|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-220 |
5.42e-165 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 453.56 E-value: 5.42e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGLG 220
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVG 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-216 |
2.23e-142 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 396.35 E-value: 2.23e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
3.35e-121 |
|
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: 342.69 E-value: 3.35e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
3.43e-95 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 277.31 E-value: 3.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGG---RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFL 77
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQ-IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISrRSYRMLTLSDGHLHG 217
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
4.99e-94 |
|
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: 273.90 E-value: 4.99e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQI 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
3.78e-92 |
|
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: 268.97 E-value: 3.78e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGR---QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRE-VPFL 77
Cdd:cd03255 1 IELKNLSKTYGGGGekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSyRMLTLSDGHL 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYAD-RIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-196 |
2.59e-80 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 243.45 E-value: 2.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQ---ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFL 77
Cdd:COG1135 1 MIELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHD 196
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINReLGLTIVLITHE 200
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-213 |
2.41e-79 |
|
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: 237.09 E-value: 2.41e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQ---ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFL 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINReLGLTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-215 |
2.40e-75 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 230.84 E-value: 2.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGR---QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFL 77
Cdd:PRK11153 1 MIELKNISKVFPQGGrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINReLGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-215 |
2.47e-72 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 219.93 E-value: 2.47e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNV------AIPLI--IAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgRTSTWrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-216 |
5.73e-69 |
|
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: 210.75 E-value: 5.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQA---LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFL 77
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQ-IGMIFQDHHLLMDRTVFDNVAIPLIIAGAsyDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLIsRRSYRMLTLSDGHLH 216
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALA-ARCDRVLRLRAGRLV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-215 |
1.41e-68 |
|
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: 209.88 E-value: 1.41e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE---LRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQ--DHHLLMDrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:COG1122 78 GLVFQnpDDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
2.41e-67 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 207.63 E-value: 2.41e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYL---GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevpfl 77
Cdd:COG1116 7 ALELRGVSKRFPtggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 158 VLLADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDI 197
Cdd:COG1116 159 VLLMDEPFGALDaltrERLQDELLRLWQETGK---TVLFVTHDV 199
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-214 |
2.91e-67 |
|
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: 206.65 E-value: 2.91e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLI--------IAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRLgrrstwrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-196 |
8.63e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 206.87 E-value: 8.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnrevPFlRRQ 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----PE-KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDH----HLlmdrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:COG3842 79 VGMVFQDYalfpHL----TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 157 AVLLADEPTGNLD----DALSEGILRLFEEfnrVGVTVLMATHD 196
Cdd:COG3842 155 RVLLLDEPLSALDaklrEEMREELRRLQRE---LGITFIYVTHD 195
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-197 |
2.51e-62 |
|
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: 193.46 E-value: 2.51e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGR---QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdisrlknREVPFLR 78
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 79 RQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 159 LLADEPTGNLD----DALSEGILRLFEEFnrvGVTVLMATHDI 197
Cdd:cd03293 153 LLLDEPFSALDaltrEQLQEELLDIWRET---GKTVLLVTHDI 192
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-198 |
2.76e-62 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 194.06 E-value: 2.76e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISrLKNREVPFLRRQ 80
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIA-GASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIG 198
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMG 197
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
5.80e-62 |
|
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: 201.29 E-value: 5.80e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYL----GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPF 76
Cdd:COG1123 260 LLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQD-HHLLMDR-TVFDNVAIPLIIAG-ASYDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAV 152
Cdd:COG1123 340 LRRRVQMVFQDpYSSLNPRmTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
4.72e-61 |
|
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: 189.99 E-value: 4.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 3 RFEHVSKAYLGG-RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQI 81
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE---LRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQ--DHHLLMDrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:cd03225 78 GLVFQnpDDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-215 |
5.35e-61 |
|
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: 190.96 E-value: 5.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ 80
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGA-SYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-215 |
1.11e-60 |
|
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: 189.27 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlknreVPFLRRQI 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-----VPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 162 DEPTGNLDDALSEGILRLFEE-FNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03259 155 DEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-196 |
1.94e-60 |
|
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: 188.98 E-value: 1.94e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevPFLRRQI 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 162 DEPTGNLDDALSEGI-LRLFEEFNRVGVTVLMATHD 196
Cdd:cd03300 155 DEPLGALDLKLRKDMqLELKRLQKELGITFVFVTHD 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
1.21e-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: 1.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGR---QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFL 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMD--RTVFDNVAIPLIIAGASYDD--IRRRVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGIARAV 152
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-215 |
1.15e-58 |
|
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: 185.19 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNV---------AIPLIIAGASYDDIRRRVSAaLDKVGLLDKAKNFPIQLSGGEQQRVGIARA 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEEDKERALSA-LERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKeDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-215 |
1.50e-58 |
|
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: 184.24 E-value: 1.50e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQI 81
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGA-SYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-219 |
3.40e-58 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 183.48 E-value: 3.40e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 7 VSKAYLGGR---QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLR-RQIG 82
Cdd:PRK11629 11 LCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 MIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
Cdd:PRK11629 91 FIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 163 EPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSyRMLTLSDGHLHGGL 219
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLTAEL 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-215 |
1.50e-57 |
|
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: 182.31 E-value: 1.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAY---LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfL 77
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMD--RTVFDNVAIPLIIAGasYDDIRRRVSAALDKVGL----LDKaknFPIQLSGGEQQRVGIARA 151
Cdd:COG1124 78 RRRVQMVFQDPYASLHprHTVDRILAEPLRIHG--LPDREERIAELLEQVGLppsfLDR---YPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-196 |
7.52e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 183.74 E-value: 7.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpflrRQ 80
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-----RN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDH----HLlmdrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:COG3839 77 IAMVFQSYalypHM----TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 157 AVLLADEPTGNLDDAL-----SEgILRLFEEFnrvGVTVLMATHD 196
Cdd:COG3839 153 KVFLLDEPLSNLDAKLrvemrAE-IKRLHRRL---GTTTIYVTHD 193
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
1.07e-56 |
|
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: 178.88 E-value: 1.07e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnREVPFLRRQI 81
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDK-KNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIA-GASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
2.52e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 177.70 E-value: 2.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnreVPFLRRQI 81
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDrTVFDNVAIPLIIAGASYDdiRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
4.90e-55 |
|
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: 172.45 E-value: 4.90e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlknREVPFLRRQIGMIFQDHHLLMDRTVF 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD---DERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 98 DNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAK----NFPIQLSGGEQQRVGIARAVVNKPAVLLADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-215 |
5.95e-55 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 175.25 E-value: 5.95e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEM-AFLtGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlKNREVpflRRQ 80
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIfGLL-GPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEV---RRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-216 |
9.70e-55 |
|
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: 175.23 E-value: 9.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRE---LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVA---IPLI--IAGASYDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVAlgrYPHLglFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIV 217
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-210 |
3.54e-54 |
|
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: 172.41 E-value: 3.54e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREV-PFLRRQIGM 83
Cdd:TIGR03608 2 KNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAsKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 84 IFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503938019 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIgLISRRSYRMLTL 210
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-215 |
1.21e-53 |
|
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: 171.59 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDIsRLKNREVPF 76
Cdd:cd03260 1 IELRDLNVYY-GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDI-YDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQdHHLLMDRTVFDNVAIPLIIAG-ASYDDIRRRVSAALDKVGLLDKAKN--FPIQLSGGEQQRVGIARAVV 153
Cdd:cd03260 79 LRRRVGMVFQ-KPNPFPGSIYDNVAYGLRLHGiKLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVgVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-197 |
6.44e-52 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 170.71 E-value: 6.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIsrlkNREVPFLRRQI 81
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDH----HLlmdrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:COG1118 78 GFVFQHYalfpHM----TVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 158 VLLADEPTGNLDDAL-SEgiLR--LFEEFNRVGVTVLMATHDI 197
Cdd:COG1118 154 VLLLDEPFGALDAKVrKE--LRrwLRRLHDELGGTTVFVTHDQ 194
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
6.73e-52 |
|
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: 165.44 E-value: 6.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLkNREVPFLRRQI 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPliiagasyddirrrvsaaldkvglldkaknfpiqLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-197 |
7.61e-52 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 169.50 E-value: 7.61e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGL-----LDKaknFPIQLSGGEQQRVGIARAVVNK 155
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpeeyRDR---YPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503938019 156 PAVLLADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDI 197
Cdd:COG1125 155 PPILLMDEPFGALDpitrEQLQDELLRLQRELGK---TIVFVTHDI 197
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-196 |
4.07e-51 |
|
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: 165.59 E-value: 4.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpflrRQI 81
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-----RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASY----DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHD 196
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHD 196
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
6.43e-50 |
|
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: 169.70 E-value: 6.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGR-QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSA---GKIWFSGHDISRLKNREvpf 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEAL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQDH-HLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
Cdd:COG1123 81 RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 156 PAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-213 |
3.86e-49 |
|
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: 160.30 E-value: 3.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPflRRQIGMI 84
Cdd:cd03219 4 RGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDHHLLMDRTVFDNVAIPLIIAG----------ASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-196 |
6.16e-49 |
|
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: 159.34 E-value: 6.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpflrRQI 81
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVG---LLDKaknFPIQLSGGEQQRVGIARAVVNKPAV 158
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQiehLLDR---KPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 159 LLADEPTGNLDDAL-----SEgILRLFEefnRVGVTVLMATHD 196
Cdd:cd03301 152 FLMDEPLSNLDAKLrvqmrAE-LKRLQQ---RLGTTTIYVTHD 190
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-218 |
7.09e-49 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.87 E-value: 7.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevpflRRQ 80
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA--------RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLlmDR----TVFDNVAIPL-----IIAGASYDDiRRRVSAALDKVGLLDKAKNfPI-QLSGGEQQRVGIAR 150
Cdd:COG1121 77 IGYVPQRAEV--DWdfpiTVRDVVLMGRygrrgLFRRPSRAD-REAVDEALERVGLEDLADR-PIgELSGGQQQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAHG 220
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-215 |
3.23e-48 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 158.25 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIS---RLKNREVPFLR 78
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 79 RQIGMIFQDHHLLMDRTVFDN-VAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-216 |
3.81e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 157.61 E-value: 3.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlgGRQALQgVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevPFLRRQ 80
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-----PPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIA 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-215 |
8.17e-48 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 157.18 E-value: 8.17e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI--SRLKNREVpflR 78
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLI---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 79 RQIGMIFQDHHLLMDRTVFDNVAI-PLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-197 |
1.41e-47 |
|
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: 156.69 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQI 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE---LRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDK--AKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503938019 160 LADEPTGNLD----DALSEGILRLFEEfnrVGVTVLMATHDI 197
Cdd:cd03295 158 LMDEPFGALDpitrDQLQEEFKRLQQE---LGKTIVFVTHDI 196
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
5-196 |
1.17e-46 |
|
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: 157.51 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKaYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevPFLRRQIGMI 84
Cdd:TIGR03265 8 DNIRK-RFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRL-----PPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 165 TGNLD----DALSEGILRLFEefnRVGVTVLMATHD 196
Cdd:TIGR03265 162 LSALDarvrEHLRTEIRQLQR---RLGVTTIMVTHD 194
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-215 |
2.44e-46 |
|
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: 155.73 E-value: 2.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISrlknrEVPFLRRQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYD 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 113 DIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI-LRLFEEFNRVGVTVL 191
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMqLELKTIQEQLGITFV 155
|
170 180
....*....|....*....|....
gi 503938019 192 MATHDIGLISRRSYRMLTLSDGHL 215
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKI 179
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
3.50e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 153.48 E-value: 3.50e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQ---ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIsrlknrEVPFL 77
Cdd:COG4525 3 MLTVRHVSVRYPGGGQpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV------TGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRqiGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 158 VLLADEPTGNLD----DALSEGILRLfeeFNRVGVTVLMATHDI 197
Cdd:COG4525 155 FLLMDEPFGALDaltrEQMQELLLDV---WQRTGKGVFLITHSV 195
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-215 |
5.97e-46 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 152.48 E-value: 5.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DISRLKN-REVPFLR 78
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSdKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 79 RQIGMIFQDHHLLMDRTVFDN-VAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-208 |
1.08e-45 |
|
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: 154.06 E-value: 1.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGR---QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERP---SAGKIWFSGHDISRLKNREV 74
Cdd:COG0444 1 LLEVRNLKVYFPTRRgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 75 PFLR-RQIGMIFQDHhllMD-----RTVFDNVAIPLII-AGASYDDIRRRVSAALDKVGLLDK---AKNFPIQLSGGEQQ 144
Cdd:COG0444 81 RKIRgREIQMIFQDP---MTslnpvMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPerrLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 145 RVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRML 208
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVA 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-212 |
2.43e-45 |
|
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: 149.55 E-value: 2.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpfLRRQ 80
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----YRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDdiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDigLISRRSYRMLTLSD 212
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ--PLELAAARVLDLGD 204
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-215 |
3.54e-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: 159.61 E-value: 3.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQ-ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHlLMDRTVFDNVAIPLiiAGASYDDIRRrvsaALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIA 149
Cdd:COG2274 551 IGVVLQDVF-LFSGTIRENITLGD--PDATDEEIIE----AARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
4.84e-45 |
|
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: 147.91 E-value: 4.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG-RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHlLMDRTVFDNVaipliiagasyddirrrvsaaldkvglldkaknfpiqLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:cd03228 78 IAYVPQDPF-LFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLIsRRSYRMLTLSDGH 214
Cdd:cd03228 120 LDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-203 |
4.90e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 152.58 E-value: 4.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDPYASLNpr 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNVAIPLIIAG-ASYDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
Cdd:COG4608 112 MTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 172 LSEGILRLFEEF-NRVGVTVLMATHDIGL---ISRR 203
Cdd:COG4608 192 IQAQVLNLLEDLqDELGLTYLFISHDLSVvrhISDR 227
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
6.93e-45 |
|
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: 147.01 E-value: 6.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 3 RFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQIG 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 MIFqdhhllmdrtvfdnvaipliiagasyddirrrvsaaldkvglldkaknfpiQLSGGEQQRVGIARAVVNKPAVLLAD 162
Cdd:cd00267 77 YVP---------------------------------------------------QLSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503938019 163 EPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-202 |
1.95e-44 |
|
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: 149.03 E-value: 1.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPflRRQ 80
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA--RLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAI---------------PLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQR 145
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVaaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISR 202
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMG 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-215 |
4.68e-44 |
|
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: 148.56 E-value: 4.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ-IGMIFQDHHLLMDRT 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 96 VFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DA 171
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDplirRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 172 LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03294 199 MQDELLRLQAELQK---TIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-195 |
1.10e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 153.78 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQI 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLmDRTVFDNVAIPLIiaGASYDDIRrrvsAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
Cdd:COG1132 417 GVVPQDTFLF-SGTIRENIRYGRP--DATDEEVE----EAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503938019 151 AVVNKPAVLLADEPTGNLdDALSEgiLRLFEEFNRV--GVTVLMATH 195
Cdd:COG1132 490 ALLKDPPILILDEATSAL-DTETE--ALIQEALERLmkGRTTIVIAH 533
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
6-215 |
1.28e-43 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 146.08 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 6 HVSKAYLGGRQA---LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLR-RQI 81
Cdd:PRK10584 11 HLKKSVGQGEHElsiLTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:PRK10584 91 GFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISrRSYRMLTLSDGHL 215
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHDLQLAA-RCDRRLRLVNGQL 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-215 |
1.32e-43 |
|
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: 146.54 E-value: 1.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpfLRRQ 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----ARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-216 |
1.39e-43 |
|
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: 144.50 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQIGMI 84
Cdd:cd03214 3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE---LARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQdhhllmdrtvfdnvaipliiagasyddirrrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 165 TGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-196 |
2.44e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 148.69 E-value: 2.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKaYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpflrRQI 81
Cdd:PRK10851 3 IEIANIKK-SFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLII----AGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 158 VLLADEPTGNLD----DALSEGILRLFEEFNRVGVTVlmaTHD 196
Cdd:PRK10851 157 ILLLDEPFGALDaqvrKELRRWLRQLHEELKFTSVFV---THD 196
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-215 |
2.76e-43 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 153.73 E-value: 2.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 7 VSKAYLGGRQA---LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ-IG 82
Cdd:PRK10535 10 IRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 MIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 163 EPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDiGLISRRSYRMLTLSDGHL 215
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEI 221
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-197 |
3.51e-43 |
|
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: 146.04 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG-RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNreVPFLRRQ 80
Cdd:TIGR04520 1 IEVENVSFSYPESeKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEN--LWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQ--DHHLLmDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
Cdd:TIGR04520 79 VGMVFQnpDNQFV-GATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503938019 159 LLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDI 197
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDM 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
5.16e-43 |
|
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: 142.54 E-value: 5.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIsrlkNREVPFLRRQI 81
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNvaipliiagasyddirrrvsaaldkvglldkaknfpIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03230 76 GYLPEEPSLYENLTVREN------------------------------------LKLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-196 |
2.36e-42 |
|
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: 150.30 E-value: 2.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLG-GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:COG4987 334 LELEDVSFRYPGaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDrTVFDNvaipLIIA--GASYDDIRrrvsAALDKVGLLDKAKNFP-----------IQLSGGEQQRVG 147
Cdd:COG4987 411 IAVVPQRPHLFDT-TLREN----LRLArpDATDEELW----AALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503938019 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHD 196
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHR 529
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-216 |
2.81e-42 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 143.37 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAyLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:PRK13548 2 MLEARNLSVR-LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAE---LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV------N 154
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503938019 155 KPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLV 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-216 |
3.36e-42 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 143.33 E-value: 3.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSkAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:COG4559 1 MLEAENLS-VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE---LARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARA-------VV 153
Cdd:COG4559 77 RAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVlaqlwepVD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503938019 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLV 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-196 |
4.42e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 145.86 E-value: 4.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEmaFLT--GHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlknreVPFLRR 79
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGE--FLTllGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH-----VPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHD 196
Cdd:PRK09452 167 LLDESLSALDYKLRKQMQNELKALQRkLGITFVFVTHD 204
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-196 |
1.50e-41 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 140.31 E-value: 1.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSkAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERP---SAGKIWFSGHDISRLknrevPFL 77
Cdd:COG4136 1 MLSLENLT-ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL-----PAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFDNV--AIPLIIAGAsydDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLafALPPTIGRA---QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503938019 156 PAVLLADEPTGNLDDALSEGILRL-FEEFNRVGVTVLMATHD 196
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHD 193
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-215 |
1.61e-41 |
|
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: 147.98 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQI 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS---WRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDrTVFDNVAipliIAGASYDDirRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLR----LGRPDASD--EELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRI 549
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-213 |
8.26e-41 |
|
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: 138.16 E-value: 8.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 3 RFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlKNRevpflRRQIG 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KER-----RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 MIFQD--HHLLMDrTVFDNVAIPLIIAGASYDDIRrrvsAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:cd03226 75 YVMQDvdYQLFTD-SVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-200 |
1.03e-40 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 137.55 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 11 YLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DISRLKNREVpflRRQIGMIFQD- 87
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLER---RQRVGLVFQDp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 88 HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
Cdd:TIGR01166 78 DDQLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180 190
....*....|....*....|....*....|...
gi 503938019 168 LDDALSEGILRLFEEFNRVGVTVLMATHDIGLI 200
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
1.11e-40 |
|
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: 138.09 E-value: 1.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGeMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpfLRRQI 81
Cdd:cd03264 1 LQLENLTKRY-GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
1.94e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 139.06 E-value: 1.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISrLKNREVPFLRRQ 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQ--DHHLLMDrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
Cdd:PRK13639 80 VGIVFQnpDDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-197 |
2.07e-40 |
|
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: 137.50 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlKNREVpflRRQI 81
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREV---RRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDI 197
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYM 192
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-216 |
3.85e-40 |
|
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: 136.51 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 3 RFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevpflRRQIG 82
Cdd:cd03235 1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 MIFQdhHLLMDR----TVFDNVAIPL-----IIAGASYDDiRRRVSAALDKVGLLDKAKNfPI-QLSGGEQQRVGIARAV 152
Cdd:cd03235 72 YVPQ--RRSIDRdfpiSVRDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSELADR-QIgELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLsDGHLH 216
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-197 |
4.60e-40 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 137.52 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIsrlknrEVPFLRRq 80
Cdd:PRK11248 1 MLQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV------EGPGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 iGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503938019 161 ADEPTGNLD----DALSEGILRLFEEfnrVGVTVLMATHDI 197
Cdd:PRK11248 152 LDEPFGALDaftrEQMQTLLLKLWQE---TGKQVLLITHDI 189
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-196 |
1.27e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 139.59 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 14 GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlknreVPFLRRQIGMIFQDHHLLMD 93
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH-----VPPYQRPINMMFQSYALFPH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
Cdd:PRK11607 106 MTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180
....*....|....*....|....
gi 503938019 174 EGI-LRLFEEFNRVGVTVLMATHD 196
Cdd:PRK11607 186 DRMqLEVVDILERVGVTCVMVTHD 209
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-198 |
4.47e-39 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 135.31 E-value: 4.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIsRLK---------- 70
Cdd:COG4598 8 ALEVRDLHKSF-GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLKpdrdgelvpa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 71 -NREVPFLRRQIGMIFQDHHLLMDRTVFDNV-AIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGI 148
Cdd:COG4598 86 dRRQLQRIRTRLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 149 ARAVVNKPAVLLADEPTGNLDDALSEGILR----LFEEfnrvGVTVLMATHDIG 198
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKvmrdLAEE----GRTMLVVTHEMG 215
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-196 |
1.12e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.51 E-value: 1.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpflrRQ 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAA---LDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAariLELEPLLDRK---PRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 158 VLLADEPTGNLDDAL-----SEgILRLFEefnRVGVTVLMATHD 196
Cdd:PRK11650 155 VFLFDEPLSNLDAKLrvqmrLE-IQRLHR---RLKTTSLYVTHD 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-215 |
2.88e-38 |
|
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: 132.46 E-value: 2.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevPFLRRQIGMIFQDHHLLMDRTVF 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL-----PPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 98 DNVAIPLIIAGASYDDIRRRVSAALDKVG---LLDKAknfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGidhLLNRK---PETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503938019 175 GILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03299 167 KLREELKKIRKeFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-213 |
3.48e-38 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 132.79 E-value: 3.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKN----------REVPFLRRQIG 82
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadkNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 MIFQDHHLLMDRTVFDNV-AIPLIIAGASYDDIRRRVSAALDKVGLLDKAK-NFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
4.82e-38 |
|
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: 131.79 E-value: 4.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAY----LGGRQ--ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF-SGH---DISRLK 70
Cdd:COG4778 4 LLEVENLSKTFtlhlQGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrHDGgwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 71 NREVPFLRRQ-IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGI 148
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-215 |
5.15e-38 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 132.89 E-value: 5.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAY-----LGGRQA---LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPF 76
Cdd:PRK10419 7 SGLSHHYahgglSGKHQHqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQDHHLLMD--RTVFDNVAIPLI-IAGASYDDIRRRVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGIARAV 152
Cdd:PRK10419 87 FRRDIQMVFQDSISAVNprKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 |
8.39e-38 |
|
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: 131.05 E-value: 8.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlknrevPFLRRQIgmIFQDHHLLMDRTVF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE------PGPDRMV--VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 98 DNVAIPL--IIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLdDALSEG 175
Cdd:TIGR01184 73 ENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL-DALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503938019 176 IL--RLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:TIGR01184 152 NLqeELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-215 |
9.31e-38 |
|
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: 130.70 E-value: 9.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQ-ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpfLRRQ 80
Cdd:cd03263 1 LQIRNLTKTYKKGTKpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA----ARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-216 |
1.26e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 132.06 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG-RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdiSRLKNREVPFLRRQ 80
Cdd:PRK13635 6 IRVEHISFRYPDAaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQD-HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:PRK13635 83 VGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISrRSYRMLTLSDGHLH 216
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAA-QADRVIVMNKGEIL 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-195 |
5.27e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 129.77 E-value: 5.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSkAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI--ERPSA---GKIWFSGHDISRlKNREVPF 76
Cdd:COG1117 12 IEVRNLN-VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGArveGEILLDGEDIYD-PDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQdhhllmdR------TVFDNVAIPLIIAG-ASYDDIRRRVSAALDKVGLLDKAKN----FPIQLSGGEQQR 145
Cdd:COG1117 90 LRRRVGMVFQ-------KpnpfpkSIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALWDEVKDrlkkSALGLSGGQQQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 146 VGIARAVVNKPAVLLADEPTGNLD----DALSEGILRLFEEFnrvgvTVLMATH 195
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDpistAKIEELILELKKDY-----TIVIVTH 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-215 |
6.96e-37 |
|
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: 129.93 E-value: 6.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGG--------RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNR 72
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 73 EVPFLRRQIGMIFQDHHLLMD--RTVFDNVAIPLI-IAGASYDDIRRRVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGI 148
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNprMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEdADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-215 |
1.10e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.03 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwFSGhdisrlkNREVPFLRRQIGMI 84
Cdd:PRK11247 16 NAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-------TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDHHLLMDRTVFDNVAIPLiiagasYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 165 TGNLdDALS-----EGILRLFEEFnrvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK11247 161 LGAL-DALTriemqDLIESLWQQH---GFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
28-196 |
1.37e-36 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 130.99 E-value: 1.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI--SRLKNREvpflrrqIGMIFQDHHLLMDRTVFDNVAIPLI 105
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD-------ICMVFQSYALFPHMSLGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 106 IAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL----SEGILRLFE 181
Cdd:PRK11432 105 MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLrrsmREKIRELQQ 184
|
170
....*....|....*
gi 503938019 182 EFNrvgVTVLMATHD 196
Cdd:PRK11432 185 QFN---ITSLYVTHD 196
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-202 |
4.13e-36 |
|
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: 132.80 E-value: 4.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrEVPFLRRQI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA---DADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQdHHLLMDRTVFDNVAIPLiiAGASYDDIRRrvsaALDKVGLLDKAK------NFPI-----QLSGGEQQRVGIAR 150
Cdd:TIGR02857 399 AWVPQ-HPFLFAGTIAENIRLAR--PDASDAEIRE----ALERAGLDEFVAalpqglDTPIgeggaGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISR 202
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL 522
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-213 |
5.00e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 127.93 E-value: 5.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpflRRQI 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQD-HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:PRK13647 82 GLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-213 |
7.64e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 127.47 E-value: 7.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG----RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlKNREVPFL 77
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQ-DHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGL-----LDKAknfPIQLSGGEQQRVGIARA 151
Cdd:PRK13637 82 RKKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyedyKDKS---PFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 152 VVNKPAVLLADEPTGNLD----DALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDpkgrDEILNKIKELHKEYN---MTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-195 |
8.61e-36 |
|
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: 126.19 E-value: 8.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnreVPFLRRQI 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDrTVFDNVAIPLIiaGASYDDIRRRVSAAldkvGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYGRP--DATDEEVIEAAKAA----QIHDKIMRFPdgydtivgergLKLSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATH 195
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRD-VSKGRTTIVIAH 194
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-214 |
8.62e-36 |
|
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: 125.62 E-value: 8.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 10 AYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRRQIGMIFQDHH 89
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 90 LLMDRTVFDNVAIpliiagASYDDIRRRVSAALDKVglLDkakNFPI----------QLSGGEQQRVGIARAVVNKPAVL 159
Cdd:cd03224 86 IFPELTVEENLLL------GAYARRRAKRKARLERV--YE---LFPRlkerrkqlagTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-213 |
1.19e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.77 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdisRLKNREVPFLRRQIGMIFQD-HHLLMDRTV 96
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIRHKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 97 FDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGI 176
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD---PEGR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503938019 177 LRLFEEFNRV----GVTVLMATHDIGLISrRSYRMLTLSDG 213
Cdd:PRK13650 177 LELIKTIKGIrddyQMTVISITHDLDEVA-LSDRVLVMKNG 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
17-213 |
2.80e-35 |
|
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: 130.57 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKSTL----LKLIcgierPSAGKIWFSGHDISRLKNREVPFLRRQIGMIFQDHHLLM 92
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 D--RTVFDNVAIPLII--AGASYDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
Cdd:COG4172 376 SprMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503938019 168 LDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:COG4172 456 LDVSVQAQILDLLRDLQrEHGLAYLFISHDLAVVRALAHRVMVMKDG 502
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-216 |
5.78e-35 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 123.92 E-value: 5.78e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSkaYLGGRQALQgVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDisrlkNREVPFLRRQ 80
Cdd:PRK10771 1 MLKLTDIT--WLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIA 209
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-215 |
6.35e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 125.33 E-value: 6.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG----RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-SRLKNREVPF 76
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQ-DHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDK-AKNFPIQLSGGEQQRVGIARAVVN 154
Cdd:PRK13641 83 LRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-213 |
7.25e-35 |
|
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: 122.99 E-value: 7.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevPFLRRQIGMIFQDHHLLMDRTVFDNVAIPLIIA 107
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-----PPADRPVSMLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 108 GASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-V 186
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAeT 178
|
170 180
....*....|....*....|....*..
gi 503938019 187 GVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
8.24e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.48 E-value: 8.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQ-ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRR 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK---LRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQD-HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
Cdd:PRK13648 84 HIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503938019 159 LLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDI 197
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDL 203
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-215 |
1.18e-34 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 123.56 E-value: 1.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLI---------CGIErpsaGKIWFSGHDISRlKNR 72
Cdd:TIGR00972 2 IEIENLNLFY-GEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndlvpgVRIE----GKVLFDGQDIYD-KKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 73 EVPFLRRQIGMIFQdHHLLMDRTVFDNVAIPLIIAGA-SYDDIRRRVSAALDKVGLL----DKAKNFPIQLSGGEQQRVG 147
Cdd:TIGR00972 76 DVVELRRRVGMVFQ-KPNPFPMSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWdevkDRLHDSALGLSGGQQQRLC 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:TIGR00972 155 IARALAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFYDGEL 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-192 |
1.55e-34 |
|
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: 122.78 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRRQ 80
Cdd:COG0410 3 MLEVENLHAGY-GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNvaipLIIAGASYDDiRRRVSAALDKVGLLdkaknFPI----------QLSGGEQQRVGIAR 150
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEEN----LLLGAYARRD-RAEVRADLERVYEL-----FPRlkerrrqragTLSGGEQQMLAIGR 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLM 192
Cdd:COG0410 150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-202 |
2.89e-34 |
|
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: 127.88 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKS----TLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLR-RQIGMIFQD 87
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 88 -------HHllmdrTVFDNVAIPLII-AGASYDDIRRRVSAALDKVGLLD---KAKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:COG4172 101 pmtslnpLH-----TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503938019 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISR 202
Cdd:COG4172 176 DLLIADEPTTALDVTVQAQILDLLKDLQReLGMALLLITHDLGVVRR 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-195 |
4.49e-34 |
|
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: 121.50 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevPFLRR-Q 80
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-----PMHKRaR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIF--QDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
Cdd:cd03218 75 LGIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 503938019 159 LLADEPTGNLDD-ALSEgILRLFEEFNRVGVTVLMATH 195
Cdd:cd03218 155 LLLDEPFAGVDPiAVQD-IQKIIKILKDRGIGVLITDH 191
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-198 |
5.27e-34 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 121.78 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF------SGHDISRLKNReV 74
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGL-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 75 PFLRRQIGMIFQDHHLLMDRTVFDNVAI-PLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
Cdd:PRK11264 81 RQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503938019 154 NKPAVLLADEPTGNLDDALSEGIL---RLFEEFNRvgvTVLMATHDIG 198
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLntiRQLAQEKR---TMVIVTHEMS 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-195 |
7.01e-34 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 126.29 E-value: 7.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGE-MAfLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRR 79
Cdd:COG1129 4 LLEMRGISKSF-GGVKALDGVSLELRPGEvHA-LLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA--QAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQDHHLLMDRTVFDNVAIPLIIAGA---SYDDIRRRVSAALDKVGL-LD---KAKNfpiqLSGGEQQRVGIARAV 152
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLdIDpdtPVGD----LSVAQQQLVEIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISH 198
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-221 |
9.27e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 122.26 E-value: 9.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DISRlknREVPFLR 78
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSR---KGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 79 RQIGMIFQD-HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGlLDKAKNFPIQ-LSGGEQQRVGIARAVVNKP 156
Cdd:PRK13636 82 ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTG-IEHLKDKPTHcLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 157 AVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH--LHGGLGE 221
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEGRviLQGNPKE 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-213 |
2.03e-33 |
|
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: 118.09 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQA-LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLmDRTVFDNVaipliiagasyddirrrvsaaldkvglldkaknfpiqLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:cd03246 78 VGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyRMLTLSDG 213
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASAD-RILVLEDG 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
23-215 |
2.18e-33 |
|
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: 119.32 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 23 FHLQ-----PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DISRlKNREVPFLRRQIGMIFQDHHLLMDRT 95
Cdd:cd03297 13 FTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSR-KKINLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 96 VFDNVAIPLiiAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEG 175
Cdd:cd03297 92 VRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503938019 176 ILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03297 170 LLPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-214 |
4.79e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 121.35 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQIGMIFQD--HHLLMD 93
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNVAIPLII--AGASYDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
Cdd:PRK15079 115 MTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPNLINrYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 171 ALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:PRK15079 195 SIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-212 |
5.03e-33 |
|
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: 118.46 E-value: 5.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG-RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDrTVFDNVAipliIAGASYDDirRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIA 149
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNIT----LGAPLADD--ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 150 RAVVNKPAVLLADEPTGNLDDALSEgilRLFEEFNRV--GVTVLMATHdiglisrrSYRMLTLSD 212
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEE---RLKERLRQLlgDKTLIIITH--------RPSLLDLVD 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-213 |
6.24e-33 |
|
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: 117.77 E-value: 6.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnrevpflRRQI 81
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------RNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-196 |
1.18e-32 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 117.51 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQIGMIFQDHHLL 91
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 MDrTVFDNVAIPLIIAGASYDdiRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
Cdd:PRK10247 94 GD-TVYDNLIFPWQIRNQQPD--PAIFLDDLERFALPDTILTKNIaELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190
....*....|....*....|....*....|
gi 503938019 171 A----LSEGILRLFEEFNrvgVTVLMATHD 196
Cdd:PRK10247 171 SnkhnVNEIIHRYVREQN---IAVLWVTHD 197
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-213 |
1.61e-32 |
|
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: 117.72 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLG-GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDrTVFDNVAIPLiiAGASYDDIRRRVSAAldkvGLLDKAKNFP-----------IQLSGGEQQRVGIA 149
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGR--PGATREEVEEAARAA----NAHEFIMELPegydtvigergVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 150 RAVVNKPAVLLADEPTGNLD----DALSEGILRLFEefNRvgvTVLMATHDIGLIsRRSYRMLTLSDG 213
Cdd:cd03251 151 RALLKDPPILILDEATSALDteseRLVQAALERLMK--NR---TTFVIAHRLSTI-ENADRIVVLEDG 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-213 |
3.08e-32 |
|
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: 116.56 E-value: 3.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQI 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLmDRTVFDN------------VAIPLIIAGAsyDDIRRRVSAALDKVgLLDKAKNfpiqLSGGEQQRVGIA 149
Cdd:cd03254 80 GVVLQDTFLF-SGTIMENirlgrpnatdeeVIEAAKEAGA--HDFIMKLPNGYDTV-LGENGGN----LSQGERQLLAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 150 RAVVNKPAVLLADEPTGNLD----DALSEGILRLFEefnrvGVTVLMATHDIGLIsRRSYRMLTLSDG 213
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDteteKLIQEALEKLMK-----GRTSIIIAHRLSTI-KNADKILVLDDG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-214 |
4.42e-32 |
|
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: 119.44 E-value: 4.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 21 VTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH---DISRLKNreVPFLRRQIGMIFQDHHLLMDRTVF 97
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIF--LPPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 98 DNVA-----IPLIIAGASYDDirrrVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
Cdd:COG4148 96 GNLLygrkrAPRAERRISFDE----VVELLGIGHLLDR---RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503938019 173 SEGIL----RLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:COG4148 169 KAEILpyleRLRDELD---IPILYVSHSLDEVARLADHVVLLEQGR 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
8.91e-32 |
|
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: 115.01 E-value: 8.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNrevpfLRRQI 81
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----ALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRrvsaALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 162 DEPTGNLD-DALSEgILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03268 151 DEPTNGLDpDGIKE-LRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-214 |
1.15e-31 |
|
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: 115.57 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGK-IWFSGHdisRLKNREVPFLRR 79
Cdd:COG1119 3 LLELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGE---RRGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQDHHLLMDR--TVFDnvaiplIIAGASYDDI----------RRRVSAALDKVGLLDKA-KNFPiQLSGGEQQRV 146
Cdd:COG1119 79 RIGLVSPALQLRFPRdeTVLD------VVLSGFFDSIglyreptdeqRERARELLELLGLAHLAdRPFG-TLSQGEQRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 147 GIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVG-VTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-196 |
1.93e-31 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 117.82 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 7 VSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISrlknrEVPFLRRQIGMIFQ 86
Cdd:PRK11000 9 VTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 87 DHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAA---LDKVGLLDKAknfPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVaevLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 503938019 164 PTGNLDDAL-----SEgILRLFEefnRVGVTVLMATHD 196
Cdd:PRK11000 160 PLSNLDAALrvqmrIE-ISRLHK---RLGRTMIYVTHD 193
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-195 |
2.24e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.01 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 9 KAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDISRLknrEVPFLRRQIGM 83
Cdd:PRK14247 10 KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM---DVIELRRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 84 IFQDHHLLMDRTVFDNVAIPLII--AGASYDDIRRRVSAALDKVGLLDKAKN---FPI-QLSGGEQQRVGIARAVVNKPA 157
Cdd:PRK14247 87 VFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLWDEVKDrldAPAgKLSGGQQQRLCIARALAFQPE 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATH 195
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTH 203
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-169 |
2.83e-31 |
|
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: 119.82 E-value: 2.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLG-GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS---LRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDrTVFDNVAIPLIiAGASYDDIRRRVSAA--LDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAVV 153
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAYGRT-EQADRAEIERALAAAyaQDFVDKLPLGLDTPIgengvLLSGGQRQRLAIARALL 485
|
170
....*....|....*.
gi 503938019 154 NKPAVLLADEPTGNLD 169
Cdd:TIGR02203 486 KDAPILILDEATSALD 501
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-215 |
3.20e-31 |
|
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: 119.47 E-value: 3.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQA-LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLkNREVpfLRRQ 80
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-DREE--LGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLmDRTVFDNVAipliiagaSYDDI-RRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGI 148
Cdd:COG4618 408 IGYLPQDVELF-DGTIAENIA--------RFGDAdPEKVVAAAKLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 149 ARAVVNKPAVLLADEPTGNLDD----ALSEGILRLFEEfnrvGVTVLMATHDIGLISrRSYRMLTLSDGHL 215
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLDDegeaALAAAIRALKAR----GATVVVITHRPSLLA-AVDKLLVLRDGRV 544
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-202 |
1.27e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 114.05 E-value: 1.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEM-AFLtGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnrevpflRR 79
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIfGLL-GPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED-------RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIG-----------MifqdhhllmdrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNfPIQ-LSGGEQQRVG 147
Cdd:COG4152 72 RIGylpeerglypkM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANK-KVEeLSKGNQQKVQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 148 IARAVVNKPAVLLADEPTGNLD----DALSEGILrlfeEFNRVGVTVLMATHDIGLISR 202
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDpvnvELLKDVIR----ELAAKGTTVIFSSHQMELVEE 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.31e-30 |
|
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: 110.60 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRRQI 81
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA--RRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFqdhhllmdrtvfdnvaipliiagasyddirrrvsaaldkvglldkaknfpiQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03216 78 AMVY---------------------------------------------------QLSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-164 |
1.50e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.43 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrevP-FLRR 79
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-----PmHKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIF--QDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:COG1137 77 RLGIGYlpQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
....*..
gi 503938019 158 VLLADEP 164
Cdd:COG1137 157 FILLDEP 163
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
15-214 |
2.14e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 112.62 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdisRLKNREVPFLRRQIGMIFQDhhllmDR 94
Cdd:COG4167 26 FEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGDYKYRCKHIRMIFQD-----PN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFD---NVA----IPLIIAgASYDDIRR--RVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEP 164
Cdd:COG4167 98 TSLNprlNIGqileEPLRLN-TDLTAEEReeRIFATLRLVGLLPEHANFYPHmLSSGQKQRVALARALILQPKIIIADEA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503938019 165 TGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:COG4167 177 LAALDMSVRSQIINLMLELQeKLGISYIYVSQHLGIVKHISDKVLVMHQGE 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-210 |
2.40e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.79 E-value: 2.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdisrlknrevpflrRQIGMIFQdhHLLM 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--------------ARVAYVPQ--RSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DR----TVFDNVAI----PLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
Cdd:NF040873 67 PDslplTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503938019 165 TGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLIsRRSYRMLTL 210
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-214 |
2.98e-30 |
|
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: 111.86 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLG--GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLIcgiER---PSAGKIWFSGHDISRLKNRevpF 76
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDLNLR---W 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQDHHLlMDRTVFDNvaipliIAGASYDDIRRRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQR 145
Cdd:cd03249 75 LRSQIGLVSQEPVL-FDGTIAEN------IRYGKPDATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 146 VGIARAVVNKPAVLLADEPTGNLdDALSEGILRlfEEFNRV--GVTVLMATHDIGLIsRRSYRMLTLSDGH 214
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSAL-DAESEKLVQ--EALDRAmkGRTTIVIAHRLSTI-RNADLIAVLQNGQ 214
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-200 |
5.88e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.14 E-value: 5.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQIGMIFQDHH--LLMD 93
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPYgsLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNVAIPLII-AGASYDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
Cdd:PRK11308 109 KKVGQILEEPLLInTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188
|
170 180 190
....*....|....*....|....*....|...
gi 503938019 172 LSEGILRLF----EEFnrvGVTVLMATHDIGLI 200
Cdd:PRK11308 189 VQAQVLNLMmdlqQEL---GLSYVFISHDLSVV 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-213 |
6.15e-30 |
|
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: 111.04 E-value: 6.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLG-GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknrEVPFLRRQ 80
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDhHLLMDRTVFDNVAipLIIAGASyddiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIA 149
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIA--LADPGMS----MERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDG 213
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV-KNADRIIVMEKG 212
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-197 |
7.85e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 111.40 E-value: 7.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQIGMIFQDHHLLM 92
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DRTVFDNVAIPLIIAGASYDDI-RRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP-TGNldD 170
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLlHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPfVGQ--D 175
|
170 180
....*....|....*....|....*....
gi 503938019 171 ALSEGIL-RLFEEFNR-VGVTVLMATHDI 197
Cdd:PRK11831 176 PITMGVLvKLISELNSaLGVTCVVVSHDV 204
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-196 |
1.22e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.78 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 4 FEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdisrlknrevpfLRrqIGM 83
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------------LR--IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 84 IFQDHHLLMDRTVFDNVA---IPLIIAGASYD-----------------------------DIRRRVSAALDKVGLLDKA 131
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLdgdAELRALEAELEeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEED 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 132 KNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLfEEF--NRVGvTVLMATHD 196
Cdd:COG0488 146 LDRPVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWL-EEFlkNYPG-TVLVVSHD 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-195 |
1.26e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG----RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-SRLKNREVPF 76
Cdd:PRK13649 3 INLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQ-DHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDK--AKNfPIQLSGGEQQRVGIARAVV 153
Cdd:PRK13649 83 IRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlfEKN-PFELSGGQMRRVAIAGILA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503938019 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-207 |
1.53e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 111.92 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPS----AGKIWFSGHDISRL---KNREVpfLRRQIGMIFQDH 88
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLsprERRKI--IGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 89 HLLMD--RTVFDNV--AIPLIIAGASY----DDIRRRVSAALDKVGLLD-KA--KNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:COG4170 99 SSCLDpsAKIGDQLieAIPSWTFKGKWwqrfKWRKKRAIELLHRVGIKDhKDimNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRM 207
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTI 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-215 |
2.13e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 110.10 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI---ERPSAGKIWFSGHDISRLKN--REVP 75
Cdd:PRK09984 4 IIRVEKLAKTF-NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaRDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 76 FLRRQIGMIFQDHHLLMDRTVFDNVAI------PLIIAGASY--DDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVG 147
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSWftREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-215 |
2.89e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 110.59 E-value: 2.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLG----GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDI---SRLKNRE 73
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsSTSKQKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 74 VPFLRRQIGMIFQ-DHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLldkAKNF----PIQLSGGEQQRVGI 148
Cdd:PRK13643 79 IKPVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL---ADEFweksPFELSGGQMRRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK13643 156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-196 |
3.50e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGG-RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnreVPFLRR 79
Cdd:PRK13632 7 MIKVENVSFSYPNSeNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQ--DHHLLmDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:PRK13632 84 KIGIIFQnpDNQFI-GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGV-TVLMATHD 196
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHD 202
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
7.23e-29 |
|
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: 107.94 E-value: 7.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLG--GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpFLRR 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQDhHLLMDRTVFDNVAIPLiiAGASYDdirrRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVGI 148
Cdd:cd03248 89 KVSLVGQE-PVLFARSLQDNIAYGL--QSCSFE----CVKEAAQKAHAHSFISELASgydtevgekgsQLSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-169 |
8.36e-29 |
|
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: 112.99 E-value: 8.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIsrlknREVP--FLRR 79
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDI-----RDVTqaSLRA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQDHHLLMDrTVFDNVAIPLiiAGASYDDIRRRVSAA-LD------------KV---GLldkaknfpiQLSGGEQ 143
Cdd:COG5265 433 AIGIVPQDTVLFND-TIAYNIAYGR--PDASEEEVEAAARAAqIHdfieslpdgydtRVgerGL---------KLSGGEK 500
|
170 180
....*....|....*....|....*.
gi 503938019 144 QRVGIARAVVNKPAVLLADEPTGNLD 169
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALD 526
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-214 |
8.42e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.47 E-value: 8.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG-----HDISRLKNREVPFL-R 78
Cdd:PRK11701 10 RGLTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRLlR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 79 RQIGMIFQD--HHLLMDRTVFDNVAIPLIIAGAS-YDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVN 154
Cdd:PRK11701 89 TEWGFVHQHprDGLRMQVSAGGNIGERLMAVGARhYGDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 155 KPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
1.19e-28 |
|
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: 112.07 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpflRRQI 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLmDRTVFDNVAIPLiiAGASYDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENLRLAR--PDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHD 196
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHH 529
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-213 |
1.60e-28 |
|
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: 107.61 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWF-----SGHDISRLKNREVP 75
Cdd:TIGR02323 3 LLQVSGLSKSY-GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrsgAELELYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 76 FL-RRQIGMIFQDHH--LLMDRTVFDNVAIPLIIAGAS-YDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIAR 150
Cdd:TIGR02323 82 RLmRTEWGFVHQNPRdgLRMRVSAGANIGERLMAIGARhYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRdLGLAVIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-195 |
1.79e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 108.18 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG----RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIS-RLKNREVPF 76
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQ-DHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGL----LDKAknfPIQLSGGEQQRVGIARA 151
Cdd:PRK13634 83 LRKKVGIVFQfPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpeelLARS---PFELSGGQMRRVAIAGV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATH 195
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTH 204
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-195 |
1.83e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.25 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQ-----ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNreVP 75
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 76 FLRRQIGMIFQD-HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503938019 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATH 195
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITH 203
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-195 |
1.84e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 111.84 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQ-ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDrTVFDNvaipLIIAGASYDDirRRVSAALDKVGL-----LDKAKNFPI-----QLSGGEQQRVGIAR 150
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLeklleDDKGLNAWLgeggrQLSGGEQRRLGIAR 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATH 195
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITH 532
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-195 |
1.90e-28 |
|
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: 105.47 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLG-GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpfLRRQ 80
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLmDRTVFDNVAipliiagasyddirrrvsaaldkvglldkaknfpIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190
....*....|....*....|....*....|....*
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATH 195
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITH 155
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-169 |
1.93e-28 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.98 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLkNREVpfLRRQI 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV-TRAS--LRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDhHLLMDRTVFDNVAIPLiiAGASYDDIRR--RVSAALDKVglLDKAKNFPI-------QLSGGEQQRVGIARAV 152
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNIRVGR--PDATDEEMRAaaERAQAHDFI--ERKPDGYDTvvgergrQLSGGERQRLAIARAL 486
|
170
....*....|....*..
gi 503938019 153 VNKPAVLLADEPTGNLD 169
Cdd:PRK13657 487 LKDPPILILDEATSALD 503
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-215 |
2.45e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 111.87 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQIGMIFQDHHLLMD--R 94
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASLDprQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFDNVAIPLIIAG-ASYDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
Cdd:PRK10261 419 TVGDSIMEPLRVHGlLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 173 SEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK10261 499 RGQIINLLLDLQRdFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-195 |
2.70e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 2.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEM-AFLtGHSGAGKSTLLKLICGIERPSAGKIWFSGhdisrlknREVPF--- 76
Cdd:COG3845 5 ALELRGITKRF-GGVVANDDVSLTVRPGEIhALL-GENGAGKSTLMKILYGLYQPDSGEILIDG--------KPVRIrsp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 ---LRRQIGMIFQdHHLLMDR-TVFDNVAI---PLIIAGASYDDIRRRVSAALDKVGL---LDKaknfPI-QLSGGEQQR 145
Cdd:COG3845 75 rdaIALGIGMVHQ-HFMLVPNlTVAENIVLglePTKGGRLDRKAARARIRELSERYGLdvdPDA----KVeDLSVGEQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503938019 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:COG3845 150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-215 |
9.45e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 106.42 E-value: 9.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG-RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSA---GKIWFSGhdiSRLKNREVPFL 77
Cdd:PRK13640 6 VEFKHVSFTYPDSkKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDG---ITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQD-HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:PRK13640 83 REKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 157 AVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEANMAD-QVLVLDDGKL 221
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-215 |
1.12e-27 |
|
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: 105.11 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpfLRRQIGMIF-QDHHLLMDRT 95
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK----FLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 96 VFDNVAIPLIIAGASYDDIRRRV---SAALDKVGLLDKaknfPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLdelSELLDLEELLDT----PVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 172 LSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03267 188 AQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-200 |
1.77e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 105.66 E-value: 1.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpflRRQ 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV---RKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQD-HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:PRK13652 80 VGLVFQNpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 160 LADEPTGNLDdalSEGILRLFEEFNRV----GVTVLMATHDIGLI 200
Cdd:PRK13652 160 VLDEPTAGLD---PQGVKELIDFLNDLpetyGMTVIFSTHQLDLV 201
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-197 |
2.01e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 105.45 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnrEVPFLRRQ 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHL-LMDRTV-----F--DNVAIPLIiagasydDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
Cdd:PRK13644 79 VGIVFQNPETqFVGRTVeedlaFgpENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNL 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-216 |
2.98e-27 |
|
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: 103.60 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAY---LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnREVpfl 77
Cdd:cd03266 1 MITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-AEA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-197 |
3.45e-27 |
|
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: 107.97 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYL----GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFS-GH---DISRLKNR 72
Cdd:TIGR03269 279 IIKVRNVSKRYIsvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 73 EVPFLRRQIGMIFQDHHLLMDRTVFDNV--AIPLIIAgasyDDI-RRRVSAALDKVGLLD-KAKN----FPIQLSGGEQQ 144
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLteAIGLELP----DELaRMKAVITLKMVGFDEeKAEEildkYPDELSEGERH 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 145 RVGIARAVVNKPAVLLADEPTGNLD----DALSEGILRLFEEFNRvgvTVLMATHDI 197
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQ---TFIIVSHDM 488
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-213 |
5.01e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 103.62 E-value: 5.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRE---LAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAI---PliiagasY-------DDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIAR 150
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFgrfP-------YskgrltaED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGIL----RLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMkllrRLADELGK---TVVIVLHDINFASCYADHIVAMKDG 212
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-215 |
5.83e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 104.78 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGR----QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-WFSGHD----------- 65
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 66 ------ISRLKNREVPF---LRRQIGMIFQ-DHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGL----LDKA 131
Cdd:PRK13651 83 vleklvIQKTRFKKIKKikeIRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdesyLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 132 knfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
Cdd:PRK13651 163 ---PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
....
gi 503938019 212 DGHL 215
Cdd:PRK13651 240 DGKI 243
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-215 |
1.37e-26 |
|
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: 100.58 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpFLRRQIGMIFQDHH-- 89
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD--AIRAGIAYVPEDRKre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 90 -LLMDRTVFDNVAIpliiagasyddirrrvsaaldkvglldkaknfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
Cdd:cd03215 88 gLVLDLSVAENIAL--------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503938019 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-195 |
1.77e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlknrEVPFLRRQI 81
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190
....*....|....*....|....*....|....
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTH 196
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-215 |
3.21e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.96 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLG--GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpFLRR 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH---YLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQDHhLLMDRTVFDNVAIPLiiAGASYDDIRR--RVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIARAV 152
Cdd:TIGR00958 556 QVALVGQEP-VLFSGSVRENIAYGL--TDTPDEEIMAaaKAANAHDFIMEFPNGYDTEVgekgsQLSGGQKQRIAIARAL 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503938019 153 VNKPAVLLADEPTGNLdDALSEGILRlfEEFNRVGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215
Cdd:TIGR00958 633 VRKPRVLILDEATSAL-DAECEQLLQ--ESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSV 691
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-215 |
3.68e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 3.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 11 YLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKL------ICGIERPSAGKIWFSGHDISRLKNREvpfLRRQIGMI 84
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIK---LRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDHHLLMDRTVFDNVAIPLIIAG-ASYDDIRRRVSAALDKVGLL----DKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:PRK14246 96 FQQPNPFPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-216 |
3.88e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.15 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsGHDIsrlknrevpflrrQ 80
Cdd:COG0488 315 VLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------------K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLL-MDRTVFDNvaipliIAGASYDDIRRRVSAAL-------DKVglLDKAKNfpiqLSGGEQQRVGIARAV 152
Cdd:COG0488 380 IGYFDQHQEELdPDKTVLDE------LRDGAPGGTEQEVRGYLgrflfsgDDA--FKPVGV----LSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 153 VNKPAVLLADEPTGNLD----DALSEGIlrlfEEFNrvGvTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDietlEALEEAL----DDFP--G-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-215 |
3.96e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 102.09 E-value: 3.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdisRLKNREVPFLRRQIGMIFQD-HHLLMDRTV 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 97 FDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503938019 177 LRLFEEF-NRVGVTVLMATHDIGLISrRSYRMLTLSDGHL 215
Cdd:PRK13642 180 MRVIHEIkEKYQLTVLSITHDLDEAA-SSDRILVMKAGEI 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-221 |
4.39e-26 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.62 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnREVPFLRRQIGMIFQDHHLLMDRT 95
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQQVATVFQDPEQQIFYT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 96 VFD-NVAIPLIIAGASYDDIRRRVSAALDkvgLLDkAKNF---PIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
Cdd:PRK13638 94 DIDsDIAFSLRNLGVPEAEITRRVDEALT---LVD-AQHFrhqPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 171 ALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL--HGGLGE 221
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQIltHGAPGE 222
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-215 |
4.95e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 101.01 E-value: 4.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 11 YLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDISRLKNREVPfLRRQIGMIF 85
Cdd:PRK14239 14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTVD-LRKEIGMVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 86 QDHHLLmDRTVFDNVAIPLIIAGASYDDI-RRRVSAALDKVGLLDKAKNF----PIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:PRK14239 93 QQPNPF-PMSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIWDEVKDRlhdsALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 161 ADEPTGNLD----DALSEGILRLFEEFnrvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK14239 172 LDEPTSALDpisaGKIEETLLGLKDDY-----TMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-215 |
5.07e-26 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.96 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQ-IGMIFQDHHLLMDRT 95
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 96 VFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD----DA 171
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 172 LSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK10070 203 MQDELVKLQAKHQR---TIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
33-217 |
5.37e-26 |
|
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: 102.88 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 33 LTGHSGAGKSTLLKLICGIERPSAGKI------WFSGHdisrlKNREVPFLRRQIGMIFQDHHLLMDRTVFDNVAIPLII 106
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtLFDSR-----KGIFLPPEKRRIGYVFQEARLFPHLSVRGNLRYGMKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 107 AGASYDDIR-RRVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL----RLFE 181
Cdd:TIGR02142 103 ARPSERRISfERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILpyleRLHA 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 182 EFNrvgVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
Cdd:TIGR02142 180 EFG---IPILYVSHSLQEVLRLADRVVVLEDGRVAA 212
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-216 |
5.47e-26 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 104.74 E-value: 5.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQ-ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLkNREvpFLRRQ 80
Cdd:TIGR01842 317 LSVENVTIVPPGGKKpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRE--TFGKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLlMDRTVFDNVAIpliiAGASYDDirRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIA 149
Cdd:TIGR01842 394 IGYLPQDVEL-FPGTVAENIAR----FGENADP--EKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQRQRIALA 466
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHLH 216
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDK-ILVLQDGRIA 532
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-197 |
5.63e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 101.32 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGG----RQALQGVTFHLQPGEmaFLT--GHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnrev 74
Cdd:COG1101 1 MLELKNLSKTFNPGtvneKRALDGLNLTIEEGD--FVTviGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 75 PFLR-RQIGMIFQDHhlLM----DRTVFDNVAI--------PLIIA--GASYDDIRRRVsAALD---------KVGLldk 130
Cdd:COG1101 75 EYKRaKYIGRVFQDP--MMgtapSMTIEENLALayrrgkrrGLRRGltKKRRELFRELL-ATLGlglenrldtKVGL--- 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 131 aknfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDI 197
Cdd:COG1101 149 -------LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNM 209
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-204 |
7.66e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 7.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 9 KAYLGGRQALQGVTFHLqPGEMAF-LTGHSGAGKSTLLK-----LICGIERPSAGKIWFSGHDISRLKNREVPfLRRQIG 82
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKI-PQNGVFaLMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDPIE-VRREVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 MIFQDHHLLMDRTVFDNVAIPLIIAG--ASYDDIRRRVSAALDKVGLLDKAKN----FPIQLSGGEQQRVGIARAVVNKP 156
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503938019 157 AVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRS 204
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVS 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-195 |
8.67e-26 |
|
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: 98.78 E-value: 8.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICG-IERPSA-GKIWFSGHDISRLKnrevpfLRR 79
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRPLDKRS------FRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQDHHLLMDRTVFDNVaipliiagasyddirrRVSAALDkvglldkaknfpiQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETL----------------MFAAKLR-------------GLSGGERKRVSIALELVSNPSLL 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-204 |
2.06e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 99.73 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI-----ERPSAGKIWFSGHDISRLK---NRe 73
Cdd:PRK14258 8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRvnlNR- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 74 vpfLRRQIGMIFQDHHLLmDRTVFDNVAIPLIIAG----ASYDDIrrrVSAALDKVGLLDKAKN----FPIQLSGGEQQR 145
Cdd:PRK14258 86 ---LRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGwrpkLEIDDI---VESALKDADLWDEIKHkihkSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRS 204
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLS 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-213 |
2.52e-25 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 99.29 E-value: 2.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPflRRQIGMIFQDHHLLM 92
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RMGVVRTFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DRTVFDN--VA---------IPLIIAGASYddiRRRVSAA-------LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
Cdd:PRK11300 94 EMTVIENllVAqhqqlktglFSGLLKTPAF---RRAESEAldraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503938019 155 KPAVLLADEPTGNLD----DALSEGILRLFEEFnrvGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK11300 171 QPEILMLDEPAAGLNpketKELDELIAELRNEH---NVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-216 |
3.21e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.46 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPflrRQIGMIFQDHHLL 91
Cdd:PRK09536 13 FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RRVASVPQDTSLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 MD---RTVFDNVAIPLI--IAGASYDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
Cdd:PRK09536 90 FEfdvRQVVEMGRTPHRsrFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503938019 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVR 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-215 |
3.33e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 3.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ---LARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAI---P-LIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-197 |
6.95e-25 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 101.71 E-value: 6.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKST----LLKLIcgierPSAGKIWFSGHDISRLKNREVPFLRRQIGMIFQD- 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 88 HHLLMDR-TVFDNVAIPLIIAGASYDDIRR--RVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
Cdd:PRK15134 372 NSSLNPRlNVLQIIEEGLRVHQPTLSAAQReqQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190
....*....|....*....|....*....|....*
gi 503938019 164 PTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDI 197
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDL 486
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-213 |
7.09e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.40 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKaYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLrrQ 80
Cdd:PRK09700 5 YISMAGIGK-SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNV-----------AIPLIiagaSYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIA 149
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigrhltkkvcGVNII----DWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-207 |
8.09e-25 |
|
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: 96.66 E-value: 8.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnrevPFLRRQIGMIFQDHHLLM 92
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR----DEPHENILYLGHLPGLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DRTVFDNvaipLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
Cdd:TIGR01189 87 ELSALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 173 SEGILRLFEEFNRVGVTVLMATH-DIGLISRRSYRM 207
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTHqDLGLVEARELRL 198
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-197 |
8.99e-25 |
|
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: 96.79 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAY-LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQ 80
Cdd:cd03244 3 IEFKNVSLRYrPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD---LRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHhLLMDRTVFDNVAiPLiiaGASYDDirrRVSAALDKVGLLDKAKNFPIQL-----------SGGEQQRVGIA 149
Cdd:cd03244 80 ISIIPQDP-VLFSGTIRSNLD-PF---GEYSDE---ELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503938019 150 RAVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNrvGVTVLMATHDI 197
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKtIREAFK--DCTVLTIAHRL 198
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-197 |
1.97e-24 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 96.57 E-value: 1.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPflRRQIGMI 84
Cdd:TIGR04406 5 ENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERA--RLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDHHLLMDRTVFDNV-AIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
Cdd:TIGR04406 82 PQEASIFRKLTVEENImAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190
....*....|....*....|....*....|....
gi 503938019 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNV 195
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
2.66e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.10 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRRQ 80
Cdd:PRK11614 5 MLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNVAIPLIIAG-ASYDDIRRRVSAALDKvgLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGFFAErDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK11614 160 LLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
12-215 |
2.78e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 96.45 E-value: 2.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRqaLQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIErPSAGKIWFSGHDISRLKNREvpfLRRQIGMIFQDHHLL 91
Cdd:COG4138 8 VAGR--LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAE---LARHRAYLSQQQSPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 MDRTVFDNVAIPLiIAGASYDDIRRRVSAALDKVGLLDKAkNFPI-QLSGGEQQRVGIARAV------VN-KPAVLLADE 163
Cdd:COG4138 82 FAMPVFQYLALHQ-PAGASSEAVEQLLAQLAEALGLEDKL-SRPLtQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503938019 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKL 211
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-197 |
3.42e-24 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 95.69 E-value: 3.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 23 FHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdisrlknREVPFLRRQIGMIFQDHHLLMDRTVfdNVAI 102
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG--------ASPGKGWRHIGYVPQRHEFAWDFPI--SVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 103 PLIIAGASYDDIRRR--------VSAALDKVGLLDKAkNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
Cdd:TIGR03771 71 TVMSGRTGHIGWLRRpcvadfaaVRDALRRVGLTELA-DRPVgELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQ 149
|
170 180
....*....|....*....|....
gi 503938019 174 EGILRLFEEFNRVGVTVLMATHDI 197
Cdd:TIGR03771 150 ELLTELFIELAGAGTAILMTTHDL 173
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
13-207 |
1.03e-23 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 96.41 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIE----RPSAGKIWFSGHDISRLKNREvpfLRRQIG----MI 84
Cdd:PRK15093 18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRE---RRKLVGhnvsMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDHHLLMDRTvfDNVAIPLI--IAGASYDDI--------RRRVSAALDKVGLLDKA---KNFPIQLSGGEQQRVGIARA 151
Cdd:PRK15093 95 FQEPQSCLDPS--ERVGRQLMqnIPGWTYKGRwwqrfgwrKRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 152 VVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRM 207
Cdd:PRK15093 173 LANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKI 229
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-215 |
1.25e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.92 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEM-AFLtGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpfLRRQIGMIF-QDHHLLMD 93
Cdd:COG4586 36 EAVDDISFTIEPGEIvGFI-GPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKE----FARRIGVVFgQRSQLWWD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 rtvfdnvaIPLI--------IAGASYDDIRRRV---SAALDKVGLLDKaknfPI-QLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:COG4586 111 --------LPAIdsfrllkaIYRIPDAEYKKRLdelVELLDLGELLDT----PVrQLSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
16-213 |
1.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.46 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-SRLKN-REVPFLRRQIGMIFQ--DHHLL 91
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKiKEVKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 MDrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
Cdd:PRK13645 105 QE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 171 ALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK13645 184 KGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-214 |
1.37e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 96.44 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISrlknREVPFLRRQI 81
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP----ARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-211 |
1.47e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 93.33 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLknREVpfLRRQigMIFQDHHLLM 92
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ--RDE--YHQD--LLYLGHQPGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DR--TVFDNVAIPLIIAGASYDDIRRrvsAALDKVGLLDKAkNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
Cdd:PRK13538 86 KTelTALENLRFYQRLHGPGDDEALW---EALAQVGLAGFE-DVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 170 DALSEGILRLFEEFNRVGVTVLMATH-DIGLISRRsYRMLTLS 211
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGGMVILTTHqDLPVASDK-VRKLRLG 203
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
10-207 |
1.63e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 10 AYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIsrlknrEVPFLRRQIGMIfqDHH 89
Cdd:PRK13539 10 CVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEACHYL--GHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 90 LLMDR--TVFDNvaipLIIAGASYDDIRRRVSAALDKVGLLD----KAKNfpiqLSGGEQQRVGIAR-AVVNKPAVLLaD 162
Cdd:PRK13539 82 NAMKPalTVAEN----LEFWAAFLGGEELDIAAALEAVGLAPlahlPFGY----LSAGQKRRVALARlLVSNRPIWIL-D 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503938019 163 EPTGNLDDALSEGILRLFEEFNRVGVTVLMATH-DIGLISRRSYRM 207
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLPGARELDL 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-216 |
2.72e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 93.61 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAY-------------LGGRQ--------ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI 59
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelLLRRRrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 60 WFSGhdisrlknREVPFLrrQIGMIFQdhhllMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGlLDKAKNFPIQ-L 138
Cdd:COG1134 84 EVNG--------RVSALL--ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAE-LGDFIDQPVKtY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 139 SGGEQQRVGIARAVVNKPAVLLADEptgnlddALSEG-------ILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDE-------VLAVGdaafqkkCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLE 220
|
....*
gi 503938019 212 DGHLH 216
Cdd:COG1134 221 KGRLV 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-182 |
4.11e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.80 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIerpsagkiWFSGH-DISRLKNREVPFLRR 79
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGL--------WPYGSgRIARPAGARVLFLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 Q----IGmifqdhhllmdrTVFDNVAIPLiiAGASYDDirRRVSAALDKVGL------LDKAKNFPIQLSGGEQQRVGIA 149
Cdd:COG4178 434 RpylpLG------------TLREALLYPA--TAEAFSD--AELREALEAVGLghlaerLDEEADWDQVLSLGEQQRLAFA 497
|
170 180 190
....*....|....*....|....*....|...
gi 503938019 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEE 182
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-195 |
6.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 94.15 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW----FSGHDISRLKNREVPF---------LRRQIGM 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdiYIGDKKNNHELITNPYskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 84 IFQ--DHHLLMDrTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGL----LDKAknfPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLddsyLERS---PFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190
....*....|....*....|....*....|....*...
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITH 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-213 |
2.26e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.77 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdisRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDYSYRSQRIRMIFQDPSTSLNpr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNVAIPLII-AGASYDDIRRRVSAALDKVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA 171
Cdd:PRK15112 104 QRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 172 LSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK15112 184 MRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-213 |
2.32e-22 |
|
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: 94.48 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIE--RPSAGKIW----------------FSG 63
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIyhvalcekcgyverpsKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 64 HDISR----LKNREVPF----------LRRQIGMIFQDHHLLM-DRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLL 128
Cdd:TIGR03269 80 EPCPVcggtLEPEEVDFwnlsdklrrrIRKRIAIMLQRTFALYgDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 129 DKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD--------DALSEGIlrlfeefNRVGVTVLMATHDIGLI 200
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDpqtaklvhNALEEAV-------KASGISMVLTSHWPEVI 232
|
250
....*....|...
gi 503938019 201 SRRSYRMLTLSDG 213
Cdd:TIGR03269 233 EDLSDKAIWLENG 245
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-216 |
2.39e-22 |
|
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: 90.67 E-value: 2.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYL---------------------GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW 60
Cdd:cd03220 1 IELENVSKSYPtykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 61 FSGhdisrlknREVPFLRRQIGMifqdhhlLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGlLDKAKNFPI-QLS 139
Cdd:cd03220 81 VRG--------RVSSLLGLGGGF-------NPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSE-LGDFIDLPVkTYS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 140 GGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-204 |
3.82e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.00 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSkAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLK-------LICGIErpSAGKIWFSGHDI--SRLKNR 72
Cdd:PRK14243 11 LRTENLN-VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLyaPDVDPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 73 EVpflRRQIGMIFQDHHLLmDRTVFDNVAIPLIIAG--ASYDDIRRRV--SAAL-DKVGllDKAKNFPIQLSGGEQQRVG 147
Cdd:PRK14243 88 EV---RRRIGMVFQKPNPF-PKSIYDNIAYGARINGykGDMDELVERSlrQAALwDEVK--DKLKQSGLSLSGGQQQRLC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRS 204
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAARVS 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-210 |
4.71e-22 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 90.56 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghdisrlknREVPFLRrq 80
Cdd:PRK09544 4 LVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLlmDRTvfdnvaIPLIIA-------GASYDDIR---RRVSAAldkvGLLDkaknFPIQ-LSGGEQQRVGIA 149
Cdd:PRK09544 69 IGYVPQKLYL--DTT------LPLTVNrflrlrpGTKKEDILpalKRVQAG----HLID----APMQkLSGGETQRVLLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 150 RAVVNKPAVLLADEPTGNLDD----ALSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTL 210
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVngqvALYDLIDQLRRELD---CAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-215 |
6.69e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPflrRQI 81
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTVFDNVA------IPLIIAGASYDDirRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNK 155
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVArgryphQPLFTRWRKEDE--EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-215 |
1.04e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 14 GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKN----REVPFLRRQI----GMif 85
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSkafaRKVAYLPQQLpaaeGM-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 86 qdhhllmdrTVFDNVAI---PLIIAGASYD-DIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:PRK10575 101 ---------TVRELVAIgryPWHGALGRFGaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-200 |
2.77e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.23 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQ-ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIS--RLKNrevpfLR 78
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRdyTLAS-----LR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 79 RQIGMIFQDHHLLMDrTVFDNVAIPliiAGASY--DDIRR--RVSAALDKVGLLDKAKNFPI-----QLSGGEQQRVGIA 149
Cdd:PRK11176 417 NQVALVSQNVHLFND-TIANNIAYA---RTEQYsrEQIEEaaRMAYAMDFINKMDNGLDTVIgengvLLSGGQRQRIAIA 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF--NRvgvTVLMATHDIGLI 200
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELqkNR---TSLVIAHRLSTI 542
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
5-202 |
3.57e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.92 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYLGG---RQALQGVTFHLQPGEMAFLTGHSGAGKS----TLLKLIcgierPS------AGKIWFSGHDISRLKN 71
Cdd:PRK15134 9 ENLSVAFRQQqtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 72 REVPFLR-RQIGMIFQDHHLLMD--RTVFDNVAIPLII-AGASYDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQ 144
Cdd:PRK15134 84 QTLRGVRgNKIAMIFQEPMVSLNplHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKrltDYPHQLSGGERQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 145 RVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISR 202
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQeLNMGLLFITHNLSIVRK 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-202 |
4.42e-21 |
|
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: 85.19 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfSGHDIsrlknrevpflrrqi 81
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-WGSTV--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 gmifqdhhllmdrtvfdnvaipliiagasyddirrrvsaaldKVGLLDkaknfpiQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03221 64 ------------------------------------------KIGYFE-------QLSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 162 DEPTGNLD----DALSEGIlrlfEEFNRvgvTVLMATHDIGLISR 202
Cdd:cd03221 95 DEPTNHLDlesiEALEEAL----KEYPG---TVILVSHDRYFLDQ 132
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-176 |
5.01e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 87.20 E-value: 5.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 10 AYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnrevPFLRRQIGMIF--QD 87
Cdd:TIGR03410 8 VYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP----PHERARAGIAYvpQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 88 HHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAAldkvglldkaknFPI----------QLSGGEQQRVGIARAVVNKPA 157
Cdd:TIGR03410 84 REIFPRLTVEENLLTGLAALPRRSRKIPDEIYEL------------FPVlkemlgrrggDLSGGQQQQLAIARALVTRPK 151
|
170
....*....|....*....
gi 503938019 158 VLLADEPTgnlddalsEGI 176
Cdd:TIGR03410 152 LLLLDEPT--------EGI 162
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-178 |
6.44e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 90.16 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRevpFLRRQI 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDrTVFDNVAIpliiaGASYDDirRRVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVGIAR 150
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVTL-----GRDISE--EQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALAR 489
|
170 180
....*....|....*....|....*...
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILR 178
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQ 517
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
9.28e-21 |
|
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: 89.88 E-value: 9.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIeRPSA---GKIWFSGHDISRLKNREVPfl 77
Cdd:TIGR02633 1 LLEMKGIVKTF-GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIRDTE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFDNV----AIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAV 152
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-215 |
1.12e-20 |
|
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: 85.93 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQIGMIFQDHHLLMDrT 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 96 VFDNVAIPliiagASYDDirRRVSAALdkvglldKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD---DAL 172
Cdd:cd03369 98 IRSNLDPF-----DEYSD--EEIYGAL-------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDyatDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 173 SEGILRlfEEFNrvGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
Cdd:cd03369 164 IQKTIR--EEFT--NSTILTIAHRLRTIIDYD-KILVMDAGEV 201
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-217 |
1.35e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPflRRQIGMI 84
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDHHLLMDRTVFDNV-AIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
Cdd:PRK10895 84 PQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL--HG 217
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLiaHG 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-215 |
1.54e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 87.14 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGG----RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDI-SRLKNREVPF 76
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQdhhlLMDRTVF-DNVAIPLIIA----GASYDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIAR 150
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFeDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-213 |
1.95e-20 |
|
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: 89.03 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQI 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT---LRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLmDRTVFDNvaipLIIA---GASYDDIRRrvsaALDKVGLLDKAKNFPI-----------QLSGGEQQRVG 147
Cdd:TIGR01193 551 NYLPQEPYIF-SGSILEN----LLLGakeNVSQDEIWA----ACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIA 621
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFeeFNRVGVTVLMATHDIGlISRRSYRMLTLSDG 213
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLS-VAKQSDKIIVLDHG 684
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-195 |
2.09e-20 |
|
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: 85.40 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICG-IERPSA--GKIWFSGHDISRLKnrevpfLRRQIGMIFQDHHLL 91
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGGGTtsGQILFNGQPRKPDQ------FQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 MDRTVFDNVAIPLIIA-GASYDDIRRRVSAA---LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
Cdd:cd03234 94 PGLTVRETLTYTAILRlPRKSSDAIRKKRVEdvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180
....*....|....*....|....*...
gi 503938019 168 LDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-217 |
2.68e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRRQIGMIFQDHH-- 89
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDA--IRAGIAYVPEDRKge 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 90 -LLMDRTVFDNVAIPLI--IAGASYDDIRRRVSAALDKVGLLD-KAKN--FPIQ-LSGGEQQRVGIARAVVNKPAVLLAD 162
Cdd:COG1129 340 gLVLDLSIRENITLASLdrLSRGGLLDRRRERALAEEYIKRLRiKTPSpeQPVGnLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 163 EPTGNLD-DALSEgILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
Cdd:COG1129 420 EPTRGIDvGAKAE-IYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-216 |
3.14e-20 |
|
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: 88.53 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 14 GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlknrEVPFLRRQIGMIFQDHHLLMD 93
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 174 EGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:TIGR01257 1098 RSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLY 1139
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
6-216 |
1.17e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 84.21 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 6 HVSKAYLGGRqaLQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDISRLKNREVP----FLRRQI 81
Cdd:PRK03695 2 QLNDVAVSTR--LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELArhraYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFqdhhlLMDrtVFDNVAIPLIiAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAV-----VNKP 156
Cdd:PRK03695 79 TPPF-----AMP--VFQYLTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 157 A--VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
Cdd:PRK03695 151 AgqLLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-215 |
2.17e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.79 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICG-IERP---SAGKIWFSGHDISRLKNREvpflRRQI-----GMIFQ 86
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlIDYPgrvMAEKLEFNGQDLQRISEKE----RRNLvgaevAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 87 DHHLLMD--RTV-FDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:PRK11022 97 DPMTSLNpcYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASrldVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-215 |
2.42e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 6 HVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnrevPFLRRQIG--M 83
Cdd:PRK15439 16 SISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT----PAKAHQLGiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 84 IFQDHHLLMDRTVFDNVAIPLiiagASYDDIRRRVSAALD----------KVGLLDKAknfpiqlsggEQQRVGIARAVV 153
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAalgcqldldsSAGSLEVA----------DRQIVEILRGLM 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-169 |
3.13e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.54 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 35 GHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNRE-VPFLRRQIGMIFQDHHLLMDRTVFDNVaipliiagaSYdD 113
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPEKRRIGYVFQDARLFPHYKVRGNL---------RY-G 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 114 IRRRVSAALDK-VGLLDKA---KNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
Cdd:PRK11144 101 MAKSMVAQFDKiVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-213 |
4.04e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlggrQALQGVTFHLQPGEMAFLTGHSGAGKS-TLLKLICGIERpsAGKIWFSGHDISRLKNREVPFLRRQ 80
Cdd:PRK10261 20 IAFMQEQQKI----AAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ--AGGLVQCDKMLLRRRSRQVIELSEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 ------------IGMIFQDHHLLMDR--TVFDNVAIPLII-AGASYDDIRRRVSAALDKVGLLDKA---KNFPIQLSGGE 142
Cdd:PRK10261 94 saaqmrhvrgadMAMIFQEPMTSLNPvfTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 143 QQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-201 |
6.44e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 83.24 E-value: 6.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKS----TLLKLICGIERPSaGKIWFSGHDISRLKNREVPFLR-RQIGMIFQD---- 87
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIG-GSATFNGREILNLPEKELNKLRaEQISMIFQDpmts 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 88 -----------------HHLLMDRTVF-------DNVAIPliiagasydDIRRRVsaaldkvglldkaKNFPIQLSGGEQ 143
Cdd:PRK09473 110 lnpymrvgeqlmevlmlHKGMSKAEAFeesvrmlDAVKMP---------EARKRM-------------KMYPHEFSGGMR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 144 QRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLIS 201
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKReFNTAIIMITHDLGVVA 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-219 |
7.10e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 21 VTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpflRRQIGMIF-----QDHHLLMDRT 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 96 VFDNVA------IPLIIAGASYDDIRRRVSAALD-KVGLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
Cdd:PRK15439 358 LAWNVCalthnrRGFWIKPARENAVLERYRRALNiKFNHAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503938019 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGL 219
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGAL 485
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
6-195 |
9.57e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.83 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 6 HVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIeRPSA---GKIWFSGHDI--SRLKNREvpflRRQ 80
Cdd:PRK13549 10 NITKTF-GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELqaSNIRDTE----RAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNvaiplIIAGA--------SYDDIRRRVSAALDKVGlLDKAKNFPI-QLSGGEQQRVGIARA 151
Cdd:PRK13549 84 IAIIHQELALVKELSVLEN-----IFLGNeitpggimDYDAMYLRAQKLLAQLK-LDINPATPVgNLGLGQQQLVEIAKA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 152 vVNKPAVLLA-DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:PRK13549 158 -LNKQARLLIlDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-213 |
2.63e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 3 RFEHVSKAYLGGRqALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdisrlknREVPF------ 76
Cdd:PRK11288 6 SFDGIGKTFPGVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG--------QEMRFasttaa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 LRRQIGMIFQDHHLLMDRTVFDNV---AIPLIIAGASYDDIRRRVSAALDKVGlLDKAKNFPIQ-LSGGEQQRVGIARAV 152
Cdd:PRK11288 77 LAAGVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLG-VDIDPDTPLKyLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503938019 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-215 |
4.31e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.53 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAG-----KIWFSGHDIsrLKNREVPFLRRQIGMIFQ 86
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 87 DHHLLmDRTVFDNVaipliIAGAS------YDDIRRRVSAALDKVGLLDKAKN----FPIQLSGGEQQRVGIARAVVNKP 156
Cdd:PRK14271 109 RPNPF-PMSIMDNV-----LAGVRahklvpRKEFRGVAQARLTEVGLWDAVKDrlsdSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 157 AVLLADEPTGNLDDALSEGIlrlfEEFNRV---GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKI----EEFIRSladRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-210 |
5.00e-18 |
|
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: 78.69 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghdisRLKNREVPFLRRQI--GMIFQDHHL 90
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV--------LLNGGPLDFQRDSIarGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 91 LMDR--TVFDNVAIPLIIAGasyddiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
Cdd:cd03231 83 GIKTtlSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503938019 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTL 210
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-195 |
5.92e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.63 E-value: 5.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPS---AGKIWFSGHDISRLKNRE-----------VPFLRRQIGM 83
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAisayvqqddlfIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 84 IFQDHhLLMDRTVfdnvaipliiagaSYDDIRRRVSAALDKVGLLDKAK------NFPIQLSGGEQQRVGIARAVVNKPA 157
Cdd:TIGR00955 121 MFQAH-LRMPRRV-------------TKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPP 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 503938019 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-201 |
1.45e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.77 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRL----------KN 71
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqknlvayvpQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 72 REV----PFLRRQIGMIFQDHHLLMDRTvfdnvaipliiagASYDDiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVG 147
Cdd:PRK15056 87 EEVdwsfPVLVEDVVMMGRYGHMGWLRR-------------AKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLIS 201
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVT 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-197 |
3.42e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.50 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 14 GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIeRPSAGKIWFSGHDISRLknrEVPFLRRQIGMIFQDHHLLmD 93
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNVAIpliiAGASYDDirRRVSAALDK------VGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLAD 162
Cdd:PRK11174 437 GTLRDNVLL----GNPDASD--EQLQQALENawvsefLPLLPQGLDTPIGdqaagLSVGQAQRLALARALLQPCQLLLLD 510
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 163 EPTGNLdDALSE-GILRLFEEFNRvGVTVLMATHDI 197
Cdd:PRK11174 511 EPTASL-DAHSEqLVMQALNAASR-RQTTLMVTHQL 544
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-215 |
5.65e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 5.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 20 GVTFHLQPGEMAFLTGHSGAGKS-----TLLKLICGIERpSAGKIWFSGHDISRLKNREvpflrRQIGMIFQDHHLLMD- 93
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAGVRQ-TAGRVLLDGKPVAPCALRG-----RKIATIMQNPRSAFNp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 -RTVFDNVAIPLIIAGASYDDirRRVSAALDKVGLLDKA---KNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
Cdd:PRK10418 95 lHTMHTHARETCLALGKPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503938019 170 DALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK10418 173 VVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-195 |
1.23e-16 |
|
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: 74.87 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 9 KAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIE--RPSAGKIWFSGHDISRLKNREVPflRRQIGMIFQ 86
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERA--RLGIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 87 DhhllmdrtvfdnvaiPLIIAGASYDDIRRRVSaaldkVGlldkaknfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
Cdd:cd03217 85 Y---------------PPEIPGVKNADFLRYVN-----EG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190
....*....|....*....|....*....|
gi 503938019 167 NLD-DALSEgILRLFEEFNRVGVTVLMATH 195
Cdd:cd03217 134 GLDiDALRL-VAEVINKLREEGKSVLIITH 162
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-195 |
2.15e-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: 73.34 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERpsagkiWFSGHdISRLKNREVPFLRRQi 81
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWP------WGSGR-IGMPEGEDLLFLPQR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 gmifqdhhllmdrtvfdnvaiPLIIAGAsyddIRRRVSAALDKVglldkaknfpiqLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03223 73 ---------------------PYLPLGT----LREQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFL 115
|
170 180 190
....*....|....*....|....*....|....
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFnrvGVTVLMATH 195
Cdd:cd03223 116 DEATSALDEESEDRLYQLLKEL---GITVISVGH 146
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-206 |
3.16e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLK---NREVPFLRRQIGMifQDHHLLMDR 94
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyQKQLCFVGHRSGI--NPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFDnvaIPLIIAGASYDDIRRRVSaaldkvglLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
Cdd:PRK13540 95 CLYD---IHFSPGAVGITELCRLFS--------LEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180 190
....*....|....*....|....*....|...
gi 503938019 174 EGILRLFEEFNRVGVTVLMATHDIGLISRRSYR 206
Cdd:PRK13540 164 LTIITKIQEHRAKGGAVLLTSHQDLPLNKADYE 196
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-196 |
3.22e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 76.70 E-value: 3.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRfehVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdisrlknrevPFLRrq 80
Cdd:PRK11819 9 MNR---VSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPA------------PGIK-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IGMIFQDHHLLMDRTVFDNV---------------------AIPL---------------IIAGASYDDIRRRVSAALDK 124
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENVeegvaevkaaldrfneiyaayAEPDadfdalaaeqgelqeIIDAADAWDLDSQLEIAMDA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 125 VGLldKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLdDALS----EGILRLFEefnrvGvTVLMATHD 196
Cdd:PRK11819 152 LRC--PPWDAKVtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHL-DAESvawlEQFLHDYP-----G-TVVAVTHD 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-196 |
7.09e-16 |
|
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: 75.74 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 6 HVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdisrlknrevPFLRrqIGMIF 85
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ------------PGIK--VGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 86 QDHHLLMDRTVFDNVAIPL------------------------------------IIAGASYDDIRRRVSAALDKVGLld 129
Cdd:TIGR03719 75 QEPQLDPTKTVRENVEEGVaeikdaldrfneisakyaepdadfdklaaeqaelqeIIDAADAWDLDSQLEIAMDALRC-- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 130 KAKNFPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHD 196
Cdd:TIGR03719 153 PPWDADVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTHD 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-213 |
2.42e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 7 VSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRRQIGMIFQ 86
Cdd:PRK10982 4 ISKSF-PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA--LENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 87 DHHLLMDRTVFDNVAI---PLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503938019 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-217 |
3.61e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.52 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpflRRQIGM--IFQDHH- 89
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE----RRRLGVayIPEDRLg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 90 --LLMDRTVFDNVAIPLIIAGA-------SYDDIRRRVSAALDK-----VGLLDKAKNfpiqLSGGEQQRVGIARAVVNK 155
Cdd:COG3845 345 rgLVPDMSVAENLILGRYRRPPfsrggflDRKAIRAFAEELIEEfdvrtPGPDTPARS----LSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503938019 156 PAVLLADEPTGNLDDALSEGIL-RLFEEFNRvGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHqRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-176 |
4.24e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 73.66 E-value: 4.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 4 FEHVSKAYLGGRQ-ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQIG 82
Cdd:PTZ00243 1311 FEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQFS 1387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 MIFQDhHLLMDRTVFDNVAiPLIIAGASyddirrRVSAALDKVGL---------------LDKAKNFpiqlSGGEQQRVG 147
Cdd:PTZ00243 1388 MIPQD-PVLFDGTVRQNVD-PFLEASSA------EVWAALELVGLrervasesegidsrvLEGGSNY----SVGQRQLMC 1455
|
170 180 190
....*....|....*....|....*....|
gi 503938019 148 IARAVVNK-PAVLLADEPTGNLDDALSEGI 176
Cdd:PTZ00243 1456 MARALLKKgSGFILMDEATANIDPALDRQI 1485
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-202 |
7.09e-15 |
|
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: 70.19 E-value: 7.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQ----ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHD--ISrlknrEVP 75
Cdd:cd03250 1 ISVEDASFTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayVS-----QEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 76 FLrrqigmifqdhhllMDRTVFDNvaiplIIAGASYDDirRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQ 144
Cdd:cd03250 76 WI--------------QNGTIREN-----ILFGKPFDE--ERYEKVIKACALEPDLEILPdgdlteigekgINLSGGQKQ 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 145 RVGIARAVVNKPAVLLADEPTGNLDDALSEGIL-RLFEEFNRVGVTVLMATHDIGLISR 202
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-211 |
1.48e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.49 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 23 FHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRL-KNREVPFLRRQIGmifqdhhLLMDRTVFDNVA 101
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGdRSRFMAYLGHLPG-------LKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 102 iplIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGIL---R 178
Cdd:PRK13543 105 ---FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD---LEGITlvnR 178
|
170 180 190
....*....|....*....|....*....|...
gi 503938019 179 LFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
Cdd:PRK13543 179 MISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
12-176 |
1.74e-14 |
|
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: 70.66 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdISrlknrevpfLRRQIGMIfqdhhll 91
Cdd:cd03291 47 LVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-IS---------FSSQFSWI------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 MDRTVFDNvaiplIIAGASYDDIRRRvsAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:cd03291 110 MPGTIKEN-----IIFGVSYDEYRYK--SVVKACQLEEDITKFPekdntvlgeggITLSGGQRARISLARAVYKDADLYL 182
|
170
....*....|....*.
gi 503938019 161 ADEPTGNLDDALSEGI 176
Cdd:cd03291 183 LDSPFGYLDVFTEKEI 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-214 |
1.77e-14 |
|
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: 71.87 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHdISRlkNREVPFlrrqigmifqdhhlLMDRTVF 97
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISF--SPQTSW--------------IMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 98 DNvaiplIIAGASYDDIRRR-------------VSAALDKVGLLDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
Cdd:TIGR01271 505 DN-----IIFGLSYDEYRYTsvikacqleediaLFPEKDKTVLGEGG----ITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 165 TGNLD-----DALSEGILRLFEEFNRVGVTVLMaTHdigliSRRSYRMLTLSDGH 214
Cdd:TIGR01271 576 FTHLDvvtekEIFESCLCKLMSNKTRILVTSKL-EH-----LKKADKILLLHEGV 624
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-213 |
2.48e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 71.43 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdisrlknrevPFLRRQ 80
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS------------AKVRMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 81 IgmiFQDHHLlmdrTVFDNVAIPLIIAGASYDDI-RRRVSAALDKVGLldkAKNFPIQ----LSGGEQQRVGIARAVVNK 155
Cdd:PLN03073 576 V---FSQHHV----DGLDLSSNPLLYMMRCFPGVpEQKLRAHLGSFGV---TGNLALQpmytLSGGQKSRVAFAKITFKK 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 156 PAVLLADEPTGNLD----DALSEGILrLFEEfnrvgvTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PLN03073 646 PHILLLDEPSNHLDldavEALIQGLV-LFQG------GVLMVSHDEHLISGSVDELWVVSEG 700
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
6-195 |
2.77e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 69.33 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 6 HVSkayLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIE--RPSAGKIWFSGHDISRLK--NREvpflRRQI 81
Cdd:COG0396 7 HVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSpdERA----RAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQD---------HHLLmdRTVFDNVAIPLIIAGASYDDIRrrvsAALDKVGL----LDKAKN--FpiqlSGGEQQRV 146
Cdd:COG0396 80 FLAFQYpveipgvsvSNFL--RTALNARRGEELSAREFLKLLK----EKMKELGLdedfLDRYVNegF----SGGEKKRN 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 147 GIARAVVNKPAVLLADEPTGNLD-DAL---SEGILRLFEEfnrvGVTVLMATH 195
Cdd:COG0396 150 EILQMLLLEPKLAILDETDSGLDiDALrivAEGVNKLRSP----DRGILIITH 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-177 |
5.61e-14 |
|
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: 69.96 E-value: 5.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsGHDIsrlknrevpflrrQI 81
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-------------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDH-HLLMDRTVFDNVAipliiAGASYDDIRRRVSAALDKVGLL-----DKAKNFPiQLSGGEQQRVGIARAVVNK 155
Cdd:TIGR03719 388 AYVDQSRdALDPNKTVWEEIS-----GGLDIIKLGKREIPSRAYVGRFnfkgsDQQKKVG-QLSGGERNRVHLAKTLKSG 461
|
170 180
....*....|....*....|....*.
gi 503938019 156 PAVLLADEPTGNLD----DALSEGIL 177
Cdd:TIGR03719 462 GNVLLLDEPTNDLDvetlRALEEALL 487
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-173 |
9.93e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.36 E-value: 9.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQIGMIFQDHHLLMDr 94
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFDNVAI------PLIIAGAS-----YDDIRRRVSAALDKVGlldkakNFPIQLSGGEQQRVGIARAVVNKPAVLLade 163
Cdd:PRK10789 404 TVANNIALgrpdatQQEIEHVArlasvHDDILRLPQGYDTEVG------ERGVMLSGGQKQRISIARALLLNAEILI--- 474
|
170
....*....|
gi 503938019 164 ptgnLDDALS 173
Cdd:PRK10789 475 ----LDDALS 480
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-195 |
1.03e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 14 GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpflrRQ---IGMIFQDHHL 90
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS-----SQeagIGIIHQELNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 91 LMDRTVFDNV----AIPLIIAGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
Cdd:PRK10762 91 IPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTD 170
|
170 180
....*....|....*....|....*....
gi 503938019 167 NLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:PRK10762 171 ALTDTETESLFRVIRELKSQGRGIVYISH 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-215 |
1.12e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.21 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 7 VSKAYLGGRQA--LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhD--ISRLKnrevpflrrqig 82
Cdd:PRK11147 6 IHGAWLSFSDAplLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DliVARLQ------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 83 mifQDHHLLMDRTVFDNVAIPLIIAGA---SYDDIRR---------------RVSAALDKVGL---------------LD 129
Cdd:PRK11147 73 ---QDPPRNVEGTVYDFVAEGIEEQAEylkRYHDISHlvetdpseknlnelaKLQEQLDHHNLwqlenrinevlaqlgLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 130 KAKNFPiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD-DALS--EGILRLFEefnrvGVTVLMaTHDIGLISRRSYR 206
Cdd:PRK11147 150 PDAALS-SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDiETIEwlEGFLKTFQ-----GSIIFI-SHDRSFIRNMATR 222
|
....*....
gi 503938019 207 MLTLSDGHL 215
Cdd:PRK11147 223 IVDLDRGKL 231
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-170 |
1.47e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 21 VTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDISRLKNREVPFLRRQIGMIFQDHhLLMDRTVFDNV 100
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDP-LLFSNSIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 101 AIPLII--------------AGASYDDIRRR-------------VSAALDKVGLLDKAKNFPI----------------- 136
Cdd:PTZ00265 481 KYSLYSlkdlealsnyynedGNDSQENKNKRnscrakcagdlndMSNTTDSNELIEMRKNYQTikdsevvdvskkvlihd 560
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503938019 137 ------------------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
Cdd:PTZ00265 561 fvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-90 |
2.90e-13 |
|
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: 67.90 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQ----ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlKNREVpfL 77
Cdd:COG4615 328 LELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA-DNREA--Y 404
|
90
....*....|...
gi 503938019 78 RRQIGMIFQDHHL 90
Cdd:COG4615 405 RQLFSAVFSDFHL 417
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
12-171 |
3.08e-13 |
|
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: 65.75 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI----ERPSaGKIWFSGHDISRLKNRevpfLRRQIGMIFQD 87
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYKEFAEK----YPGEIIYVSEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 88 HHLLMDRTVFDNVAIPLIIAGasyDDIRRRVsaaldkvglldkaknfpiqlSGGEQQRVGIARAVVNKPAVLLADEPTGN 167
Cdd:cd03233 92 DVHFPTLTVRETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
....
gi 503938019 168 LDDA 171
Cdd:cd03233 149 LDSS 152
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-195 |
3.49e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 3.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsghdisrlknrEVPflrrqigmifqDHHLLMDR 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-----------DVP-----------DNQFGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFDNVAIPLIIAGASYddirrrvsaALDKVGLLD----KAKnfPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
Cdd:COG2401 101 SLIDAIGRKGDFKDAVE---------LLNAVGLSDavlwLRR--FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180
....*....|....*....|....*.
gi 503938019 171 ALSEGILRLFEEFNR-VGVTVLMATH 195
Cdd:COG2401 170 QTAKRVARNLQKLARrAGITLVVATH 195
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
14-213 |
3.80e-13 |
|
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: 65.82 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 14 GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQIGMIFQDHHLLMD 93
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNvaiplIIAGASYDdiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLAD 162
Cdd:cd03290 93 ATVEEN-----ITFGSPFN--KQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 163 EPTGNLDDALS-----EGILRLFEEFNRvgvTVLMATHDIGLISRRSYrMLTLSDG 213
Cdd:cd03290 166 DPFSALDIHLSdhlmqEGILKFLQDDKR---TLVLVTHKLQYLPHADW-IIAMKDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-194 |
6.14e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.07 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRRQI 81
Cdd:NF033858 2 ARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA--VCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQ--DHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGLLDkaknFPI----QLSGGEQQRVGIARAVVNK 155
Cdd:NF033858 79 AYMPQglGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP----FADrpagKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 156 PAVLLADEPTGNLdDALS-----EGILRLFEEfnRVGVTVLMAT 194
Cdd:NF033858 155 PDLLILDEPTTGV-DPLSrrqfwELIDRIRAE--RPGMSVLVAT 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
20-217 |
6.88e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 20 GVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVpfLRRQIGMIFQDHH---LLMDRTV 96
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDG--LANGIVYISEDRKrdgLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 97 FDNVAIPlIIAGASYDDIRRRVSAALDKVGllDKAKNFPIQ----------LSGGEQQRVGIARAVVNKPAVLLADEPTG 166
Cdd:PRK10762 348 KENMSLT-ALRYFSRAGGSLKHADEQQAVS--DFIRLFNIKtpsmeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503938019 167 NLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISG 475
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-213 |
7.53e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 7.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIeRPSA---GKIWFSG-----HDIsrlKNREvpflRRQIGMI 84
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGevcrfKDI---RDSE----ALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDHHLLMDRTVFDNvaIPL--------IIagaSYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:NF040905 84 HQELALIPYLSIAEN--IFLgnerakrgVI---DWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-213 |
1.12e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.44 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPS--AGKIWFSGHDISRlknrevPFLRRqIGMIFQDH---- 88
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK------QILKR-TGFVTQDDilyp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 89 HLLMDRT-VFdnVAIPLIIAGASYDDIRRRVSAALDKVGLlDKAKN------FPIQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:PLN03211 154 HLTVRETlVF--CSLLRLPKSLTKQEKILVAESVISELGL-TKCENtiignsFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDiglISRRSYRM----LTLSDG 213
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ---PSSRVYQMfdsvLVLSEG 283
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
27-195 |
4.05e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.58 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 27 PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLRRQIGmifqdhhLLMDRTVFDNvaipLII 106
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLG-------LKLEMTVFEN----LKF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 107 AGASYDDIrRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV 186
Cdd:PRK13541 94 WSEIYNSA-ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANS 172
|
....*....
gi 503938019 187 GVTVLMATH 195
Cdd:PRK13541 173 GGIVLLSSH 181
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-163 |
6.19e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 6.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISrLKNREVpfLRRQI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT-AEQPED--YRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLlmdrtvFDNVAIPliiAGASYDDirRRVSAALDKVGLLDK-----AKNFPIQLSGGEQQRVGIARAVVNKP 156
Cdd:PRK10522 400 SAVFTDFHL------FDQLLGP---EGKPANP--ALVEKWLERLKMAHKleledGRISNLKLSKGQKKRLALLLALAEER 468
|
....*..
gi 503938019 157 AVLLADE 163
Cdd:PRK10522 469 DILLLDE 475
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-215 |
1.07e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.84 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGG-RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRR 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 80 QIGMIFQDHHLLMDRTVF--------DNVAIPLIIAGASYDDIRRRVSAALDkVGLLDKAKNFPIqlsgGEQQRVGIARA 151
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFnidpfsehNDADLWEALERAHIKDVIDRNPFGLD-AEVSEGGENFSV----GQRQLLSLARA 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 152 VVNKPAVLLADEPTGNLD---DALSEGILRlfEEFNrvGVTVLMATHDIGLISRRSyRMLTLSDGHL 215
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDvrtDSLIQRTIR--EEFK--SCTMLVIAHRLNTIIDCD-KILVLSSGQV 1447
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-200 |
1.08e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.65 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI---------WFSGHDISRLKN 71
Cdd:PRK10636 312 LLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 72 REVPFlrrqigmifqdHHLLMdrtvfdnvaipliIAGASYDDIRRRVSAALDKVGllDKAKNFPIQLSGGEQQRVGIARA 151
Cdd:PRK10636 391 DESPL-----------QHLAR-------------LAPQELEQKLRDYLGGFGFQG--DKVTEETRRFSGGEKARLVLALI 444
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503938019 152 VVNKPAVLLADEPTGNLD----DALSEGILrlfeEFNRVGVTVlmaTHDIGLI 200
Cdd:PRK10636 445 VWQRPNLLLLDEPTNHLDldmrQALTEALI----DFEGALVVV---SHDRHLL 490
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-219 |
2.64e-11 |
|
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: 62.15 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIWFSGHDISrLKNrEVPFLRRQIGMIFQD---HHL 90
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVD-IRN-PAQAIRAGIAMVPEDrkrHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 91 LMDRTVFDNVAIPL---------IIAGASYDDIRRrvsaALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLL 160
Cdd:TIGR02633 351 VPILGVGKNITLSVlksfcfkmrIDAAAELQIIGS----AIQRLKVKTASPFLPIgRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503938019 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGL 219
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDF 485
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-213 |
2.76e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlggRQ----ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfL 77
Cdd:PLN03130 1238 IKFEDVVLRY---RPelppVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---L 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 78 RRQIGMIFQDHHLLMDRTVFD--------NVAIPLIIAGASYDDIRRRVSAALDkVGLLDKAKNFpiqlSGGEQQRVGIA 149
Cdd:PLN03130 1312 RKVLGIIPQAPVLFSGTVRFNldpfnehnDADLWESLERAHLKDVIRRNSLGLD-AEVSEAGENF----SVGQRQLLSLA 1386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503938019 150 RAVVNKPAVLLADEPTGNLD---DALSEGILRlfEEFNrvGVTVLMATHDIGLISrRSYRMLTLSDG 213
Cdd:PLN03130 1387 RALLRRSKILVLDEATAAVDvrtDALIQKTIR--EEFK--SCTMLIIAHRLNTII-DCDRILVLDAG 1448
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-177 |
3.13e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.06 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsGHDIsrlknrevpflrrQI 81
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV-------------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDH-HLLMDRTVFDNVAipliiAGASYDDIRRRVSAALDKVGlldkAKNF-------PI-QLSGGEQQRVGIARAV 152
Cdd:PRK11819 390 AYVDQSRdALDPNKTVWEEIS-----GGLDIIKVGNREIPSRAYVG----RFNFkggdqqkKVgVLSGGERNRLHLAKTL 460
|
170 180
....*....|....*....|....*....
gi 503938019 153 VNKPAVLLADEPTGNLD----DALSEGIL 177
Cdd:PRK11819 461 KQGGNVLLLDEPTNDLDvetlRALEEALL 489
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-169 |
9.88e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 9.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICG--------------IERPSAGKIWfsghDIsrlknrevpflR 78
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltlfgRRRGSGETIW----DI-----------K 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 79 RQIGMIFQDHHllMDRTVFDNVaIPLIIAGAsYDDI--------RRRVSAA--LDKVGLLDKAKNFPIQ-LSGGEQQRVG 147
Cdd:PRK10938 336 KHIGYVSSSLH--LDYRVSTSV-RNVILSGF-FDSIgiyqavsdRQQKLAQqwLDILGIDKRTADAPFHsLSWGQQRLAL 411
|
170 180
....*....|....*....|..
gi 503938019 148 IARAVVNKPAVLLADEPTGNLD 169
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLD 433
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-213 |
1.63e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.07 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRqALQGVTFHLQPGEMAFLTGHSGAGKSTLLKL----ICGIERPSA----GKIWFSGHDISRLKNR 72
Cdd:PRK13547 1 MLTADHLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRGarvtGDVTLNGEPLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 73 EVPFLRRQIGMIFQDHHLLMDRTVFDNVAIPLII-AGASYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARA 151
Cdd:PRK13547 80 RLARLRAVLPQAAQPAFAFSAREIVLLGRYPHARrAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503938019 152 VVN---------KPAVLLADEPTGNLDDA----LSEGILRLFEEFNrvgVTVLMATHDIGLISRRSYRMLTLSDG 213
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAhqhrLLDTVRRLARDWN---LGVLAIVHDPNLAARHADRIAMLADG 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
15-215 |
1.82e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.80 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISrlKNREVPFLRRQIGMIFQ---DHHLL 91
Cdd:PRK09700 276 RKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYITEsrrDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 MDRTVFDNVAIPLIIAGASYD---------DIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:PRK09700 354 PNFSIAQNMAISRSLKDGGYKgamglfhevDEQRTAENQRELLALKCHSVNQNItELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-169 |
2.22e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 5 EHVSKAYlGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghdisrlKNrevpflrRQIGMI 84
Cdd:PRK15064 323 ENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-------EN-------ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 FQDH--HLLMDRTVFDNVAI-------PLIIAGA------SYDDIRRRVsaaldKVglldkaknfpiqLSGGEQQRVGIA 149
Cdd:PRK15064 388 AQDHayDFENDLTLFDWMSQwrqegddEQAVRGTlgrllfSQDDIKKSV-----KV------------LSGGEKGRMLFG 450
|
170 180
....*....|....*....|
gi 503938019 150 RAVVNKPAVLLADEPTGNLD 169
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD 470
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-205 |
1.92e-09 |
|
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: 56.68 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 1 MIRFEHVSKAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGI--------ERPSAGKIWFsghdISRLKNR 72
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY----VPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 73 EVPFLRRQIgmIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIrrrvsaaLDKVGLLDKAKNFPIQLSGGEQQRVGIARAV 152
Cdd:TIGR00954 527 TLGTLRDQI--IYPDSSEDMKRRGLSDKDLEQILDNVQLTHI-------LEREGGWSAVQDWMDVLSGGEKQRIAMARLF 597
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 153 VNKPAVLLADEPTgnldDALS---EGilRLFEEFNRVGVTVLMATHDIGLISRRSY 205
Cdd:TIGR00954 598 YHKPQFAILDECT----SAVSvdvEG--YMYRLCREFGITLFSVSHRKSLWKYHEY 647
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-219 |
2.93e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.07 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 21 VTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREV--------PFLRRQIGMIfqdhhllM 92
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAiragimlcPEDRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DRTVFDNVAIP---------LIIAGASYDDIRRRVSAALD-KVGLLDKAKNFpiqLSGGEQQRVGIARAVVNKPAVLLAD 162
Cdd:PRK11288 345 VHSVADNINISarrhhlragCLINNRWEAENADRFIRSLNiKTPSREQLIMN---LSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 163 EPTGNLD-DALSEgILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGL 219
Cdd:PRK11288 422 EPTRGIDvGAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGEL 478
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-195 |
3.78e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 21 VTFHLQPGEM-AFLtGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRlKNREVpflRRQIGMIFQDHHLLMDRTVFDN 99
Cdd:NF033858 285 VSFRIRRGEIfGFL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDA-GDIAT---RRRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 100 VA-------IPLiiagasyDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
Cdd:NF033858 360 LElharlfhLPA-------AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180
....*....|....*....|....
gi 503938019 173 SEGILRLFEEFNRV-GVTVLMATH 195
Cdd:NF033858 433 RDMFWRLLIELSREdGVTIFISTH 456
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-219 |
7.19e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 21 VTFHLQPGEMAFLTGHSGAGKSTLLKLICGIER-PSAGKIWFSGHDISRLKNREVpfLRRQIGMIFQD---HHLLMDRTV 96
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQA--IAQGIAMVPEDrkrDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 97 FDNVAIPLI--IAGASYDDIRRRVSAALDKVGLLdKAKNF----PI-QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
Cdd:PRK13549 359 GKNITLAALdrFTGGSRIDDAAELKTILESIQRL-KVKTAspelAIaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503938019 170 DALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGL 219
Cdd:PRK13549 438 VGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGDL 487
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-196 |
7.26e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 7.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 12 LGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsgHDISRLknrEVPFlrrqigmiFQDHHLL 91
Cdd:PRK11147 329 IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKL---EVAY--------FDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 MD--RTVFDNVA---IPLIIAGASyddirRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVnKPAVLLA-DEP 164
Cdd:PRK11147 394 LDpeKTVMDNLAegkQEVMVNGRP-----RHVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLARLFL-KPSNLLIlDEP 467
|
170 180 190
....*....|....*....|....*....|....
gi 503938019 165 TGNLDDAlsegILRLFEEF--NRVGvTVLMATHD 196
Cdd:PRK11147 468 TNDLDVE----TLELLEELldSYQG-TVLLVSHD 496
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-195 |
7.66e-09 |
|
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: 53.40 E-value: 7.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGieRPSAGKIwfSGhDISRLKNREVPFLRRQIGMIFQDHHLLM 92
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI--TG-EILINGRPLDKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DRTVfdNVAIpliiagasyddirrRVSAALDkvglldkaknfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
Cdd:cd03232 93 NLTV--REAL--------------RFSALLR-------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|...
gi 503938019 173 SEGILRLFEEFNRVGVTVLMATH 195
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIH 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-208 |
1.37e-08 |
|
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: 53.57 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISrlknrevpFLRRQIGMIFQD--HHLLMDRTvfDNVAIpli 105
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPQYIKADYEGtvRDLLSSIT--KDFYT--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 106 iagASYddIRRRVSAALDKVGLLDKAKNfpiQLSGGEQQRVGIArAVVNKPA-VLLADEPTGNLDD----ALSEGILRLF 180
Cdd:cd03237 92 ---HPY--FKTEIAKPLQIEQILDREVP---ELSGGELQRVAIA-ACLSKDAdIYLLDEPSAYLDVeqrlMASKVIRRFA 162
|
170 180
....*....|....*....|....*...
gi 503938019 181 EEFNRvgvTVLMATHDIGLISRRSYRML 208
Cdd:cd03237 163 ENNEK---TAFVVEHDIIMIDYLADRLI 187
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
9-179 |
4.30e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 9 KAYLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGieRPS----AGKIWFSGHDISRLKnrevPFLRRQIGMI 84
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLE----PEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 85 --FQdhhllmdrtvfdnvaIPLIIAGASYDDIRRR----------------------VSAALDKVGLLDK--AKNFPIQL 138
Cdd:CHL00131 88 laFQ---------------YPIEIPGVSNADFLRLaynskrkfqglpeldplefleiINEKLKLVGMDPSflSRNVNEGF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503938019 139 SGGEQQRVGIARAVVNKPAVLLADEPTGNLD-DAL---SEGILRL 179
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDiDALkiiAEGINKL 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-202 |
4.56e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 55 SAGKIWFSGHDISRLKNREVpflrRQIGMIFQDHHLLMDRTVFDNvaIPLIIAGASYDDIRRRVS-AALDK--------- 124
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLFNMSIYEN--IKFGKEDATREDVKRACKfAAIDEfieslpnky 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 125 ---VGLLDKAknfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLI 200
Cdd:PTZ00265 1349 dtnVGPYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADKTIITIAHRIASI 1422
|
..
gi 503938019 201 SR 202
Cdd:PTZ00265 1423 KR 1424
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2-215 |
6.20e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.20 E-value: 6.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAY------------LGGRQ-------ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfs 62
Cdd:PRK13545 5 VKFEHVTKKYkmynkpfdklkdLFFRSkdgeyhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 63 ghDIsrlknrevpflRRQIGMIFQDHHLLMDRTVFDNVAIPLIIAGASYDDIRRRVSAALDkVGLLDKAKNFPIQ-LSGG 141
Cdd:PRK13545 82 --DI-----------KGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIE-FADIGKFIYQPVKtYSSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503938019 142 EQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
Cdd:PRK13545 148 MKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV 221
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-197 |
6.99e-08 |
|
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: 52.22 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERpSAGKIWFSGHDISRLKNREvpfLRRQIGMIFQDHHLLm 92
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQT---WRKAFGVIPQKVFIF- 1304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 dRTVFDNVAIPLiiagASYDDirRRVSAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:TIGR01271 1305 -SGTFRKNLDPY----EQWSD--EEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLL 1377
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 162 DEPTGNLdDALSEGILRLFEEFNRVGVTVLMATHDI 197
Cdd:TIGR01271 1378 DEPSAHL-DPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-193 |
1.92e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 25 LQPGEMAFLTGHSGAGKSTLLKLIC----GIERPSAGKIWFSGHDisrlKNREVPFLRRQIGMIFQ-DHHlLMDRTVFDN 99
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT----PEEIKKHYRGDVVYNAEtDVH-FPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 100 V--AIPLIIAGASYDDIRRRVSAA-LDKVGL----LDKAKN------FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
Cdd:TIGR00956 159 LdfAARCKTPQNRPDGVSREEYAKhIADVYMatygLSHTRNtkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
170 180
....*....|....*....|....*...
gi 503938019 167 NLDDALSEGILR-LFEEFNRVGVTVLMA 193
Cdd:TIGR00956 239 GLDSATALEFIRaLKTSANILDTTPLVA 266
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-178 |
2.42e-07 |
|
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: 49.91 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKnreVPFLRRQIGMIFQDHHLL------ 91
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILFsgsirf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 --------MDRTVFDNVAIpliiagASYDDIRRRVSAALDKVgLLDKAKNFpiqlSGGEQQRVGIARAVVNKPAVLLADE 163
Cdd:cd03288 114 nldpeckcTDDRLWEALEI------AQLKNMVKSLPGGLDAV-VTEGGENF----SVGQRQLFCLARAFVRKSSILIMDE 182
|
170
....*....|....*
gi 503938019 164 PTGNLDDAlSEGILR 178
Cdd:cd03288 183 ATASIDMA-TENILQ 196
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
110-195 |
2.79e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 110 SYDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVT 189
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
....*.
gi 503938019 190 VLMATH 195
Cdd:NF000106 197 VLLTTQ 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-213 |
2.79e-07 |
|
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: 50.71 E-value: 2.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREvpfLRRQIGMIFQDHHLL-----M 92
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD---LRFKITIIPQDPVLFsgslrM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DRTVFDNVAIPLIIAGASYDDIRRRVSAALDKVGL--LDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD- 169
Cdd:TIGR00957 1379 NLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHecAEGGEN----LSVGQRQLVCLARALLRKTKILVLDEATAAVDl 1454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503938019 170 --DALSEGILRL-FEEfnrvgVTVLMATHDIGLISRRSyRMLTLSDG 213
Cdd:TIGR00957 1455 etDNLIQSTIRTqFED-----CTVLTIAHRLNTIMDYT-RVIVLDKG 1495
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-197 |
5.09e-07 |
|
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: 49.08 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERpSAGKIWFSGHDISRLKNREvpfLRRQIGMIFQDHhLLM 92
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQK---WRKAFGVIPQKV-FIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 93 DRTVFDNvaipLIIAGASYDDIRRRVSaalDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03289 90 SGTFRKN----LDPYGKWSDEEIWKVA---EEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 162 DEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDI 197
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKQ-AFADCTVILSEHRI 197
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-169 |
9.30e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.97 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGkiwfsGHDISRLKNREVPflrrQIGMIFqdhhllmDR 94
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-----ASVVIRGTVAYVP----QVSWIF-------NA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFDNvaiplIIAGASYDdiRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADE 163
Cdd:PLN03130 694 TVRDN-----ILFGSPFD--PERYERAIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
....*.
gi 503938019 164 PTGNLD 169
Cdd:PLN03130 767 PLSALD 772
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-197 |
1.07e-06 |
|
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: 48.13 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 26 QPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-----W------FSGHDI----SRLKNREV-PFLRRQigmiFQDHh 89
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdWdeildeFRGSELqnyfTKLLEGDVkVIVKPQ----YVDL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 90 llmdrtvfdnvaIPLIIAGASYDDIRRR--------VSAALDKVGLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLA 161
Cdd:cd03236 99 ------------IPKAVKGKVGELLKKKdergkldeLVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-200 |
1.32e-06 |
|
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: 48.24 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 25 LQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwFSGHDIS----RLKN------REvpFLRRQIGMIFQDHHLlmdr 94
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKISykpqYISPdydgtvEE--FLRSANTDDFGSSYY---- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 tvfdnvaipliiagasYDDIRRRVSaaLDKvgLLDKAKNfpiQLSGGEQQRVGIArAVVNKPA-VLLADEPTGNLDD--- 170
Cdd:COG1245 436 ----------------KTEIIKPLG--LEK--LLDKNVK---DLSGGELQRVAIA-ACLSRDAdLYLLDEPSAHLDVeqr 491
|
170 180 190
....*....|....*....|....*....|.
gi 503938019 171 -ALSEGILRLFEEFnrvGVTVLMATHDIGLI 200
Cdd:COG1245 492 lAVAKAIRRFAENR---GKTAMVVDHDIYLI 519
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-200 |
1.61e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 28 GEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwFSGHDIS----RLK---NREVPFLRRQIGMIFQDHHLlmdrtvfdnv 100
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-DPELKISykpqYIKpdyDGTVEDLLRSITDDLGSSYY---------- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 101 aipliiagasYDDIRRRVSaaLDKvgLLDKAKNfpiQLSGGEQQRVGIArAVVNKPAVL-LADEPTGNLD----DALSEG 175
Cdd:PRK13409 434 ----------KSEIIKPLQ--LER--LLDKNVK---DLSGGELQRVAIA-ACLSRDADLyLLDEPSAHLDveqrLAVAKA 495
|
170 180
....*....|....*....|....*
gi 503938019 176 ILRLFEEFnrvGVTVLMATHDIGLI 200
Cdd:PRK13409 496 IRRIAEER---EATALVVDHDIYMI 517
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-172 |
1.81e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 13 GGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRLKNREVPFLR-----------RQI 81
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPqpaleyvidgdREY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 82 GMIFQDHHLLMDRTvfDNVAIPLIIAGASYDD---IRRRVSAALDKVGLLDKAKNFPIQ-LSGGEQQRVGIARAVVNKPA 157
Cdd:PRK10636 92 RQLEAQLHDANERN--DGHAIATIHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSD 169
|
170
....*....|....*.
gi 503938019 158 VLLADEPTGNLD-DAL 172
Cdd:PRK10636 170 LLLLDEPTNHLDlDAV 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-213 |
2.51e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghdisrlknrevpfLRRQIGMIFQdHHLLMDRTVF 97
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----------------AERSIAYVPQ-QAWIMNATVR 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 98 DNVAIPLIIAGASYDDIRR--RVSAALDKV--GLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
Cdd:PTZ00243 739 GNILFFDEEDAARLADAVRvsQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 174 EgilRLFEEFNR---VGVTVLMATHDIGLISRRSYrMLTLSDG 213
Cdd:PTZ00243 819 E---RVVEECFLgalAGKTRVLATHQVHVVPRADY-VVALGDG 857
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-217 |
2.55e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIsrlKNRE-----------VPFLRRQIGmif 85
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI---NNHNaneainhgfalVTEERRSTG--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 86 qdhhllmdrtVFDNVAIpliiagaSYDDIRRRVSAALDKVGLLDKAK--------------NFPIQ------LSGGEQQR 145
Cdd:PRK10982 337 ----------IYAYLDI-------GFNSLISNIRNYKNKVGLLDNSRmksdtqwvidsmrvKTPGHrtqigsLSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503938019 146 VGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAG 471
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-195 |
2.91e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 15 RQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKliCGIERPSAGKIwFSGHDISRLKNREVPFLRRqIGMIFQ-DHHLlmd 93
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLN--VLAERVTTGVI-TGGDRLVNGRPLDSSFQRS-IGYVQQqDLHL--- 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVfdNVAIPLIIAGA-------SYDDIRRRVSAALDKVGLLDKAKNF----PIQLSGGEQQRVGIARAVVNKPAVLL-A 161
Cdd:TIGR00956 849 PTS--TVRESLRFSAYlrqpksvSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|....
gi 503938019 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
7-205 |
1.36e-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: 43.85 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 7 VSKAYLggrQALQGVTFHLQPGEMAFLTGHSGAGKSTLLK----------LICGIERPSAGKIWFsghdISRLKNrevpf 76
Cdd:cd03238 3 VSGANV---HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglyasgkarLISFLPKFSRNKLIF----IDQLQF----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 77 lrrqigmifqdhhllmdrtvfdnvaipLIIAGASYDDIRRRVSAaldkvglldkaknfpiqLSGGEQQRVGIAR--AVVN 154
Cdd:cd03238 71 ---------------------------LIDVGLGYLTLGQKLST-----------------LSGGELQRVKLASelFSEP 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503938019 155 KPAVLLADEPTGNLDDalsEGILRLFEEFNRV---GVTVLMATHDIGLISRRSY 205
Cdd:cd03238 107 PGTLFILDEPSTGLHQ---QDINQLLEVIKGLidlGNTVILIEHNLDVLSSADW 157
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-215 |
1.51e-05 |
|
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: 45.32 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdisrlknrEVPFLRRQiGMIFQD---HHLLMDR 94
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG---------SVAYVPQQ-AWIQNDslrENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFDNVAIPLIIAGASYDDIRRRVSAALDKVGllDKAKNfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE 174
Cdd:TIGR00957 724 ALNEKYYQQVLEACALLPDLEILPSGDRTEIG--EKGVN----LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503938019 175 GIlrlfeeFNRV--------GVTVLMATHDIGLISRRSYrMLTLSDGHL 215
Cdd:TIGR00957 798 HI------FEHVigpegvlkNKTRILVTHGISYLPQVDV-IIVMSGGKI 839
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-203 |
1.68e-05 |
|
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: 43.52 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 27 PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghdisrlknrevpflrrqigmifqdhhllmdrtvfdnvaipLII 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------------------------IYI 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 107 AGasyDDIRRRVSAALDKVGLLDKAKnfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILR------LF 180
Cdd:smart00382 37 DG---EDILEEVLDQLLLIIVGGKKA----SGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
|
170 180
....*....|....*....|...
gi 503938019 181 EEFNRVGVTVLMATHDIGLISRR 203
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGPA 132
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-198 |
2.77e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 44.04 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 17 ALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghdisrLKNREVPFLRRQIGMIFQdhhllmdRTV 96
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV---------DRNGEVSVIAISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 97 FDNVAIPLIIAGASyddiRRRVSAALDKVGLLDKAKNFPIQ----LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
Cdd:PRK13546 103 IENIEFKMLCMGFK----RKEIKAMTPKIIEFSELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180
....*....|....*....|....*.
gi 503938019 173 SEGILRLFEEFNRVGVTVLMATHDIG 198
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLG 204
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-207 |
4.71e-05 |
|
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: 42.56 E-value: 4.71e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503938019 136 IQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD----ALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRM 207
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrlNAARAIRRLSEEGKK---TALVVEHDLAVLDYLSDRI 142
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
59-201 |
1.12e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 59 IWFSGHDISRLKNREVPFLRrqigmIFQDHHLLMDRTVFDNVAIPLI-IAGASYDDIRRRVSAALDKVGLL--------- 128
Cdd:pfam13304 151 LSFLLLLDEGLLLEDWAVLD-----LAADLALFPDLKELLQRLVRGLkLADLNLSDLGEGIEKSLLVDDRLrerglille 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 129 -DKAKNFPI-QLSGGEQQ---RVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLIS 201
Cdd:pfam13304 226 nGGGGELPAfELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-195 |
1.65e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 16 QALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGieRPSAGKIwfSGH-DISRLKNREVPFLRRQiGMIFQDHHLLMDR 94
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EGDiRISGFPKKQETFARIS-GYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFDNV---AIPLIIAGASYDDIRRRVSAALDKV---GLLDKAKNFP--IQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
Cdd:PLN03140 969 TVRESLiysAFLRLPKEVSKEEKMMFVDEVMELVeldNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180
....*....|....*....|....*....
gi 503938019 167 NLDDALSEGILRLFEEFNRVGVTVLMATH 195
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-169 |
1.98e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 2 IRFEHVSKAyLGGRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLK-----LICGIerPSAGKIW-----FSGHDISRLK- 70
Cdd:PLN03073 178 IHMENFSIS-VGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRymamhAIDGI--PKNCQILhveqeVVGDDTTALQc 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 71 ----NREVPFLRRQIGMIFQDHHLLMDRTVFDNVAIPLIiAGASYDDIRRRVSAALDKVGLLD----KAKNFPI------ 136
Cdd:PLN03073 255 vlntDIERTQLLEEEAQLVAQQRELEFETETGKGKGANK-DGVDKDAVSQRLEEIYKRLELIDaytaEARAASIlaglsf 333
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503938019 137 ----------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
Cdd:PLN03073 334 tpemqvkatkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-169 |
2.81e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 41.50 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 18 LQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGiERPSAgkiwfsgHDISRLKNREVPFLRrQIGMIFqdhhllmDRTVF 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG-ELSHA-------ETSSVVIRGSVAYVP-QVSWIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 98 DNvaiplIIAGASYDDirRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADEPTG 166
Cdd:PLN03232 697 EN-----ILFGSDFES--ERYWRAIDVTALQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
...
gi 503938019 167 NLD 169
Cdd:PLN03232 770 ALD 772
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-197 |
4.15e-04 |
|
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: 40.92 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 25 LQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI-----WfsghdisrlknREVpfLRRQIGMIFQDHhllmdrtvFDN 99
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepsW-----------DEV--LKRFRGTELQDY--------FKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 100 VA---------------IPLIIAG------ASYDDiRRRVSAALDKVGL---LDKAKNfpiQLSGGEQQRVGIARAVVNK 155
Cdd:COG1245 155 LAngeikvahkpqyvdlIPKVFKGtvrellEKVDE-RGKLDELAEKLGLeniLDRDIS---ELSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503938019 156 PAVLLADEPTGNLDdaLSE--GILRLFEEFNRVGVTVLMATHDI 197
Cdd:COG1245 231 ADFYFFDEPSSYLD--IYQrlNVARLIRELAEEGKYVLVVEHDL 272
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-165 |
6.02e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 14 GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLIcgierpsAGKIWfsGHDISrlknrevpflrrqiGMIFQDHHLLMD 93
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSV-------FGRSY--GRNIS--------------GTVFKDGKEVDV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 94 RTVFDNVAipliiAGASY-------------DDIRRRVS-AALDKV---GLLDKAKNFPI-------------------- 136
Cdd:NF040905 329 STVSDAID-----AGLAYvtedrkgyglnliDDIKRNITlANLGKVsrrGVIDENEEIKVaeeyrkkmniktpsvfqkvg 403
|
170 180
....*....|....*....|....*....
gi 503938019 137 QLSGGEQQRVGIARAVVNKPAVLLADEPT 165
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
14-176 |
7.19e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 7.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 14 GRQALQGVTFHLQPGEMAFLTGHSGAGKSTLLKLICGIE--RPSAGKIWFSGHDISRLKNREVPflRRQIGMIFQdhhll 91
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA--GEGIFMAFQ----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 92 mdrtvfdnvaIPLIIAGAS--------YDDIRR-RVSAALD----------KVGLLDKAKNF-----PIQLSGGEQQRVG 147
Cdd:PRK09580 86 ----------YPVEIPGVSnqfflqtaLNAVRSyRGQEPLDrfdfqdlmeeKIALLKMPEDLltrsvNVGFSGGEKKRND 155
|
170 180 190
....*....|....*....|....*....|...
gi 503938019 148 IARAVVNKPAVLLADEPTGNLD-DAL---SEGI 176
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDiDALkivADGV 188
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-45 |
1.14e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 36.04 E-value: 1.14e-03
10 20
....*....|....*....|....*..
gi 503938019 19 QGVTFHLQPGEMAFLTGHSGAGKSTLL 45
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
129-201 |
1.30e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.87 E-value: 1.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503938019 129 DKAKNFPI-QLSGGEQQRVGIARAVVN---KPAVLLADEPTGNLDDALSEGILRLF-EEFNRVGVTVLMATHDIGLIS 201
Cdd:COG1106 193 GGNVPLPLsEESDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFlDLANKNNAQLIFTTHSTELLD 270
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-196 |
1.66e-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: 38.36 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 33 LTGHSGAGKSTL---LKLICGIERPSAGKIWFSGHDISRLKNRevpflRRQIGMIFQ-----DHHLLMDRTVFDNVAIpl 104
Cdd:cd03240 27 IVGQNGAGKTTIieaLKYALTGELPPNSKGGAHDPKLIREGEV-----RAQVKLAFEnangkKYTITRSLAILENVIF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 105 iiagasyddIRRRVSAALdkvgLLDKAKnfpiQLSGGEQQ------RVGIARAVVNKPAVLLADEPTGNLD-DALSEGIL 177
Cdd:cd03240 100 ---------CHQGESNWP----LLDMRG----RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeENIEESLA 162
|
170 180
....*....|....*....|
gi 503938019 178 RLFEEFNRVGV-TVLMATHD 196
Cdd:cd03240 163 EIIEERKSQKNfQLIVITHD 182
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-197 |
2.18e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.46 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 23 FHLQPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDISRL------KNREVPFLRRQIGMIFQDHHllmD--R 94
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfeqlqKLVSDEWQRNNTDMLSPGED---DtgR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 95 TVFDnvaiplIIAGASYDDIR-RRVSAALDKVGLLDKakNFpIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
Cdd:PRK10938 101 TTAE------IIQDEVKDPARcEQLAQQFGITALLDR--RF-KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180
....*....|....*....|....*..
gi 503938019 174 EGILRLFEEFNRVGVT---VLMATHDI 197
Cdd:PRK10938 172 QQLAELLASLHQSGITlvlVLNRFDEI 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-169 |
2.58e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 33 LTGHSGAGKSTLLKLICGIERPSAGkiwfsghDISRLKNREVPFLRrqigmifQDHHLLMDRTVFDNV------------ 100
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAG-------NVSLDPNERLGKLR-------QDQFAFEEFTVLDTVimghtelwevkq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 101 ------AIP------------LIIAGASYD--DIRRRVSAALDKVGLLDKAKNFPI-QLSGGEQQRVGIARAVVNKPAVL 159
Cdd:PRK15064 98 erdriyALPemseedgmkvadLEVKFAEMDgyTAEARAGELLLGVGIPEEQHYGLMsEVAPGWKLRVLLAQALFSNPDIL 177
|
170
....*....|
gi 503938019 160 LADEPTGNLD 169
Cdd:PRK15064 178 LLDEPTNNLD 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
137-169 |
4.75e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 37.48 E-value: 4.75e-03
10 20 30
....*....|....*....|....*....|...
gi 503938019 137 QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
28-50 |
5.21e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.61 E-value: 5.21e-03
10 20
....*....|....*....|...
gi 503938019 28 GEMAFLTGHSGAGKSTLLKLICG 50
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNALLP 107
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-213 |
7.96e-03 |
|
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: 35.80 E-value: 7.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503938019 136 IQLSGGEQQRVGIA-----RAVVNKPAVLLaDEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLI--SRRSYRML 208
Cdd:cd03227 76 LQLSGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAelADKLIHIK 154
|
....*
gi 503938019 209 TLSDG 213
Cdd:cd03227 155 KVITG 159
|
|
| |
