 99 siVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1472203387 170 DHLNEELLKIWQKTKKTVIFVTHSIEEATFlSDRVLVM 207
Cdd:PRK13648 179 QNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVM 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-214 |
1.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 82.87 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGA-------------DQQMGFVFQ--DSVLLPW 89
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqiRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLVIQKKQtEENEKKLDELLELAGLSE-FKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALT 168
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQ-EEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1472203387 169 RdhlnEELLKIWQKTKK---TVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:PRK13649 181 R----KELMTLFKKLHQsgmTIVLVTHLMDDVANYADFVYVLEK--GKL 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
25-214 |
1.11e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.37 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNL---DKPTSGTIEY------RDG--------ADQQMGFVFQDSVLL 87
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELlgrtvqREGrlardirkSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 88 PWKNVRQN--------AEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:PRK09984 99 NRLSVLENvligalgsTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 160 PFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL--RQGHV 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
7-214 |
1.68e-18 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 81.18 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGADQQ---------- 76
Cdd:COG0410 5 EVENLHAGYG-----GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRF-DGEDITglpphriarl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 -MGFVFQDSVLLPWKNVRQNaefpLVI---QKKQTEENEKKLDELLEL-AGLSEFKTALPRELSGGMKQRVSIVRALSYD 151
Cdd:COG0410 79 gIGYVPEGRRIFPSLTVEEN----LLLgayARRDRAEVRADLERVYELfPRLKERRRQRAGTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 152 APLLLMDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRV 214
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLER--GRI 214
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-208 |
2.10e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.59 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD---GAD------- 74
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyiGDKknnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 ---------------QQMGFVFQDSVLLPWKN-VRQNAEFPLVIQKKQTEENEKKLDELLELAGLSE-FKTALPRELSGG 137
Cdd:PRK13631 101 tnpyskkiknfkelrRRVSMVFQFPEYQLFKDtIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 138 MKQRVSIVRALSYDAPLLLMDEPFGALDAlTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDP-KGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-214 |
2.13e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.56 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNLlkedtVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGA--------DQQM 77
Cdd:PRK15439 12 LCARSISKQYSGV-----EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPcarltpakAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 G--FVFQDSVLLPWKNVRQNAEFPLviqkKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLL 155
Cdd:PRK15439 87 GiyLVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 156 LMDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVM--RDGTI 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-216 |
2.55e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 83.70 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLD--KPTSGTIEYRDGADQQMGFV--- 80
Cdd:TIGR03269 1 IEVKNLTKKF-----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHVALCEKCGYVerp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 81 -------------FQDSVLLPW---KNVRQNAEFPLVIQKKQT---EENEKKLD---------------------ELLEL 120
Cdd:TIGR03269 76 skvgepcpvcggtLEPEEVDFWnlsDKLRRRIRKRIAIMLQRTfalYGDDTVLDnvlealeeigyegkeavgravDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 121 AGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFL 200
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250
....*....|....*.
gi 1472203387 201 SDRVLVMSArpGRVKE 216
Cdd:TIGR03269 236 SDKAIWLEN--GEIKE 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-192 |
2.79e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 83.24 E-value: 2.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGAdqQMGFV 80
Cdd:PRK11819 2 MAQYIYTMNRVSKVVPP----KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGI--KVGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 81 FQDSVLLPWKNVRQNAEFPL-VIQKKQTEENE-------------------KKLDELLELAGLSEFKTALPR-------- 132
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEEGVaEVKAALDRFNEiyaayaepdadfdalaaeqGELQEIIDAADAWDLDSQLEIamdalrcp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 133 -------ELSGGMKQRVSIVRALsYDAP-LLLMDEPFGALDALTRDHLNEELlkiwQKTKKTVIFVTH 192
Cdd:PRK11819 156 pwdakvtKLSGGERRRVALCRLL-LEKPdMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTH 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
26-222 |
2.91e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTS-----GTIEYRDGA-----------DQQMGFVFQDSVLLPw 89
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNiyerrvnlnrlRRQVSMVHPKPNLFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEF--PLVIQKKQTE-----ENEKKLDELLELAGLSEFKTALprELSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:PRK14258 102 MSVYDNVAYgvKIVGWRPKLEiddivESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIARALAVKPKVLLMDEPCF 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 163 ALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSARPGRVKEMVEIDL 222
Cdd:PRK14258 180 GLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQLVEFGL 239
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-234 |
3.84e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 3.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSNLLkedtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADQ----- 75
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLL-----AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpgh 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 76 ---QMGFV--FQDSVLLPWKNVRQNAefpLVIQKKQTEEN---------------EKKLD---ELLELAGLSEFKTALPR 132
Cdd:PRK11300 76 qiaRMGVVrtFQHVRLFREMTVIENL---LVAQHQQLKTGlfsgllktpafrraeSEALDraaTWLERVGLLEHANRQAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 133 ELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS-ARP 211
Cdd:PRK11300 153 NLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNqGTP 232
|
250 260
....*....|....*....|...
gi 1472203387 212 grvkemveidLPRPRGEATRNDP 234
Cdd:PRK11300 233 ----------LANGTPEEIRNNP 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-207 |
6.04e-18 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 82.65 E-value: 6.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 15 YSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrdgaDQQMGFVFQDSVLLPwKNVRQ 94
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH----SGRISFSPQTSWIMP-GTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 95 NAEFPL---------VIQKKQTEENEKKLDEllelaglsEFKTALPR---ELSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:TIGR01271 506 NIIFGLsydeyrytsVIKACQLEEDIALFPE--------KDKTVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1472203387 163 ALDALTRDHLNEE-LLKIWqkTKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:TIGR01271 578 HLDVVTEKEIFEScLCKLM--SNKTRILVTSKLEHLK-KADKILLL 620
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-207 |
6.69e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 80.61 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSNLLKEdtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKP---------------TSG 65
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKP---ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskitvdgitlTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 66 TI-EYRDgadqQMGFVFQ--DSVLLPwKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRV 142
Cdd:PRK13640 78 TVwDIRE----KVGIVFQnpDNQFVG-ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 143 SIVRALSYDAPLLLMDEPFGALDALTRdhlnEELLKIWQKTKK----TVIFVTHSIEEATfLSDRVLVM 207
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKLKKknnlTVISITHDIDEAN-MADQVLVL 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-208 |
1.20e-17 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.98 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNLLkedtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD------QQMGFV 80
Cdd:TIGR03740 2 ETKNLSKRFGKQT-----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEI-IFDGHPwtrkdlHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 81 FQDSVLLPWKNVRQNaefpLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:TIGR03740 76 IESPPLYENLTAREN----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1472203387 161 FGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:TIGR03740 152 TNGLDPIGIQEL-RELIRSFPEQGITVILSSHILSEVQQLADHIGIIS 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-214 |
1.68e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.28 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGA-----------DQQMGFVFQD-SVLLP 88
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalRQQVATVFQDpEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 WKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALT 168
Cdd:PRK13638 92 YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1472203387 169 RDHLNEELLKIWQKTKKTVIfVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:PRK13638 172 RTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVL--RQGQI 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-207 |
1.92e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 80.91 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD---------------GADQQMGFVFQDSVL 86
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDipltklqldswrsrlAVVSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 87 lpwKNV---RQNAefplviqkkqTEEnekKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDA 152
Cdd:PRK10789 407 ---NNIalgRPDA----------TQQ---EIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 153 PLLLMDEPFGALDALTRDHLNEElLKIWQKtKKTVIFVTHSIEEATfLSDRVLVM 207
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHN-LRQWGE-GRTVIISAHRLSALT-EASEILVM 522
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-207 |
2.69e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 2.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKS----TLLRIIGN-----------LDKPTSGTIEYRDGADQQM--------GFVF 81
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQagglvqcdkmlLRRRSRQVIELSEQSAAQMrhvrgadmAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 82 QDSV--LLPWKNV-RQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTAL---PRELSGGMKQRVSIVRALSYDAPLL 155
Cdd:PRK10261 111 QEPMtsLNPVFTVgEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILsryPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 156 LMDEPFGALDALTRDHLnEELLKIWQKTKKT-VIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK10261 191 IADEPTTALDVTIQAQI-LQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVM 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-224 |
2.97e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSNLlkedtVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI----------EYR 70
Cdd:PRK09700 1 MATPYISMAGIGKSFGPV-----HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynklDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 71 DGADQQMGFVFQDSVLLPWKNVRQNAEFPLVIQKK-------QTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVS 143
Cdd:PRK09700 76 LAAQLGIGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 144 IVRALSYDAPLLLMDEPFGALDALTRDHLNeELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM----SARPGRVKEMVE 219
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMkdgsSVCSGMVSDVSN 234
|
....*
gi 1472203387 220 IDLPR 224
Cdd:PRK09700 235 DDIVR 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-222 |
3.11e-17 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.49 E-value: 3.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKG--LNKVYSNLlkedTVAlKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGadQQMG 78
Cdd:PRK10253 1 MTESVARLRGeqLTLGYGKY----TVA-ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDG--EHIQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 79 FVFQDSVLLPWKNVRQNAEFP--LVIQK--------------KQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRV 142
Cdd:PRK10253 73 HYASKEVARRIGLLAQNATTPgdITVQElvargryphqplftRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 143 SIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRV------KE 216
Cdd:PRK10253 153 WIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIvaqgapKE 230
|
....*.
gi 1472203387 217 MVEIDL 222
Cdd:PRK10253 231 IVTAEL 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-214 |
4.47e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 4.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLL-----RIIGNLDKPTSGTIEYRDGADQQM----GFVFQDSVLLPWKNVRQN- 95
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKGSGSVLLNGMPIDAKEMraisAYVQQDDLFIPTLTVREHl 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 ---AEFPLviqKKQTEENEKKL--DELLELAGLS---EFKTALP---RELSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:TIGR00955 121 mfqAHLRM---PRRVTKKEKRErvDEVLQALGLRkcaNTRIGVPgrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 165 DALTRDHLNEELLKIWQKtKKTVIFVTHS-IEEATFLSDRVLVMSArpGRV 214
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQK-GKTIICTIHQpSSELFELFDKIILMAE--GRV 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-208 |
6.62e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 6.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 19 LKEDTVaLKDINLQIRPGEFISIIGPSGCGKSTLL-----RIIGNldkPTSGTIEYRDG--ADQQM---GFVFQDSVLLP 88
Cdd:PLN03211 78 IQERTI-LNGVTGMASPGEILAVLGPSGSGKSTLLnalagRIQGN---NFTGTILANNRkpTKQILkrtGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 WKNVRQNAEFPLVIQKKQTEENEKKL---DELLELAGLSEFKTALP-----RELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:PLN03211 154 HLTVRETLVFCSLLRLPKSLTKQEKIlvaESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1472203387 161 FGALDALTRDHLNEELLKIWQKtKKTVIFVTHSIEEATF-LSDRVLVMS 208
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQPSSRVYqMFDSVLVLS 281
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-204 |
7.92e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.39 E-value: 7.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 18 LLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRD-----GAD----------QQMGFVFQ 82
Cdd:PRK14246 18 LYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfGKDifqidaiklrKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 83 DSVLLPWKNVRQNAEFPLVIQK-KQTEENEKKLDELLELAGLseFKTALPR------ELSGGMKQRVSIVRALSYDAPLL 155
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1472203387 156 LMDEPFGALDALTRDHLNEELLKIwqKTKKTVIFVTHSIEEATFLSDRV 204
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYV 222
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-214 |
8.16e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.40 E-value: 8.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDG--ADQQmgfvFQD 83
Cdd:NF033858 2 ARLEGVSHRYG-----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGdmADAR----HRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 84 SV--------------LLPWKNVRQNAEF--PLVIQKKQteENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRA 147
Cdd:NF033858 73 AVcpriaympqglgknLYPTLSVFENLDFfgRLFGQDAA--ERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 148 LSYDAPLLLMDEPFGALDALTR-------DHLNEEllkiwqKTKKTVIFVTHSIEEAT-FlsDRVLVMSArpGRV 214
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRrqfweliDRIRAE------RPGMSVLVATAYMEEAErF--DWLVAMDA--GRV 215
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-208 |
1.59e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.50 E-value: 1.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADqqMGFVFQ----------DSVLLPWK 90
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGED--LLFLPQrpylplgtlrEQLIYPWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 91 nvrqnaefplviqkkqteenekkldellelaglsefktalpRELSGGMKQRVSIVRALsYDAP-LLLMDEPFGALDALTR 169
Cdd:cd03223 90 -----------------------------------------DVLSGGEQQRLAFARLL-LHKPkFVFLDEATSALDEESE 127
|
170 180 190
....*....|....*....|....*....|....*....
gi 1472203387 170 DHlneeLLKIWQKTKKTVIFVTHSIEEATFlSDRVLVMS 208
Cdd:cd03223 128 DR----LYQLLKELGITVISVGHRPSLWKF-HDRVLDLD 161
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-217 |
1.72e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 78.45 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-IIGNLDK-----PTSGTIEYRdgadQQMGFVFQDSVllpwknvR 93
Cdd:TIGR00957 648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKveghvHMKGSVAYV----PQQAWIQNDSL-------R 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNAEF--PLviqkkqteeNEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:TIGR00957 717 ENILFgkAL---------NEKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 161 FGALDALTRDHLNEELLKIWQKTK-KTVIFVTHSIeeaTFL--SDRVLVMSArpGRVKEM 217
Cdd:TIGR00957 788 LSAVDAHVGKHIFEHVIGPEGVLKnKTRILVTHGI---SYLpqVDVIIVMSG--GKISEM 842
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-216 |
3.09e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 76.69 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKS-TLLRIIGNLDKP--TSGTIEYrDGAD--------------QQMGFVFQDS 84
Cdd:PRK09473 28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATF-NGREilnlpekelnklraEQISMIFQDP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 85 V--LLPWKNVRQNAEFPLVIQKKQT-----EENEKKLDELlelaGLSEFK---TALPRELSGGMKQRVSIVRALSYDAPL 154
Cdd:PRK09473 107 MtsLNPYMRVGEQLMEVLMLHKGMSkaeafEESVRMLDAV----KMPEARkrmKMYPHEFSGGMRQRVMIAMALLCRPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 155 LLMDEPFGALD----ALTRDHLNEelLKiwQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:PRK09473 183 LIADEPTTALDvtvqAQIMTLLNE--LK--REFNTAIIMITHDLGVVAGICDKVLVMYA--GRTME 242
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-216 |
3.10e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 76.70 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKS-TLLRIIGNLDKP---TSGTIEY--RD-------------GADQQMgfVFQDSV 85
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFngQDlqrisekerrnlvGAEVAM--IFQDPM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 86 --LLPWKNV-RQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTAL---PRELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:PRK11022 100 tsLNPCYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 160 PFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKE 216
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYA--GQVVE 234
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
26-208 |
1.04e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDG----------ADQQMGFVFQDSVLLPWKNVRQN 95
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllplharARRGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 AEFPLVIQKKQTEENEK-KLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRdhlnE 174
Cdd:PRK10895 99 LMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV----I 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 1472203387 175 ELLKIWQKTKKT---VIFVTHSIEEATFLSDRVLVMS 208
Cdd:PRK10895 175 DIKRIIEHLRDSglgVLITDHNVRETLAVCERAYIVS 211
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-210 |
1.83e-15 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 75.31 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGAdqQMGFVFQDSv 85
Cdd:PRK15064 320 LEVENLTKGF-----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA--NIGYYAQDH- 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 86 llpwknvrqNAEFPLVI-------QKKQTEENEKKLDELLE--LAGLSEFKTAlPRELSGGMKQRVSIVRALSYDAPLLL 156
Cdd:PRK15064 392 ---------AYDFENDLtlfdwmsQWRQEGDDEQAVRGTLGrlLFSQDDIKKS-VKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 157 MDEPFGALDALTRDHLNEELlkiwQKTKKTVIFVTHSIEEATFLSDRVLVMSAR 210
Cdd:PRK15064 462 MDEPTNHMDMESIESLNMAL----EKYEGTLIFVSHDREFVSSLATRIIEITPD 511
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
5-216 |
2.54e-15 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 72.06 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 5 SVELKGLNKVYSNLLKEdtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------- 74
Cdd:cd03369 6 EIEVENLSVRYAPDLPP---VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDistipledlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQMGFVFQDSVLLPwKNVRQNaefpLVIQKKQTEEnekKLDELLELAGLSEfktalprELSGGMKQRVSIVRALSYDAPL 154
Cdd:cd03369 82 SSLTIIPQDPTLFS-GTIRSN----LDPFDEYSDE---EIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 155 LLMDEPFGALDALTrDHLNEELLKIwQKTKKTVIFVTHSIEE-ATFlsDRVLVMSArpGRVKE 216
Cdd:cd03369 147 LVLDEATASIDYAT-DALIQKTIRE-EFTNSTILTIAHRLRTiIDY--DKILVMDA--GEVKE 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-228 |
2.70e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.56 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 7 ELKGLNKVYSNLLkedtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY----------RDGADQQ 76
Cdd:PRK11288 6 SFDGIGKTFPGVK-----ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqemrfastTAALAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 77 MGFVFQDSVLLPWKNVRQN-------AEFPLVIQKKQTEENEKKLDELlelaGLsEFKTALP-RELSGGMKQRVSIVRAL 148
Cdd:PRK11288 81 VAIIYQELHLVPEMTVAENlylgqlpHKGGIVNRRLLNYEAREQLEHL----GV-DIDPDTPlKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 149 SYDAPLLLMDEPFGALDAltRDhlNEELLKIWQKTK---KTVIFVTHSIEEATFLSDRVLVMsaRPGR------------ 213
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSA--RE--IEQLFRVIRELRaegRVILYVSHRMEEIFALCDAITVF--KDGRyvatfddmaqvd 229
|
250 260
....*....|....*....|....*.
gi 1472203387 214 ----VKEMV--EID-----LPRPRGE 228
Cdd:PRK11288 230 rdqlVQAMVgrEIGdiygyRPRPLGE 255
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-230 |
3.13e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIE----------YRDGADQQMGFV----FQDSVLLPwK 90
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRldgkpvrirsPRDAIRAGIAYVpedrKGEGLVLD-L 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 91 NVRQN---------AEFPLVIQKKQTEENEKKLDELlelaglsEFKTALP----RELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:COG1129 346 SIRENitlasldrlSRGGLLDRRRERALAEEYIKRL-------RIKTPSPeqpvGNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 158 DEPF-----GA-------LDALTRDhlneellkiwqktKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMVeidlprP 225
Cdd:COG1129 419 DEPTrgidvGAkaeiyrlIRELAAE-------------GKAVIVISSELPELLGLSDRILVMRE--GRIVGEL------D 477
|
....*
gi 1472203387 226 RGEAT 230
Cdd:COG1129 478 REEAT 482
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-213 |
6.47e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 73.69 E-value: 6.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 32 QIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSG------TIEYRD---GADQQMgfvfqdSVLLPWKNVRQNAEFPLVi 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGevdpelKISYKPqyiKPDYDG------TVEDLLRSITDDLGSSYY- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 103 qkkQTEENEK-KLDELLElaglSEFKtalprELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQ 181
Cdd:PRK13409 434 ---KSEIIKPlQLERLLD----KNVK-----DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAE 501
|
170 180 190
....*....|....*....|....*....|..
gi 1472203387 182 KTKKTVIFVTHSIEEATFLSDRVLVMSARPGR 213
Cdd:PRK13409 502 EREATALVVDHDIYMIDYISDRLMVFEGEPGK 533
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-212 |
6.77e-15 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 70.29 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEF-----ISIIGPSGCGKSTLLRIIGNLDKPTSGTIEyrdgadqqmgfvfqdsvllpWKNVRqnaefpl 100
Cdd:cd03222 10 YGVFFLLVELGVVkegevIGIVGPNGTGKTTAVKILAGQLIPNGDNDE--------------------WDGIT------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 101 VIQKKQteenekKLDellelaglsefktalpreLSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIW 180
Cdd:cd03222 63 PVYKPQ------YID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180 190
....*....|....*....|....*....|..
gi 1472203387 181 QKTKKTVIFVTHSIEEATFLSDRVLVMSARPG 212
Cdd:cd03222 119 EEGKKTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
36-166 |
8.08e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.60 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 36 GEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADQQMGFVFQDSVLlpWK----------NVRQNAEFPLVIQkk 105
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL--YLghapgikttlSVLENLRFWHADH-- 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 106 QTEENEKKLDEllelAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDA 166
Cdd:cd03231 102 SDEQVEEALAR----VGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-244 |
8.25e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 73.28 E-value: 8.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 32 QIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEyrdgadqqmgfvfqDSVLLPWKNVRQNAEFPLVIQKKQTEENE 111
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--------------EDLKISYKPQYISPDYDGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 112 KKLD------ELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKK 185
Cdd:COG1245 428 DDFGssyyktEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGK 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 186 TVIFVTHSIEEATFLSDRVLVMSARPGRvkemveidlprpRGEATRNDPKFTEYNKYLR 244
Cdd:COG1245 508 TAMVVDHDIYLIDYISDRLMVFEGEPGV------------HGHASGPMDMREGMNRFLK 554
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
40-248 |
2.00e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.90 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 40 SIIGPSGCGKSTLLRIIGNLDKPTSG-------------TIEYRDGAD--QQMGFVFQDSVLLPWK---NVRQNAE-FPL 100
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrsIFNYRDVLEfrRRVGMLFQRPNPFPMSimdNVLAGVRaHKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 101 VIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIW 180
Cdd:PRK14271 131 VPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 181 QKTkkTVIFVTHSIEEATFLSDRVLVMSarPGRVKEmveidlpRPRGEATRNDPKFTEYNKYLRGIIG 248
Cdd:PRK14271 211 DRL--TVIIVTHNLAQAARISDRAALFF--DGRLVE-------EGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
11-168 |
2.06e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 11 LNKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY--------RDGADQQMGFVFQ 82
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFerqsikkdLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 83 DSVLLPWKNVRQNAEFPLVIQKKQTEENEkkLDELLELAGLSEFKTALpreLSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:PRK13540 82 RSGINPYLTLRENCLYDIHFSPGAVGITE--LCRLFSLEHLIDYPCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
....*.
gi 1472203387 163 ALDALT 168
Cdd:PRK13540 157 ALDELS 162
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
26-165 |
2.21e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGAdqQMGFVFQDSVLlpwknvrqNAEFPLVIQK- 104
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKL--RIGYVPQKLYL--------DTTLPLTVNRf 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 105 KQTEENEKKLDEL--LELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:PRK09544 90 LRLRPGTKKEDILpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-216 |
2.92e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 71.75 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 29 INLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI-------------EYRdgadQQMGFVFQDSVLlpwknvrqn 95
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEIlldgqpvtadnreAYR----QLFSAVFSDFHL--------- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 aeFPLVIQkKQTEENEKKLDELLELAGLSEfKTAL------PRELSGGMKQRVSIVRALSYDAPLLLMDE-------PFg 162
Cdd:COG4615 418 --FDRLLG-LDGEADPARARELLERLELDH-KVSVedgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdpEF- 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 163 aldaltRDHLNEELLKIWQKTKKTVIFVTHsiEEATF-LSDRVLVMSArpGRVKE 216
Cdd:COG4615 493 ------RRVFYTELLPELKARGKTVIAISH--DDRYFdLADRVLKMDY--GKLVE 537
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
20-235 |
5.63e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.21 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGAD----------QQMGFVFQDSVLLPw 89
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlkdinlkwwrSKIGVVSQDPLLFS- 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEFPLVIQKK-------------QTEENEKKL--------------------DELLELAG-------------- 122
Cdd:PTZ00265 474 NSIKNNIKYSLYSLKDlealsnyynedgnDSQENKNKRnscrakcagdlndmsnttdsNELIEMRKnyqtikdsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 123 ----LSEFKTALP-----------RELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTV 187
Cdd:PTZ00265 554 kkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1472203387 188 IFVTHSIEEATFlSDRVLVMSARPGRVKEMVEIDLPRPRGEATRNDPK 235
Cdd:PTZ00265 634 IIIAHRLSTIRY-ANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNK 680
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-165 |
8.01e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 68.34 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY------RDGADQQMGFVFQDSVLLPWKNVR 93
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdgktatRGDRSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 94 QNAEFPLVIQ---KKQTEENEkkldelLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:PRK13543 101 ENLHFLCGLHgrrAKQMPGSA------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-207 |
9.33e-14 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 70.43 E-value: 9.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSNllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSG--TIEYRD------GADQQM 77
Cdd:TIGR01257 1938 LRLNELTKVYSG---TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdaTVAGKSiltnisDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVFQDSVLLPWKNVRQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLM 157
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1472203387 158 DEPFGALDALTRDHLNEELLKIWQKtKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIM 2143
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-177 |
1.42e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.58 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrdGADQQMGFVFQD-S 84
Cdd:TIGR03719 323 IEAENLTKAF-----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI--GETVKLAYVDQSrD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 85 VLLPWKNVrqnaefplviqkkqTEENEKKLDELL---------ELAGLSEFKTA----LPRELSGGMKQRVSIVRALSYD 151
Cdd:TIGR03719 396 ALDPNKTV--------------WEEISGGLDIIKlgkreipsrAYVGRFNFKGSdqqkKVGQLSGGERNRVHLAKTLKSG 461
|
170 180
....*....|....*....|....*.
gi 1472203387 152 APLLLMDEPFGALDALTRDHLNEELL 177
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALL 487
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
26-214 |
2.64e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeyrdgadqqmgfVFQDSVLLPWKN---VRQNAEFPLvi 102
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI------------LLDAQPLESWSSkafARKVAYLPQ-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 103 QKKQTE------------------------ENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMD 158
Cdd:PRK10575 93 QLPAAEgmtvrelvaigrypwhgalgrfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 159 EPFGALDALtrdHLNEELLKIWQKTKK---TVIFVTHSIEEATFLSDRVLVMsaRPGRV 214
Cdd:PRK10575 173 EPTSALDIA---HQVDVLALVHRLSQErglTVIAVLHDINMAARYCDYLVAL--RGGEM 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-216 |
2.89e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 2.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGADqqmgfvFQDSVLlpwKNVRQNaeFPLV 101
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGHD------LRDYTL---ASLRNQ--VALV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 102 IQK---------------KQTEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLL 155
Cdd:PRK11176 423 SQNvhlfndtianniayaRTEQYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 156 LMDEPFGALDALTRDHLNEELLKIwQKtKKTVIFVTH---SIEEAtflsDRVLVMSArpGRVKE 216
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDEL-QK-NRTSLVIAHrlsTIEKA----DEILVVED--GEIVE 558
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-216 |
1.23e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 28 DINLQIRPGEFISIIGPSGCGKS-TLLRIIGNLDKP----TSGTIEYRDG----ADQQ---------MGFVFQDSV--LL 87
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGEsllhASEQtlrgvrgnkIAMIFQEPMvsLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 88 PWKNV-RQNAEFPLVIQKKQTEENEKKLDELLELAGLSEFKTAL---PRELSGGMKQRVSIVRALSYDAPLLLMDEPFGA 163
Cdd:PRK15134 107 PLHTLeKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIAMALLTRPELLIADEPTTA 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 164 LDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKE 216
Cdd:PRK15134 187 LDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM--QNGRCVE 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-207 |
1.35e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.68 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY----------RDGADQQMGFVFQDSVLLPWKNVRQ 94
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqgkeidfkssKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 95 N---AEFPL----VIQKKQTEENEKKLDEL-LELAglsefktalPRE----LSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:PRK10982 93 NmwlGRYPTkgmfVDQDKMYRDTKAIFDELdIDID---------PRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1472203387 163 ALDALTRDHlneeLLKIWQKTKKT---VIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK10982 164 SLTEKEVNH----LFTIIRKLKERgcgIVYISHKMEEIFQLCDEITIL 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
26-208 |
1.94e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.21 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPT---SGTIEYrDGAD---------QQMGFVFQDSVLLPWKNVR 93
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHY-NGIPykefaekypGEIIYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNAEFPLVIQKkqteenekklDELLelaglsefktalpRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLN 173
Cdd:cd03233 102 ETLDFALRCKG----------NEFV-------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 1472203387 174 EELLKIWQKTKKTVIF-VTHSIEEATFLSDRVLVMS 208
Cdd:cd03233 159 KCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLY 194
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-213 |
2.01e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRII------GNLDkptsGTIeYRDGAD 74
Cdd:PRK13549 1 MMEYLLEMKNITKTFG-----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphGTYE----GEI-IFEGEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 75 QQ-----------MGFVFQDSVLLPWKNVRQN-------AEFPLVIQKKQTEENEKKLDELlelaGLsEFKTALP-RELS 135
Cdd:PRK13549 71 LQasnirdteragIAIIHQELALVKELSVLENiflgneiTPGGIMDYDAMYLRAQKLLAQL----KL-DINPATPvGNLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 136 GGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHlneeLLKIWQKTKK---TVIFVTHSIEEATFLSDRVLVMsaRPG 212
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLTESETAV----LLDIIRDLKAhgiACIYISHKLNEVKAISDTICVI--RDG 219
|
.
gi 1472203387 213 R 213
Cdd:PRK13549 220 R 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-231 |
2.11e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD---------------------QQMGFV-- 80
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL-DGEDitglsprerrrlgvayipedrLGRGLVpd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 81 ----------------FQDSVLLPWKNVRQNAEfplviqkkqteenekkldELLElaglsEF--KTALP----RELSGGM 138
Cdd:COG3845 351 msvaenlilgryrrppFSRGGFLDRKAIRAFAE------------------ELIE-----EFdvRTPGPdtpaRSLSGGN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 139 KQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKiwQKTK-KTVIFVTHSIEEATFLSDRVLVMSArpGRVKEm 217
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE--LRDAgAAVLLISEDLDEILALSDRIAVMYE--GRIVG- 482
|
250
....*....|....
gi 1472203387 218 veidlPRPRGEATR 231
Cdd:COG3845 483 -----EVPAAEATR 491
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-224 |
2.26e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYSnllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNL--DKPTSGTIEY----------RDGA 73
Cdd:TIGR02633 2 LEMKGIVKTFG-----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWsgsplkasniRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 74 DQQMGFVFQDSVLLPWKNVRQNA----EFPLVIQKKQTEENEKKLDELLELAGLSEFKTALP-RELSGGMKQRVSIVRAL 148
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 149 SYDAPLLLMDEPFGaldALTRDHLnEELLKIWQKTKK---TVIFVTHSIEEATFLSDRVLVMsaRPGR---VKEMVEIDL 222
Cdd:TIGR02633 157 NKQARLLILDEPSS---SLTEKET-EILLDIIRDLKAhgvACVYISHKLNEVKAVCDTICVI--RDGQhvaTKDMSTMSE 230
|
..
gi 1472203387 223 PR 224
Cdd:TIGR02633 231 DD 232
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-235 |
2.42e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.84 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEyRDGadqQMGFVFQDSVLLPWKNVRQNAEFPL 100
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-RNG---EVSVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 101 VIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEpfgALDALTRDHLNEELLKIW 180
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE---ALSVGDQTFAQKCLDKIY 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 181 Q--KTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMVEIDLPRPRGEATRNDPK 235
Cdd:PRK13546 188 EfkEQNKTIFFVSHNLGQVRQFCTKIAWIEG--GKLKDYGELDDVLPKYEAFLNDFK 242
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-202 |
2.71e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.90 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 1 MSEYSVELKGLNKVYSNllkeDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADQQMgfV 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRN----GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA--L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 81 FQDSVLLPWKNVRQNAEFPLVIQ--------------KKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVR 146
Cdd:PRK15056 76 QKNLVAYVPQSEEVDWSFPVLVEdvvmmgryghmgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 147 ALSYDAPLLLMDEPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSD 202
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARI-ISLLRELRDEGKTMLVSTHNLGSVTEFCD 210
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
25-217 |
3.74e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 3.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI-------------EYRdgadQQMGFVFQDSVLlpwkn 91
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIlldgkpvtaeqpeDYR----KLFSAVFTDFHL----- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 vrqnaeFPLVIQKKQTEENEKKLDELLELAG------LSEFKTALPReLSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:PRK10522 409 ------FDQLLGPEGKPANPALVEKWLERLKmahkleLEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 166 ALTRDHLNEELLKIWQKTKKTVIFVTHsiEEATFLS-DRVLVMsaRPGRVKEM 217
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISH--DDHYFIHaDRLLEM--RNGQLSEL 530
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-207 |
5.89e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 5.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY----------RDGADQQMGFVFQDSVLLPWKNVRQ 94
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgkevtfngpKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 95 NA----EFPLVIQKKQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPfgaLDALTrD 170
Cdd:PRK10762 99 NIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---TDALT-D 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1472203387 171 HLNEELLKIWQKTKKT---VIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK10762 175 TETESLFRVIRELKSQgrgIVYISHRLKEIFEICDDVTVF 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-165 |
6.84e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 29 INLQIRPGEFISIIGPSGCGKSTLL-RIIGNLdkPTSGTIeyrdgadqqmgfVFQDSVLLPWKNV-----------RQNA 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSI------------QFAGQPLEAWSAAelarhraylsqQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 97 EFPL-VIQ--------KKQTEENEKKLDELLELAGLSEFktaLPR---ELSGGMKQRV-------SIVRALSYDAPLLLM 157
Cdd:PRK03695 81 PFAMpVFQyltlhqpdKTRTEAVASALNEVAEALGLDDK---LGRsvnQLSGGEWQRVrlaavvlQVWPDINPAGQLLLL 157
|
....*...
gi 1472203387 158 DEPFGALD 165
Cdd:PRK03695 158 DEPMNSLD 165
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-215 |
8.53e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 8.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-IIGNLDKpTSGtieyRDGADQQMGFVFQDsvllPW---KNVRQNA 96
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEI-SEG----RVWAERSIAYVPQQ----AWimnATVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 97 EFplviqkkQTEENEKKLDEL-----LElAGLSEFKTALPRE-------LSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:PTZ00243 742 LF-------FDEEDAARLADAvrvsqLE-ADLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 165 DALTRDHLNEELLkIWQKTKKTVIFVTHSIEEATfLSDRVLVMSArpGRVK 215
Cdd:PTZ00243 814 DAHVGERVVEECF-LGALAGKTRVLATHQVHVVP-RADYVVALGD--GRVE 860
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-165 |
9.59e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.94 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLL-RIIGNLdkPTSGTIEYrDGAD----------QQMGFVFQDSVLLPWKNVRQ 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILL-NGRPlsdwsaaelaRHRAYLSQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 95 naefplVIQ-----KKQTEENEKKLDELLELAGLSEFktaLPR---ELSGGMKQRVSIVRAL-------SYDAPLLLMDE 159
Cdd:COG4138 89 ------YLAlhqpaGASSEAVEQLLAQLAEALGLEDK---LSRpltQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLLDE 159
|
....*.
gi 1472203387 160 PFGALD 165
Cdd:COG4138 160 PMNSLD 165
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-214 |
2.30e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGT------------IEYRdgadQQMGFVFQDSVLLPW 89
Cdd:NF033858 278 DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEawlfgqpvdagdIATR----RRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAE-----FPLviqkkQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:NF033858 354 LTVRQNLElharlFHL-----PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGV 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1472203387 165 DALTRDHLNEELLKIWQKTKKTvIFV-THSIEEATfLSDRVLVMSArpGRV 214
Cdd:NF033858 429 DPVARDMFWRLLIELSREDGVT-IFIsTHFMNEAE-RCDRISLMHA--GRV 475
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-216 |
2.30e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-IIGNLDKPTSGTIEYRDgadqQMGFVFQDSvllpW---KNVRQN 95
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG----TVAYVPQVS----WifnATVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 AEFPLviqkkqtEENEKKLDELLELAGLSEFKTALPR-----------ELSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:PLN03130 699 ILFGS-------PFDPERYERAIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 165 DALTRDHLNEELLKiWQKTKKTVIFVTHSIEeatFLS--DRVLVMSArpGRVKE 216
Cdd:PLN03130 772 DAHVGRQVFDKCIK-DELRGKTRVLVTNQLH---FLSqvDRIILVHE--GMIKE 819
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-192 |
2.38e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 2.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRI-IGNLdKPTSGTIeyRDGADQQMGFVFQDSVLL-PWKNVRQN-AE 97
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRI--HCGTKLEVAYFDQHRAELdPEKTVMDNlAE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 98 fplviQKKQTEENEKKLDellELAGLSEF----KTAL-P-RELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDH 171
Cdd:PRK11147 407 -----GKQEVMVNGRPRH---VLGYLQDFlfhpKRAMtPvKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLEL 478
|
170 180
....*....|....*....|.
gi 1472203387 172 LnEELLKIWQktkKTVIFVTH 192
Cdd:PRK11147 479 L-EELLDSYQ---GTVLLVSH 495
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-212 |
6.01e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 60.84 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 34 RPGEFISIIGPSGCGKSTLLRII--------GNLDKPTS--GTIEYRDGADQQMGF--VFQDSV----------LLPwKN 91
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDwdEILDEFRGSELQNYFtkLLEGDVkvivkpqyvdLIP-KA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 92 VRQNAEFPLviqkKQTEENEkKLDEL---LELAGLSEFKTAlprELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDA-- 166
Cdd:cd03236 103 VKGKVGELL----KKKDERG-KLDELvdqLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkq 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1472203387 167 -LTRDHLNEELLkiwqKTKKTVIFVTHSIEEATFLSDRVLVMSARPG 212
Cdd:cd03236 175 rLNAARLIRELA----EDDNYVLVVEHDLAVLDYLSDYIHCLYGEPG 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
26-214 |
8.77e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 59.46 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLD-KPTSGTIEYrDGAD---------QQMG-FV-FQDSVllpwknv 92
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKyEVTEGEILF-KGEDitdlppeerARLGiFLaFQYPP------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 93 rqnaEFPLViqkkqteenekKLDELLelaglsefktalpREL----SGGMKQRVSIVRALSYDAPLLLMDEPFGALD--A 166
Cdd:cd03217 88 ----EIPGV-----------KNADFL-------------RYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGLDidA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1472203387 167 LtrdHLNEELLKIWQKTKKTVIFVTHSIEEATFL-SDRVLVMSArpGRV 214
Cdd:cd03217 140 L---RLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYD--GRI 183
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-192 |
8.90e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.04 E-value: 8.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLD-KPTSGTIEYRDG------ADQ--QMG--FVFQDSVLLPW 89
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaGHPAyKILEGDILFKGEsildlePEEraHLGifLAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNvrqNAEF-PLVIQKKQTEENEKKLDEL---------LELAGLSEfkTALPREL----SGGMKQRVSIVRALSYDAPLL 155
Cdd:CHL00131 99 VS---NADFlRLAYNSKRKFQGLPELDPLefleiinekLKLVGMDP--SFLSRNVnegfSGGEKKRNEILQMALLDSELA 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1472203387 156 LMDEPFGALDAltrDHLNE--ELLKIWQKTKKTVIFVTH 192
Cdd:CHL00131 174 ILDETDSGLDI---DALKIiaEGINKLMTSENSIILITH 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-207 |
1.34e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 58.15 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 35 PGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGADQQMGFVFQDSVLLPWKNvrqnaefplviqkkqteenekkl 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 115 dellelaglsefktalPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEE-----LLKIWQKTKKTVIF 189
Cdd:smart00382 58 ----------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLTVIL 121
|
170 180
....*....|....*....|...
gi 1472203387 190 VTHSIE-----EATFLSDRVLVM 207
Cdd:smart00382 122 TTNDEKdlgpaLLRRRFDRRIVL 144
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-216 |
1.91e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.19 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRII------GNLDkptsGTIEY-------RDGAD-QQMGFVF--QDSVLLP 88
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvyphGSYE----GEILFdgevcrfKDIRDsEALGIVIihQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 WKNVRQN-------AEFPlVIQKKQTEeneKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPF 161
Cdd:NF040905 92 YLSIAENiflgnerAKRG-VIDWNETN---RRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 162 GALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKE 216
Cdd:NF040905 168 AALNEEDSAAL-LDLLLELKAQGITSIIISHKLNEIRRVADSITVL--RDGRTIE 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
12-216 |
2.55e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 60.37 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 12 NKVYSNLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLR-IIGNLDKPTSGTIEYRDgadqQMGFVFQdsvlLPW- 89
Cdd:PLN03232 619 NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG----SVAYVPQ----VSWi 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 --KNVRQNAEFPlviQKKQTEENEKKLD--------ELLELAGLSEFKTAlPRELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:PLN03232 691 fnATVRENILFG---SDFESERYWRAIDvtalqhdlDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 160 PFGALDAltrdHLNEELLKIWQKTK---KTVIFVTHSIEeatFLS--DRVLVMSArpGRVKE 216
Cdd:PLN03232 767 PLSALDA----HVAHQVFDSCMKDElkgKTRVLVTNQLH---FLPlmDRIILVSE--GMIKE 819
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-197 |
3.11e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNlDKPTS------------GTIEYRDGADQQMGFVfQDSVLLPW 89
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfgrrrGSGETIWDIKKHIGYV-SSSLHLDY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 ------KNVRQNAEFPLV-IQKKQTEENEKKLDELLELAGLSEFKTALP-RELSGGMKQRVSIVRALSYDAPLLLMDEPF 161
Cdd:PRK10938 350 rvstsvRNVILSGFFDSIgIYQAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPL 429
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1472203387 162 GALDAltrdhLNEELLKIW-----QKTKKTVIFVTHSIEEA 197
Cdd:PRK10938 430 QGLDP-----LNRQLVRRFvdvliSEGETQLLFVSHHAEDA 465
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-207 |
3.22e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 59.73 E-value: 3.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------QQMGFVFQDSVLLP- 88
Cdd:PRK10790 351 RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-RLDGRPlsslshsvlrQGVAMVQQDPVVLAd 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 --WKNVRQNAEFplviqkkqteeNEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVSIVRALSYDAPLL 155
Cdd:PRK10790 430 tfLANVTLGRDI-----------SEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 156 LMDEPFGALDALTRDHLNEELLKIWQKTkkTVIFVTH---SIEEAtflsDRVLVM 207
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHrlsTIVEA----DTILVL 547
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-177 |
3.31e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 6 VELKGLNKVYsnllkEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrdGADQQMGFVFQ--D 83
Cdd:PRK11819 325 IEAENLSKSF-----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--GETVKLAYVDQsrD 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 84 SvLLPWKNVRQN----AEfplVIQKKQTEENEKkldellelAGLSEF--------KTAlpRELSGGMKQRVSIVRALSYD 151
Cdd:PRK11819 398 A-LDPNKTVWEEisggLD---IIKVGNREIPSR--------AYVGRFnfkggdqqKKV--GVLSGGERNRLHLAKTLKQG 463
|
170 180
....*....|....*....|....*.
gi 1472203387 152 APLLLMDEPFGALDALTRDHLNEELL 177
Cdd:PRK11819 464 GNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-230 |
6.00e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 29 INLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEY----------RDGADQQMGFVFQDSV---LLPWKNVRQN 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdgkpidirspRDAIRAGIMLCPEDRKaegIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 ---------AEFPLVIQKKQTEENEKKLDELLELaglsefKTALPRE----LSGGMKQRVSIVRALSYDAPLLLMDEPFG 162
Cdd:PRK11288 352 inisarrhhLRAGCLINNRWEAENADRFIRSLNI------KTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 163 ALDALTRdhlNE--ELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMsaRPGRVKEMVeidlprPRGEAT 230
Cdd:PRK11288 426 GIDVGAK---HEiyNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVM--REGRIAGEL------AREQAT 484
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-166 |
7.13e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.87 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNldKPTSGTIE---YRDGA------DQQMGFVFQDSVLLPWKNVRQNA 96
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeiLINGRpldknfQRSTGYVEQQDVHSPNLTVREAL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 97 EFplviqkkqteenekkldellelaglsefkTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDA 166
Cdd:cd03232 101 RF-----------------------------SALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
119-219 |
9.89e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 9.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 119 ELAGLSEFKTALP-----------RELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTV 187
Cdd:PTZ00265 1333 KFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI 1412
|
90 100 110
....*....|....*....|....*....|..
gi 1472203387 188 IFVTHSIEEATfLSDRVLVMSaRPGRVKEMVE 219
Cdd:PTZ00265 1413 ITIAHRIASIK-RSDKIVVFN-NPDRTGSFVQ 1442
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
25-207 |
1.52e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 56.43 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYR--DGADQQMGFVFQDSV-LLPWKN---VRQNAEF 98
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDgkDITDWQTAKIMREAVaIVPEGRrvfSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 99 PLVI-----QKKQTEENEKKLDELleLAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDAL------ 167
Cdd:PRK11614 100 NLAMggffaERDQFQERIKWVYEL--FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIiiqqif 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1472203387 168 -TRDHLNEELLkiwqktkkTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK11614 178 dTIEQLREQGM--------TIFLVEQNANQALKLADRGYVL 210
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-212 |
1.78e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.51 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 33 IRPGEFISIIGPSGCGKSTLLRII--------GNLDKPTS--GTIEYRDGAdqQMGFVFQDsvlLPWKNVRqnaefplVI 102
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPSwdEVLKRFRGT--ELQNYFKK---LYNGEIK-------VV 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 103 QKKQ------------TEENEKKLDE---LLELAGLSEFKTALPR---ELSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:PRK13409 164 HKPQyvdlipkvfkgkVRELLKKVDErgkLDEVVERLGLENILDRdisELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 165 DALTRdhLN-----EELLKiwqktKKTVIFVTHSIEEATFLSDRVLVMSARPG 212
Cdd:PRK13409 244 DIRQR--LNvarliRELAE-----GKYVLVVEHDLAVLDYLADNVHIAYGEPG 289
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-219 |
1.90e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.84 E-value: 1.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTsgtieYRDGAD----------------------QQMGFVFQ 82
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDN-----WHVTADrfrwngidllklsprerrkiigREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 83 D--SVLLPWKNV-RQNAEfplVI----------QKKQTEENEKKldELLELAGLSEFK---TALPRELSGGMKQRVSIVR 146
Cdd:COG4170 97 EpsSCLDPSAKIgDQLIE---AIpswtfkgkwwQRFKWRKKRAI--ELLHRVGIKDHKdimNSYPHELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 147 ALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM----SARPGRVKEMVE 219
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLycgqTVESGPTEQILK 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-207 |
2.24e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 27 KDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTI--------EYRDGADQQMGFVF-----QDSVL-----LP 88
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRImlngkeinALSTAQRLARGLVYlpedrQSSGLyldapLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 WkNV---RQNaEFPLVIQKKQteenekkldellELAGLSEFKTAL----------PRELSGGMKQRVSIVRALSYDAPLL 155
Cdd:PRK15439 360 W-NVcalTHN-RRGFWIKPAR------------ENAVLERYRRALnikfnhaeqaARTLSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 156 LMDEPFGALDALTRDHLnEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVM 207
Cdd:PRK15439 426 IVDEPTRGVDVSARNDI-YQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-212 |
5.61e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.95 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 34 RPGEFISIIGPSGCGKSTLLRII--------GNLDKPTS--GTIEYRDGAdqQMGFVFQDsvlLPWKNVRqnaefplVIQ 103
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILsgelkpnlGDYDEEPSwdEVLKRFRGT--ELQDYFKK---LANGEIK-------VAH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 104 KKQ------------TEENEKKLDE---LLELAGLSEFKTALPR---ELSGGMKQRVSIVRALSYDAPLLLMDEPFGALD 165
Cdd:COG1245 165 KPQyvdlipkvfkgtVRELLEKVDErgkLDELAEKLGLENILDRdisELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1472203387 166 ALTRdhLN-EELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMSARPG 212
Cdd:COG1245 245 IYQR--LNvARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPG 290
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-216 |
6.59e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.11 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 15 YSNLLKED-TVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQD 83
Cdd:TIGR00957 1290 YCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII-DGLNiakiglhdlrFKITIIPQD 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 84 SVLLPwKNVRQNAEfPLviqkkqTEENEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVSIVRALSYDA 152
Cdd:TIGR00957 1369 PVLFS-GSLRMNLD-PF------SQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKT 1440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 153 PLLLMDEPFGALDaLTRDHLNEELLKIwQKTKKTVIFVTH---SIEEATflsdRVLVMSArpGRVKE 216
Cdd:TIGR00957 1441 KILVLDEATAAVD-LETDNLIQSTIRT-QFEDCTVLTIAHrlnTIMDYT----RVIVLDK--GEVAE 1499
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-209 |
8.90e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.50 E-value: 8.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLD---KPTSGTIEYrDGADQ---------QMGFVFQDSVLLPWKNV 92
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIaSNTDgfhIGVEGVITY-DGITPeeikkhyrgDVVYNAETDVHFPHLTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 93 RQNAEFPLVIQKKQT-------EENEKKLDEL-LELAGLSEFKTA-----LPRELSGGMKQRVSIVRALSYDAPLLLMDE 159
Cdd:TIGR00956 156 GETLDFAARCKTPQNrpdgvsrEEYAKHIADVyMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 160 PFGALDALTRDHLnEELLKIWQKTKKTVIFVT--HSIEEATFLSDRVLVMSA 209
Cdd:TIGR00956 236 ATRGLDSATALEF-IRALKTSANILDTTPLVAiyQCSQDAYELFDKVIVLYE 286
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-208 |
1.01e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 54.53 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 15 YSNLLKEdtvALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDS 84
Cdd:cd03288 29 YENNLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGIDisklplhtlrSRLSIILQDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 85 VLLPwKNVRqnaeFPLVIQKKQTEEnekKLDELLELAGLSEFKTALPREL-----------SGGMKQRVSIVRALSYDAP 153
Cdd:cd03288 105 ILFS-GSIR----FNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1472203387 154 LLLMDEPFGALDALTRDHLNEELLKIW-QKTKKTVIFVTHSIEEAtflsDRVLVMS 208
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFaDRTVVTIAHRVSTILDA----DLVLVLS 228
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-168 |
1.27e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 20 KEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGnlDKPTSGTIEY---------RDGADQQ-MGFVFQDSVLLPW 89
Cdd:TIGR00956 773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVITGgdrlvngrpLDSSFQRsIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 90 KNVRQNAEF------PLVIQKKQTEENEKKLDELLELAGLSEFKTALPRE-LSGGMKQRVSI-VRALSYDAPLLLMDEPF 161
Cdd:TIGR00956 851 STVRESLRFsaylrqPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIgVELVAKPKLLLFLDEPT 930
|
....*..
gi 1472203387 162 GALDALT 168
Cdd:TIGR00956 931 SGLDSQT 937
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-192 |
1.50e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIgnldkptSGTIEYRDGAdqqmgFVFQDSVLL------PWKNVRQN 95
Cdd:PRK11147 15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGR-----IIYEQDLIVarlqqdPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 A----------------EFPLVIQKKQTEENEKKLDEL------LELAGLSEFKT--------------ALPRELSGGMK 139
Cdd:PRK11147 83 VydfvaegieeqaeylkRYHDISHLVETDPSEKNLNELaklqeqLDHHNLWQLENrinevlaqlgldpdAALSSLSGGWL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 140 QRVSIVRALSYDAPLLLMDEPFGALDALTRDHLnEELLKIWQktkKTVIFVTH 192
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWL-EGFLKTFQ---GSIIFISH 211
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
26-193 |
1.73e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDG------------ADQQMGFVFQDSVLlpwKNVR 93
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCninniakpyctyIGHNLGLKLEMTVF---ENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 94 QNAEFPLVIQKKQTEENEKKLDELLELAGLSefktalpreLSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLN 173
Cdd:PRK13541 93 FWSEIYNSAETLYAAIHYFKLHDLLDEKCYS---------LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLN 163
|
170 180
....*....|....*....|
gi 1472203387 174 eELLKIWQKTKKTVIFVTHS 193
Cdd:PRK13541 164 -NLIVMKANSGGIVLLSSHL 182
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
25-221 |
2.85e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDGAdqqmGFVFQDSVLLPWKNVRQNAEFPLVIQK 104
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA----ALIAISSGLNGQLTGIENIELKGLMMG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 105 KQTEENEKKLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALD-ALTR---DHLNEellkiW 180
Cdd:PRK13545 115 LTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKkclDKMNE-----F 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1472203387 181 QKTKKTVIFVTHSIEEATFLSDRVLVMSArpGRVKEMVEID 221
Cdd:PRK13545 190 KEQGKTIFFISHSLSQVKSFCTKALWLHY--GQVKEYGDIK 228
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-159 |
4.43e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 53.21 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLdKPTSGTIEYRDgADQQMGFVFQDsvllPWKNV---RQNAEFPL 100
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKP-AKGKLFYVPQR----PYMTLgtlRDQIIYPD 539
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 101 VI-QKKQTEENEKKLDELLELAGLSEFktaLPRE------------LSGGMKQRVSIVRaLSYDAPLL-LMDE 159
Cdd:TIGR00954 540 SSeDMKRRGLSDKDLEQILDNVQLTHI---LEREggwsavqdwmdvLSGGEKQRIAMAR-LFYHKPQFaILDE 608
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
24-208 |
1.13e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.37 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKSTLLRII-GNLDKPTSG---------TIEYRDGA----------------DQQM 77
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGAPrgarvtgdvTLNGEPLAaidaprlarlravlpqAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 78 GFVF--QDSVLLpwknvrqnAEFPLVIQKKQTEENEKKL-DELLELAGLSEFKTALPRELSGGMKQRVSIVRALSY---- 150
Cdd:PRK13547 95 AFAFsaREIVLL--------GRYPHARRAGALTHRDGEIaWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpp 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1472203387 151 -----DAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTHSIEEATFLSDRVLVMS 208
Cdd:PRK13547 167 hdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLA 229
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-177 |
1.84e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 22 DTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYRDG------ADQQMGFVFQDsvllpwknvrqn 95
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiklgyfAQHQLEFLRAD------------ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 aEFPLV-IQKKQTEENEKKLDELLELAGLSEFK-TALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLN 173
Cdd:PRK10636 392 -ESPLQhLARLAPQELEQKLRDYLGGFGFQGDKvTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470
|
....
gi 1472203387 174 EELL 177
Cdd:PRK10636 471 EALI 474
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
26-195 |
3.08e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLdKPTSGTIEYrDGadqqmgfVFQDSVLL-PWKNVrqnaeFPLVIQK 104
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQI-DG-------VSWNSVTLqTWRKA-----FGVIPQK 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 105 ---------KQTEENEKKLDELL----ELAGLSEFKTALPRE-----------LSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:TIGR01271 1301 vfifsgtfrKNLDPYEQWSDEEIwkvaEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEP 1380
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1472203387 161 FGALDALTrdhlneelLKIWQKTKK------TVIFVTHSIE 195
Cdd:TIGR01271 1381 SAHLDPVT--------LQIIRKTLKqsfsncTVILSEHRVE 1413
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-217 |
4.24e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD----------QQMGFVFQDSVLLPwKNVRQN 95
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI-LIDGCDiskfglmdlrKVLGIIPQAPVLFS-GTVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 AEfPLviqkkqTEENEKKLDELLELAGLSEFKTALPREL-----------SGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:PLN03130 1333 LD-PF------NEHNDADLWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAV 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 165 DALTrDHLneellkiWQKTKK------TVIFVTHSIEeaTFL-SDRVLVMSArpGRVKEM 217
Cdd:PLN03130 1406 DVRT-DAL-------IQKTIReefkscTMLIIAHRLN--TIIdCDRILVLDA--GRVVEF 1453
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
17-219 |
1.26e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 17 NLLKEDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDGAD-----------QQMGFVFQ--- 82
Cdd:PRK09700 270 NVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEI-RLNGKDisprspldavkKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 83 DSVLLPWKNVRQNAEFPLVIQK---------------KQTEENEKKLDELlELAGLSEFKTalprELSGGMKQRVSIVRA 147
Cdd:PRK09700 349 DNGFFPNFSIAQNMAISRSLKDggykgamglfhevdeQRTAENQRELLAL-KCHSVNQNIT----ELSGGNQQKVLISKW 423
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 148 LSYDAPLLLMDEPFGALDALTRdhlnEELLKIWQKTK---KTVIFVTHSIEEATFLSDRVLVMsaRPGRVKEMVE 219
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAK----AEIYKVMRQLAddgKVILMVSSELPEIITVCDRIAVF--CEGRLTQILT 492
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
26-166 |
1.35e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNldKPTSGTIE----------YRDGADQQMGFVFQDSVLLPWKNVRQN 95
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEgdirisgfpkKQETFARISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1472203387 96 AEFPLVIQ-KKQTEENEKK--LDELLELAGLSEFKTA---LP--RELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDA 166
Cdd:PLN03140 974 LIYSAFLRlPKEVSKEEKMmfVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
113-214 |
1.94e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 113 KLDELLELAGLSEFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIwQKTKKTVIFVTH 192
Cdd:NF000106 124 RADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQ 202
|
90 100
....*....|....*....|..
gi 1472203387 193 SIEEATFLSDRVLVMSArpGRV 214
Cdd:NF000106 203 YMEEAEQLAHELTVIDR--GRV 222
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
116-207 |
2.29e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 116 ELLELAGLSEFKTAL---PRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKTKKTVIFVTH 192
Cdd:PRK15093 138 ELLHRVGIKDHKDAMrsfPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISH 217
|
90
....*....|....*
gi 1472203387 193 SIEEATFLSDRVLVM 207
Cdd:PRK15093 218 DLQMLSQWADKINVL 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
23-207 |
5.17e-06 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.39 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 23 TVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLdkptsgtiEYRDGADQQMGFVFQDSVLLPWKNVrqnaeFPLVI 102
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL--------LNTEGDIQIDGVSWNSVPLQKWRKA-----FGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 103 QK---------KQTEENEKKLDELL----ELAGLSEFKTALPRE-----------LSGGMKQRVSIVRALSYDAPLLLMD 158
Cdd:cd03289 84 QKvfifsgtfrKNLDPYGKWSDEEIwkvaEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1472203387 159 EPFGALDALTrdhlneelLKIWQKTKK------TVIFVTHSIeEATFLSDRVLVM 207
Cdd:cd03289 164 EPSAHLDPIT--------YQVIRKTLKqafadcTVILSEHRI-EAMLECQRFLVI 209
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
120-244 |
5.88e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.78 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 120 LAGLS---EFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKiWqktKKTVIFVTHSIE- 195
Cdd:PLN03073 328 LAGLSftpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-W---PKTFIVVSHAREf 403
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1472203387 196 EATFLSDRVLVMSARPGRVKEMVEIdLPRPRGEATRNDPKFTEYNKYLR 244
Cdd:PLN03073 404 LNTVVTDILHLHGQKLVTYKGDYDT-FERTREEQLKNQQKAFESNERSR 451
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
35-192 |
8.71e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 44.66 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 35 PGEFISIIGPSGCGKSTLLRIIGnldkptsgtieyrdgadqqMGFVFQDSVLLPWKNVRQNAEFPLVIqkkqteenekkl 114
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG-------------------LALGGAQSATRRRSGVKAGCIVAAVS------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 115 dellelaglSEFKTALPReLSGGMKQRVSIVRALS----YDAPLLLMDEPFGALDALTRDHLNEELLKIWQKtKKTVIFV 190
Cdd:cd03227 69 ---------AELIFTRLQ-LSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVK-GAQVIVI 137
|
..
gi 1472203387 191 TH 192
Cdd:cd03227 138 TH 139
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
21-192 |
9.79e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 21 EDTVALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLD--KPTSGTIEYR----------DGADQQMGFVFQDSVLLP 88
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKgkdllelspeDRAGEGIFMAFQYPVEIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 89 wkNVRQNAEFPLVIQKKQTEENEKKLDElLELAGLSEFKTAL---PREL---------SGGMKQRVSIVRALSYDAPLLL 156
Cdd:PRK09580 92 --GVSNQFFLQTALNAVRSYRGQEPLDR-FDFQDLMEEKIALlkmPEDLltrsvnvgfSGGEKKRNDILQMAVLEPELCI 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1472203387 157 MDEPFGALDAltrdhlneELLKI-------WQKTKKTVIFVTH 192
Cdd:PRK09580 169 LDESDSGLDI--------DALKIvadgvnsLRDGKRSFIIVTH 203
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-192 |
1.18e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 42 IGPSGCGKSTLLRIIGNLDKPTSGTIEY----RDGADQQMGFVFQD-SVL---------LpWKnVRQ-------NAEfpl 100
Cdd:PRK15064 33 IGANGCGKSTFMKILGGDLEPSAGNVSLdpneRLGKLRQDQFAFEEfTVLdtvimghteL-WE-VKQerdriyaLPE--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 101 viqkkQTEEN-------------------EKKLDELLELAGLS-EFKTALPRELSGGMKQRVSIVRALSYDAPLLLMDEP 160
Cdd:PRK15064 108 -----MSEEDgmkvadlevkfaemdgytaEARAGELLLGVGIPeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEP 182
|
170 180 190
....*....|....*....|....*....|..
gi 1472203387 161 FGALDALTRDHLNEELlkiwQKTKKTVIFVTH 192
Cdd:PRK15064 183 TNNLDINTIRWLEDVL----NERNSTMIIISH 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-213 |
1.54e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 25 ALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNldkpTSGTIEYRDGadqqmgfvfqdsvllpwknvRQNAEFPLVIQK 104
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLISF--------------------LPKFSRNKLIFI 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 105 KQteenekkLDELLELaGLSEFKtaLPRE---LSGGMKQRVSIVRALSYDAP--LLLMDEPFGALDALTRDHLNEELLKI 179
Cdd:cd03238 66 DQ-------LQFLIDV-GLGYLT--LGQKlstLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGL 135
|
170 180 190
....*....|....*....|....*....|....
gi 1472203387 180 WQKtKKTVIFVTHSiEEATFLSDRVLVMSARPGR 213
Cdd:cd03238 136 IDL-GNTVILIEHN-LDVLSSADWIIDFGPGSGK 167
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-165 |
2.31e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 24 VALKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIeYRDgADQQMGFVFQDSVllpwKNVRQNAEFPLVIQ 103
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRS-AKVRMAVFSQHHV----DGLDLSSNPLLYMM 596
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1472203387 104 KKQTEENEKKLDELLELAGLSEFKTALPR-ELSGGMKQRVSIVRaLSYDAP-LLLMDEPFGALD 165
Cdd:PLN03073 597 RCFPGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAK-ITFKKPhILLLDEPSNHLD 659
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
26-238 |
5.12e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.00 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLL----RII----GNL-----DKPTSGTIEYRdgadQQMGFVFQDSVLLPwKNV 92
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLltfmRMVevcgGEIrvngrEIGAYGLRELR----RQFSMIPQDPVLFD-GTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 93 RQNAEfPLViqkkqtEENEKKLDELLELAGL-----SEFKTALPRELSG------GMKQRVSIVRA-LSYDAPLLLMDEP 160
Cdd:PTZ00243 1401 RQNVD-PFL------EASSAEVWAALELVGLrervaSESEGIDSRVLEGgsnysvGQRQLMCMARAlLKKGSGFILMDEA 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 161 FGALD-ALTRdhlneellKIwQKT------KKTVIFVTHSIEE-ATFlsDRVLVMSArpGRVKEMveidlPRPRGEATRN 232
Cdd:PTZ00243 1474 TANIDpALDR--------QI-QATvmsafsAYTVITIAHRLHTvAQY--DKIIVMDH--GAVAEM-----GSPRELVMNR 1535
|
....*.
gi 1472203387 233 DPKFTE 238
Cdd:PTZ00243 1536 QSIFHS 1541
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
134-219 |
5.28e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 134 LSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKtKKTVIFVTHSIEEATFLSDRVLVMSArpGR 213
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSN--GL 468
|
....*.
gi 1472203387 214 VKEMVE 219
Cdd:PRK10982 469 VAGIVD 474
|
|
| Adeno_IVa2 |
pfam02456 |
Adenovirus IVa2 protein; IVa2 protein can interact with the adenoviral packaging signal and ... |
3-67 |
5.77e-05 |
|
Adenovirus IVa2 protein; IVa2 protein can interact with the adenoviral packaging signal and that this interaction involves DNA sequences that have previously been demonstrated to be required for packaging. During the course of lytic infection, the adenovirus major late promoter (MLP) is induced to high levels after replication of viral DNA has started. IVa2 is a transcriptional activator of the major late promoter.
Pssm-ID: 280594 Cd Length: 370 Bit Score: 43.72 E-value: 5.77e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1472203387 3 EYSVELKGLNKVYSNLLKEDTvALKDINLQIRPgeFISII-GPSGCGKSTLLR--IIGNLDKPTSGTI 67
Cdd:pfam02456 56 EAHEEVKAQEQMDSRYLQHDG-QLSSLNYGLQP--IIGVIyGPTGSGKSQLLRnlISCNLISPIPETV 120
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
26-53 |
2.06e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 2.06e-04
10 20
....*....|....*....|....*...
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLL 53
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
134-214 |
1.38e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 134 LSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRdhlnEELLKIWQKTKK---TVIFVTHSIEEATFLSDRVLVMsaR 210
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAK----KEIYQLINQFKAeglSIILVSSEMPEVLGMSDRILVM--H 469
|
....
gi 1472203387 211 PGRV 214
Cdd:PRK10762 470 EGRI 473
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-216 |
1.38e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.96 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLLRIIGNLDKPTSGTIEYrDGAD----------QQMGFVFQDSVLLPwKNVRQN 95
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMI-DDCDvakfgltdlrRVLSIIPQSPVLFS-GTVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 96 AEfPLviqkkqTEENEKKLDELLELAGLSEFKTALP-----------RELSGGMKQRVSIVRALSYDAPLLLMDEPFGAL 164
Cdd:PLN03232 1330 ID-PF------SEHNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1472203387 165 ----DALTRDHLNEELLKIwqktkkTVIFVTHSIEeaTFLS-DRVLVMSArpGRVKE 216
Cdd:PLN03232 1403 dvrtDSLIQRTIREEFKSC------TMLVIAHRLN--TIIDcDKILVLSS--GQVLE 1449
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
26-53 |
2.42e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.90 E-value: 2.42e-03
10 20
....*....|....*....|....*...
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLL 53
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLI 652
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
26-52 |
2.73e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.84 E-value: 2.73e-03
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
41-194 |
3.33e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 37.68 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 41 IIGPSGCGKSTLLRII-----GNLDKPTSGTIEY-RDGADQ---QMGFVFQDSVllpWKNVRQNAEFpLVIQKKQTEENE 111
Cdd:COG0419 28 IVGPNGAGKSTILEAIryalyGKARSRSKLRSDLiNVGSEEasvELEFEHGGKR---YRIERRQGEF-AEFLEAKPSERK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 112 KKLDELLELAGLSEFKTAL---------------------------------PRELSGGMKQRVSIVRALSydaplLLMD 158
Cdd:COG0419 104 EALKRLLGLEIYEELKERLkeleealesaleelaelqklkqeilaqlsgldpIETLSGGERLRLALADLLS-----LILD 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 1472203387 159 epFGALDALTRDHLNEELLKIwqktkktvIFVTHSI 194
Cdd:COG0419 179 --FGSLDEERLERLLDALEEL--------AIITHVI 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
127-215 |
3.70e-03 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 38.27 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 127 KTALP----RELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRDHLNEELLKIWQKtKKTVIFVTHSIEEATFLSD 202
Cdd:TIGR02633 393 KTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSD 471
|
90
....*....|...
gi 1472203387 203 RVLVMSArpGRVK 215
Cdd:TIGR02633 472 RVLVIGE--GKLK 482
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
26-53 |
3.97e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 37.59 E-value: 3.97e-03
10 20
....*....|....*....|....*...
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLL 53
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI 38
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
26-52 |
8.11e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.31 E-value: 8.11e-03
10 20
....*....|....*....|....*..
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTL 52
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
125-192 |
9.23e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 36.05 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 125 EFKTALPRE---LSGGMKQRVSIV------RALSYDAPLLLMDEPFGALDaltRDHLNEELLKIWQKTKKTVIF----VT 191
Cdd:cd03240 104 ESNWPLLDMrgrCSGGEKVLASLIirlalaETFGSNCGILALDEPTTNLD---EENIEESLAEIIEERKSQKNFqlivIT 180
|
.
gi 1472203387 192 H 192
Cdd:cd03240 181 H 181
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
26-213 |
9.31e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 36.47 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 26 LKDINLQIRPGEFISIIGPSGCGKSTLL---------------------RIIGNLDKPTSGTIEYRDGA---DQqmgfvf 81
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIEGLSPAiaiDQ------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 82 qdsvllpwKNVRQNaefPLVIQKKQTEENE------------KKLDELLELaGLSEFktALPRE---LSGGMKQRVSIVR 146
Cdd:cd03270 85 --------KTTSRN---PRSTVGTVTEIYDylrllfarvgirERLGFLVDV-GLGYL--TLSRSaptLSGGEAQRIRLAT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1472203387 147 AL--SYDAPLLLMDEPFGALDAltRDhlNEELLKIWQKTKK---TVIFVTHSiEEATFLSDRVLVMSARPGR 213
Cdd:cd03270 151 QIgsGLTGVLYVLDEPSIGLHP--RD--NDRLIETLKRLRDlgnTVLVVEHD-EDTIRAADHVIDIGPGAGV 217
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
114-215 |
9.33e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 36.83 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1472203387 114 LDELLELAGLSEF------KTALPR----ELSGGMKQRVSIVRALSYDAPLLLMDEPFGALDALTRdhlnEELLK-IWQK 182
Cdd:PRK13549 376 IDDAAELKTILESiqrlkvKTASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK----YEIYKlINQL 451
|
90 100 110
....*....|....*....|....*....|....*
gi 1472203387 183 TKK--TVIFVTHSIEEATFLSDRVLVMSArpGRVK 215
Cdd:PRK13549 452 VQQgvAIIVISSELPEVLGLSDRVLVMHE--GKLK 484
|
|
| |
