|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-223 |
8.02e-142 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 395.19 E-value: 8.02e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEKKGG 223
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
1.31e-110 |
|
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: 316.27 E-value: 1.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGL 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-213 |
1.11e-109 |
|
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: 313.80 E-value: 1.11e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-219 |
3.35e-98 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 285.01 E-value: 3.35e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA---ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:COG1136 4 LLELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRG-LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNeRVITMKQGVIVSDE 219
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARAD-RVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
5.63e-94 |
|
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: 273.98 E-value: 5.63e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA---ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYR 78
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 R-GLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVnEMNERVITMKQGVI 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-216 |
4.14e-79 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 240.75 E-value: 4.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA---ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLImkelN----PTEGTIIVNGQNLNRMKHRN 73
Cdd:COG1135 1 MIELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI----NllerPTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 74 IAKYRRGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIV 153
Cdd:COG1135 77 LRAARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 154 NEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-216 |
1.38e-77 |
|
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: 233.24 E-value: 1.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGH---AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINrELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-218 |
4.82e-75 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 227.25 E-value: 4.82e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIafaL--RVTETPT-RVIKKKVP--------AALSLVGLAQKYKSFPKELSGGEQQRVAIA 149
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNV---LagRLGRTSTwRSLLGLFPpedreralEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIArEDGITVVVNLHQVDLARRYADRIIGLRDGRVVFD 228
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-218 |
1.10e-70 |
|
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: 215.27 E-value: 1.10e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhRNIAKYRRGL 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQD-----FRllkdRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:COG1122 78 GLVFQNpddqlFA----PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
3.25e-70 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 218.43 E-value: 3.25e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhrNIAKYRRG 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT-----GLPPEKRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 161 ADEPTGNLDPTN----SWEIMSLLKeanERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG3842 159 LDEPLSALDAKLreemREELRRLQR---ELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
6.97e-70 |
|
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: 222.09 E-value: 6.97e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY----SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAK 76
Cdd:COG1123 260 LLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQD-FR-LLKDRNIYENIAFALRV-TETPTRVIKKKVPAALSLVGLAQKYKS-FPKELSGGEQQRVAIARAI 152
Cdd:COG1123 340 LRRRVQMVFQDpYSsLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-213 |
6.40e-69 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 210.89 E-value: 6.40e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-216 |
1.61e-68 |
|
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: 210.22 E-value: 1.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG 80
Cdd:COG1127 5 MIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRV-TETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
2.43e-68 |
|
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: 208.91 E-value: 2.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrniAKYRRGL 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-----PPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEA-NERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-216 |
4.17e-68 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 212.74 E-value: 4.17e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY---SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:PRK11153 1 MIELKNISKVFpqgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-219 |
1.21e-67 |
|
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: 207.67 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALN---GVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRG-LGVVFQDFRLLKDRNIYENIAFALRvtETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLE--LAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVnEMNERVITMKQGVIVSDE 219
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNrERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVEDT 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-213 |
1.26e-66 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 206.09 E-value: 1.26e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY---SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGqnlnrmkhRNIAKY 77
Cdd:COG1116 7 ALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG--------KPVTGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 158 ILLADEPTGNLDPTNSWEIMS-LLKEANERGTTVLVVTHNqeiVNE---MNERVITMKQG 213
Cdd:COG1116 159 VLLMDEPFGALDALTRERLQDeLLRLWQETGKTVLFVTHD---VDEavfLADRVVVLSAR 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-218 |
1.96e-66 |
|
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: 205.11 E-value: 1.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGL 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFAlRVTETPT-RVI--------KKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAI 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSG-RLGRRSTwRSLfglfpkeeKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFD 226
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-216 |
3.85e-66 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 204.07 E-value: 3.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrMKHRNIAKYRRG 80
Cdd:COG1126 1 MIEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENiafalrVTETPTRVikKKVPAA---------LSLVGLAQKYKSFPKELSGGEQQRVAIARA 151
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLEN------VTLAPIKV--KKMSKAeaeeramelLERVGLADKADAYPAQLSGGQQQRVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 152 IVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHnqeivnEMN------ERVITMKQGVIV 216
Cdd:COG1126 151 LAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH------EMGfarevaDRVVFMDGGRIV 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-216 |
1.40e-65 |
|
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: 202.35 E-value: 1.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKG---HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQD-FRLLKDR-NIYENIAFALRV--TETPTRVIKKKVPAALSLVGLAQKY-KSFPKELSGGEQQRVAIARAI 152
Cdd:cd03257 81 RKEIQMVFQDpMSSLNPRmTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKlQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-218 |
1.39e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 197.59 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmkHRNIAKYRRGL 81
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-216 |
3.49e-63 |
|
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: 196.57 E-value: 3.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGL 81
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRV-TETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-218 |
4.03e-63 |
|
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: 196.95 E-value: 4.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY---SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmKHRNIAKY 77
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV---TRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQD--------FRLlkDRNIYEniafALRVTETPTRviKKKVPAALSLVGLAQKYKS-FPKELSGGEQQRVAI 148
Cdd:COG1124 78 RRRVQMVFQDpyaslhprHTV--DRILAE----PLRIHGLPDR--EERIAELLEQVGLPPSFLDrYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 149 ARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEE 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-213 |
7.04e-63 |
|
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: 194.99 E-value: 7.04e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmKHRNIAKYRRGL 81
Cdd:cd03225 1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL---TKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFR--LLKDRnIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:cd03225 78 GLVFQNPDdqFFGPT-VEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-216 |
7.91e-63 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 199.14 E-value: 7.91e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRM--KHRNIAkyr 78
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLppKDRNIA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 rglgVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAI 158
Cdd:COG3839 79 ----MVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 159 LLADEPTGNLDPTNSWEIMSLLKEA-NERGTTVLVVTHNQEivnE---MNERVITMKQGVIV 216
Cdd:COG3839 155 FLLDEPLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTHDQV---EamtLADRIAVMNDGRIQ 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-216 |
1.94e-62 |
|
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: 194.38 E-value: 1.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhrNIAKYRRGL 81
Cdd:cd03300 1 IELENVSKFYGGFVA-LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-210 |
2.52e-61 |
|
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: 191.15 E-value: 2.52e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG---HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrniakyR 78
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP--------G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 RGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAI 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 159 LLADEPTGNLDP-TNswEIM--SLLKEANERGTTVLVVTHNqeiVNE---MNERVITM 210
Cdd:cd03293 153 LLLDEPFSALDAlTR--EQLqeELLDIWRETGKTVLLVTHD---IDEavfLADRVVVL 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
1.96e-60 |
|
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: 197.43 E-value: 1.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPT---EGTIIVNGQNLNRMkhrNIAK 76
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL---SEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQDFRL-LKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:COG1123 81 RGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-218 |
3.08e-60 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 190.36 E-value: 3.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG----HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQ--DFRLLKDrNIYENIAFALR---VTETPtrvIKKKVPAALSLVGLAQKY--KSfPKELSGGEQQRVAIAR 150
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLFEE-TVYKDIAFGPKnlgLSEEE---AEERVKEALELVGLDEEYleRS-PFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
3.40e-60 |
|
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: 188.12 E-value: 3.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmKHRNIAKYRRGL 81
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIafalrvTETPTRVIKKKVPAA-------LSLVGLAQKYKSFPKELSGGEQQRVAIARAIVN 154
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENI------TLAPIKVKGMSKAEAeeralelLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 155 EPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-210 |
4.11e-60 |
|
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: 187.82 E-value: 4.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG-LG 82
Cdd:TIGR03608 1 LKNISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREkLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 VVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLAD 162
Cdd:TIGR03608 80 YLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505341235 163 EPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVnEMNERVITM 210
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-213 |
7.37e-60 |
|
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: 186.24 E-value: 7.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhRNIAKYRRGL 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFAlrvtetptrvikkkvpaalslvglaqkyksfpkeLSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-218 |
1.24e-59 |
|
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: 187.89 E-value: 1.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFAlRVTETPT-RVI--------KKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARA 151
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHG-RLGYKPTwRSLlgrfseedKERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 152 IVNEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-216 |
5.07e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 184.19 E-value: 5.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhrNIAKYRRGL 81
Cdd:COG1118 3 IEVRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKE--ANERGTTVLvVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRlhDELGGTTVF-VTHDQEEALELADRVVVMNQGRIE 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
5.24e-57 |
|
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: 180.14 E-value: 5.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRM--KHRNIAkyrr 79
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLppKDRDIA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 glgVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:cd03301 76 ---MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
1.12e-56 |
|
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: 182.56 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY--SKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNP---TEGTIIVNGQNLNRMKHRNI 74
Cdd:COG0444 1 LLEVRNLKVYFptRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 75 AKYR-RGLGVVFQD--------FRllkdrnIYENIAFALRV-TETPTRVIKKKVPAALSLVGL---AQKYKSFPKELSGG 141
Cdd:COG0444 81 RKIRgREIQMIFQDpmtslnpvMT------VGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 142 EQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
1.52e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.86 E-value: 1.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRGL 81
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM---PPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRnIYENIAFALRVTETptRVIKKKVPAALSLVGLAQKYKSFP-KELSGGEQQRVAIARAIVNEPAILL 160
Cdd:COG4619 77 AYVPQEPALWGGT-VRDNLPFPFQLRER--KFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-213 |
2.69e-56 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 178.86 E-value: 2.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA---ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 R-RGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:PRK11629 85 RnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNeRVITMKQG 213
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQLAKRMS-RQLEMRDG 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-218 |
3.20e-56 |
|
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: 179.47 E-value: 3.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYrrg 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDfrllkdrniyENIAFALRVTET--------------PTRVIKKKVPAALSLVGLAQ-KYKSFPkELSGGEQQR 145
Cdd:COG1120 77 IAYVPQE----------PPAPFGLTVRELvalgryphlglfgrPSAEDREAVEEALERTGLEHlADRPVD-ELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHnqeivnEMN------ERVITMKQGVIVSD 218
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLH------DLNlaaryaDRLVLLKDGRIVAQ 219
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-213 |
1.91e-55 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 176.06 E-value: 1.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA---ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKH-RNIAK 76
Cdd:NF038007 1 MLNMQNAEKCYITKTIktkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYsQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNeRVITMKQG 213
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGN-RIINMKDG 216
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-216 |
1.93e-55 |
|
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: 176.60 E-value: 1.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLI--MKELN---PTEGTIIVNGQNLNRMKHrNIAK 76
Cdd:cd03260 1 IELRDLNVYYGDKHA-LKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIpgaPDEGEVLLDGKDIYDLDV-DVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQD---FRLlkdrNIYENIAFALRV-TETPTRVIKKKVPAALSLVGLAQ--KYKSFPKELSGGEQQRVAIAR 150
Cdd:cd03260 79 LRRRVGMVFQKpnpFPG----SIYDNVAYGLRLhGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERgTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
3.66e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 176.43 E-value: 3.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRnIAkYrrg 80
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-IG-Y--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 lgvVFQDFRLlkDRNiyeniaFALRVTET--------------PTRVIKKKVPAALSLVGLAqKYKSFP-KELSGGEQQR 145
Cdd:COG1121 80 ---VPQRAEV--DWD------FPITVRDVvlmgrygrrglfrrPSRADREAVDEALERVGLE-DLADRPiGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-224 |
4.28e-55 |
|
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: 186.96 E-value: 4.28e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSK-GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRG 80
Cdd:COG2274 474 IELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIAFAlRVTETPTRVIKkkvpaALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIA 149
Cdd:COG2274 551 IGVVLQDVFLFSG-TIRENITLG-DPDATDEEIIE-----AARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIA 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANeRGTTVLVVTHNQEIVNEMNeRVITMKQGVIVSD-------EKKG 222
Cdd:COG2274 624 RALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLAD-RIIVLDKGRIVEDgtheellARKG 701
|
..
gi 505341235 223 GY 224
Cdd:COG2274 702 LY 703
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-218 |
9.46e-55 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 175.28 E-value: 9.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLN--RMKHRNIakyR 78
Cdd:PRK09493 1 MIEFKNVSKHFGP-TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLI---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 RGLGVVFQDFRLLKDRNIYENIAFA-LRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-216 |
1.21e-54 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 176.82 E-value: 1.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRG 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDL---DPVELRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGL-----AQKYksfPKELSGGEQQRVAIARAIVNE 155
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpeeyRDRY---PHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHnqeivnEMNE------RVITMKQGVIV 216
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRElGKTIVFVTH------DIDEalklgdRIAVMREGRIV 216
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-215 |
3.02e-54 |
|
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: 173.68 E-value: 3.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniakyRRGL 81
Cdd:cd03296 3 IEVRNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-----ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRV----IKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSERPpeaeIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-213 |
1.30e-53 |
|
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: 169.87 E-value: 1.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRG 80
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL---DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLkDRNIYENIafalrvtetptrvikkkvpaalslvglaqkyksfpkeLSGGEQQRVAIARAIVNEPAILL 160
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKeANERGTTVLVVTHNQEIVNEMNeRVITMKQG 213
Cdd:cd03228 120 LDEATSALDPETEALILEALR-ALAKGKTVIVIAHRLSTIRDAD-RIIVLDDG 170
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-216 |
5.09e-53 |
|
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: 170.94 E-value: 5.09e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRGL 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ---DPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGL-----AQKYksfPKELSGGEQQRVAIARAIVNEP 156
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpaefADRY---PHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-218 |
8.28e-53 |
|
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: 168.00 E-value: 8.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKyrrglg 82
Cdd:cd03214 1 EVENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELAR------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 vvfqdfrllkdrniyeNIAFalrvtetptrvikkkVPAALSLVGLAQ-KYKSFpKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03214 74 ----------------KIAY---------------VPQALELLGLAHlADRPF-NELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
2.70e-51 |
|
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: 164.11 E-value: 2.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmkHRNIAKYRRGL 81
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIafalrvtetptrvikkkvpaalslvglaqkyksfpkELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-218 |
3.18e-51 |
|
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: 166.07 E-value: 3.18e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkyRRGL 81
Cdd:cd03219 1 LEVRGLTKRF-GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPT----------RVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARA 151
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 152 IVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-215 |
4.63e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 169.74 E-value: 4.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhrNIAKYRRGL 81
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-----HVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKAlQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
16-216 |
7.44e-51 |
|
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: 166.28 E-value: 7.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 16 AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG-LGVVFQDFRLLKDR 94
Cdd:cd03294 38 VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 95 NIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSW 174
Cdd:cd03294 118 TVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505341235 175 EIMS-LLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03294 198 EMQDeLLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-216 |
1.30e-50 |
|
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: 172.64 E-value: 1.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRGL 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL---DPASWRRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDrNIYENIAFAlRVTETPTRVIkkkvpAALSLVGLAQKYKSFPK-------E----LSGGEQQRVAIAR 150
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLG-RPDASDEELE-----AALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANeRGTTVLVVTHNQEIVNEMNeRVITMKQGVIV 216
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQAD-RILVLDDGRIV 550
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-218 |
2.55e-50 |
|
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: 164.53 E-value: 2.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGqnLNRMKHRNIAKYRRG 80
Cdd:TIGR04520 1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDfrllKDRNIY-----ENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:TIGR04520 79 VGMVFQN----PDNQFVgatveDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNqeivneMNE-----RVITMKQGVIVSD 218
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNkEEGITVISITHD------MEEavladRVIVMNKGKIVAE 217
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-218 |
2.56e-50 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 163.39 E-value: 2.56e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYskGHAALNgVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrniAKYRRG 80
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL-----PPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDElCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAAD 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-213 |
3.60e-50 |
|
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: 160.49 E-value: 3.60e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniaKYRRGLG 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE---ELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 VVFQdfrllkdrniyeniafalrvtetptrvikkkvpaalslvglaqkyksfpkeLSGGEQQRVAIARAIVNEPAILLAD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505341235 163 EPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-218 |
8.90e-50 |
|
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: 161.55 E-value: 8.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniakyrrgLG 82
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR--------IG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 VVFQDFRLLKDRNI--YENIAFAL----RVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:cd03235 72 YVPQRRSIDRDFPIsvRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-215 |
4.98e-49 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 163.72 E-value: 4.98e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYskGHAA-LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNiakyrRG 80
Cdd:PRK10851 3 IEIANIKKSF--GRTQvLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVT---ETPTR-VIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:PRK10851 76 VGFVFQHYALFRHMTVFDNIAFGLTVLprrERPNAaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANE--RGTTVLvVTHNQEIVNEMNERVITMKQGVI 215
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVF-VTHDQEEAMEVADRVVVMSQGNI 215
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-216 |
9.77e-49 |
|
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: 159.81 E-value: 9.77e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHaaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhrNIAKYRRGL 81
Cdd:cd03299 1 LKVENLSKDWKEFK--LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEA-NERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
9.91e-49 |
|
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: 156.65 E-value: 9.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhRNIAKYRRGLGVVFQDFRLLKDRNIY 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD---DERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 98 ENIAFALRVTETPTRVIKKKVPAALSLVGL----AQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-216 |
5.61e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 165.72 E-value: 5.61e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRGL 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL---TLESLRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLkDRNIYENIAFAlRVTETPTRVIkkkvpAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIAR 150
Cdd:COG1132 417 GVVPQDTFLF-SGTIRENIRYG-RPDATDEEVE-----EAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANeRGTTVLVVTHNQEIVNEMNeRVITMKQGVIV 216
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNAD-RILVLDDGRIV 553
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-216 |
1.41e-47 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 157.22 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRN-----IA 75
Cdd:PRK11264 3 AIEVKNLVKKF-HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSqqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 KYRRGLGVVFQDFRLLKDRNIYENIafalrvTETPtrVIKKKVPAA---------LSLVGLAQKYKSFPKELSGGEQQRV 146
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENI------IEGP--VIVKGEPKEeatararelLAKVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 147 AIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-218 |
5.87e-47 |
|
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: 155.58 E-value: 5.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkyRRG 80
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA--RLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPT---------------RVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQR 145
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreeREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-215 |
6.58e-47 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 155.73 E-value: 6.58e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLI-MKElNPTEGTIIVNGQNLnRMKH-------- 71
Cdd:COG4598 8 ALEVRDLHKSFG-DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCInLLE-TPDSGEIRVGGEEI-RLKPdrdgelvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 72 ---RNIAKYRRGLGVVFQDFRLLKDRNIYENiafalrVTETPTRVikKKVPAA---------LSLVGLAQKYKSFPKELS 139
Cdd:COG4598 85 adrRQLQRIRTRLGMVFQSFNLWSHMTVLEN------VIEAPVHV--LGRPKAeaieraealLAKVGLADKRDAYPAHLS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 140 GGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:COG4598 157 GGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-216 |
1.15e-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: 157.89 E-value: 1.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrniAKYRRGL 81
Cdd:TIGR03265 5 LSIDNIRKRFGA-FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRL-----PPQKRDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:TIGR03265 79 GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 162 DEPTGNLDPTN----SWEIMSLLKEAnerGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:TIGR03265 159 DEPLSALDARVrehlRTEIRQLQRRL---GVTTIMVTHDQEEALSMADRIVVMNHGVIE 214
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-218 |
2.07e-45 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 159.89 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGH---AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:PRK10535 4 LLELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRG-LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:PRK10535 84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMnERVITMKQGVIVSD 218
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQA-ERVIEIRDGEIVRN 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-216 |
2.27e-45 |
|
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: 157.92 E-value: 2.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY--SKG--------HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKeLNPTEGTIIVNGQNLNRMKH 71
Cdd:COG4172 276 LEARDLKVWFpiKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 72 RNIAKYRRGLGVVFQD-FRLLKDR-NIYENIAFALRV--TETPTRVIKKKVPAALSLVGL----AQKYksfPKELSGGEQ 143
Cdd:COG4172 355 RALRPLRRRMQVVFQDpFGSLSPRmTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdpaaRHRY---PHEFSGGQR 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 144 QRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDlQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-216 |
2.31e-45 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 153.73 E-value: 2.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY---------SKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKH 71
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 72 RNIAKYRRGLGVVFQD-FRLLKDR-NIYENIAFALRV-TETPTRVIKKKVPAALSLVGLAQKYKS-FPKELSGGEQQRVA 147
Cdd:COG4608 88 RELRPLRRRMQMVFQDpYASLNPRmTVGDIIAEPLRIhGLASKAERRERVAELLELVGLRPEHADrYPHEFSGGQRQRIG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDlQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIV 237
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-216 |
2.64e-45 |
|
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: 150.84 E-value: 2.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmKHRNIAKYRRGL 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDrNIYENIAFAlRVTETPTRVIKKKVPAAL--SLVGLAQKYKSFPKE----LSGGEQQRVAIARAIVNE 155
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRYG-RPDATDEEVIEAAKAAQIhdKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLkEANERGTTVLVVTHN-QEIVNEmnERVITMKQGVIV 216
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAAL-RDVSKGRTTIVIAHRlSTIVNA--DKIIVLKDGRIV 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-216 |
4.42e-45 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 150.55 E-value: 4.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLimkeLN----PTEGTIIVNGQNLN---RMKHRNI 74
Cdd:COG4161 3 IQLKNINCFYGS-HQALFDINLECPSGETLVLLGPSGAGKSSLLRV----LNlletPDSGQLNIAGHQFDfsqKPSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 75 AKYRRGLGVVFQDFRLLKDRNIYENIafalrvTETPTRVIKKKVPAA-------LSLVGLAQKYKSFPKELSGGEQQRVA 147
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENL------IEAPCKVLGLSKEQArekamklLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-216 |
1.00e-44 |
|
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: 156.85 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRG 80
Cdd:COG4987 334 LELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL---DEDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIAFAlRVTETPTRVIkkkvpAALSLVGLAQKYKSFPK-------E----LSGGEQQRVAIA 149
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRLA-RPDATDEELW-----AALERVGLGDWLAALPDgldtwlgEggrrLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHNQEIVNEMNeRVITMKQGVIV 216
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLAGLERMD-RILVLEDGRIV 548
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-216 |
2.51e-44 |
|
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: 148.60 E-value: 2.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLI--MKELNP---TEGTIIVNGQNLNRmKHRNIAK 76
Cdd:TIGR00972 2 IEIENLNLFYGEKEA-LKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrMNDLVPgvrIEGKVLFDGQDIYD-KKIDVVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQDFRLLKdRNIYENIAFALRVTETPTR-VIKKKVPAALSLVGLAQKYKS----FPKELSGGEQQRVAIARA 151
Cdd:TIGR00972 80 LRRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKkELDEIVEESLKKAALWDEVKDrlhdSALGLSGGQQQRLCIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 152 IVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERgTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:TIGR00972 159 LAVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELV 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-216 |
3.70e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 149.43 E-value: 3.70e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG----HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmKHRNIAKY 77
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQ--DFRLLKDrNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQ---KYKSfPKELSGGEQQRVAIARAI 152
Cdd:PRK13637 82 RKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedyKDKS-PFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-216 |
3.84e-44 |
|
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: 146.95 E-value: 3.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVfIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHrniaKYRRGL 81
Cdd:cd03264 1 LQLENLTKRYGKKRA-LDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ----KLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANErGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-215 |
6.29e-44 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 150.76 E-value: 6.29e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRM--KHRNIAkyr 78
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELepADRDIA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 rglgVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAI 158
Cdd:PRK11650 80 ----MVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 159 LLADEPTGNLDP----TNSWEIMSLLKEAnerGTTVLVVTHNQeiVNEMN--ERVITMKQGVI 215
Cdd:PRK11650 156 FLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQ--VEAMTlaDRVVVMNGGVA 213
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-218 |
1.22e-43 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 149.18 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 33 IVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhrNIAKYRRGLGVVFQDFRLLKDRNIYENIAFALRVTETPTR 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT-----NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 113 VIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDpTNSWEIMSL-LKEANER-GTTV 190
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD-KKLRDQMQLeLKTIQEQlGITF 154
|
170 180
....*....|....*....|....*...
gi 505341235 191 LVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQI 182
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-216 |
2.46e-43 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 145.93 E-value: 2.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLimkeLN----PTEGTIIVNGQNLNRMKHRN---I 74
Cdd:PRK11124 3 IQLNGINCFYGA-HQALFDITLDCPQGETLVLLGPSGAGKSSLLRV----LNllemPRSGTLNIAGNHFDFSKTPSdkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 75 AKYRRGLGVVFQDFRLLKDRNIYENIafalrvTETPTRVI-------KKKVPAALSLVGLAQKYKSFPKELSGGEQQRVA 147
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNL------IEAPCRVLglskdqaLARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-218 |
2.95e-43 |
|
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: 144.94 E-value: 2.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYskGHAALNgVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNlnrMKHRNIAkyRRGL 81
Cdd:cd03298 1 VRLDKIRFSY--GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVD---VTAAPPA--DRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03298 73 SMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-198 |
6.65e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 145.39 E-value: 6.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKG---HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNL-----NRmkhr 72
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgaDR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 73 niakyrrglGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAI 152
Cdd:COG4525 79 ---------GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505341235 153 VNEPAILLADEPTGNLDPTNSwEIMS--LLKEANERGTTVLVVTHNQE 198
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTR-EQMQelLLDVWQRTGKGVFLITHSVE 196
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
7.61e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 146.38 E-value: 7.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA----ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLN---------- 67
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKnkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 68 -----------RMKHRNIAKYRRGLGVVFQ--DFRLLKDrNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKY-KS 133
Cdd:PRK13651 83 vleklviqktrFKKIKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYlQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 134 FPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
....*
gi 505341235 214 VIVSD 218
Cdd:PRK13651 242 KIIKD 246
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-218 |
2.21e-42 |
|
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: 142.82 E-value: 2.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 28 GEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLN-RMKHRNIAKYRRGLGVVFQDFRLLKDRNIYENIAFALRV 106
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFdSRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 107 TETptRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANER 186
Cdd:cd03297 103 KRN--REDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKN 180
|
170 180 190
....*....|....*....|....*....|...
gi 505341235 187 -GTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:cd03297 181 lNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-216 |
3.32e-42 |
|
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: 142.57 E-value: 3.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkyRRGL 81
Cdd:cd03224 1 LEVENLNAGYGKSQI-LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--RAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTetPTRVIKKKVPAALSLV-GLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-216 |
3.34e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 146.90 E-value: 3.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrniAKYRRG 80
Cdd:PRK11607 19 LLEIRNLTKSFD-GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-----PPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 161 ADEPTGNLDPT----NSWEIMSLLkeanER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK11607 173 LDEPMGALDKKlrdrMQLEVVDIL----ERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-216 |
9.65e-42 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 144.86 E-value: 9.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkHRNIAKyrRGL 81
Cdd:PRK11432 7 VVLKNITKRFGS-NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQ--RDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-218 |
1.17e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 142.22 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTkeYSKGHAA-LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRr 79
Cdd:PRK13548 2 MLEARNLS--VRLGGRTlLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 glGVVFQdfrllkdrniYENIAFALRVTE------TPTRVIKKK----VPAALSLVGLAQ-KYKSFPkELSGGEQQRVAI 148
Cdd:PRK13548 79 --AVLPQ----------HSSLSFPFTVEEvvamgrAPHGLSRAEddalVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 149 ARAIV------NEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHnqeivnEMN------ERVITMKQGVI 215
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLH------DLNlaaryaDRIVLLHQGRL 219
|
...
gi 505341235 216 VSD 218
Cdd:PRK13548 220 VAD 222
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
10-216 |
2.05e-41 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 144.22 E-value: 2.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 10 EYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRR-GLGVVFQDF 88
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 89 RLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNL 168
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 169 DPTNSWEIM-SLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:TIGR01186 161 DPLIRDSMQdELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIV 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-207 |
5.66e-41 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 139.53 E-value: 5.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALN---GVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKY 77
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSiltGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 R-RGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:PRK10584 86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERV 207
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIADLLFSLNrEHGTTLILVTHDLQLAARCDRRL 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
15-216 |
8.18e-41 |
|
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: 145.98 E-value: 8.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 15 HAALNGVSVKIERGEFVFIVGDSGSGKS----TLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYR-RGLGVVFQD-- 87
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 88 ------FRLlkDRNIYENIAFALRVTETPTRvikKKVPAALSLVGL---AQKYKSFPKELSGGEQQRVAIARAIVNEPAI 158
Cdd:COG4172 103 tslnplHTI--GKQIAEVLRLHRGLSGAAAR---ARALELLERVGIpdpERRLDAYPHQLSGGQRQRVMIAMALANEPDL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 159 LLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG4172 178 LIADEPTTALDVTVQAQILDLLKDlQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-195 |
3.45e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.84 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmkHRNIAKYRRG 80
Cdd:COG4133 2 MLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTetPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALY--GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH 195
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-218 |
4.66e-40 |
|
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: 136.95 E-value: 4.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRG 80
Cdd:cd03245 3 IEFRNVSFSYpNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIAFALRVTETptrvikKKVPAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIA 149
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITLGAPLADD------ERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHNQEIVnEMNERVITMKQGVIVSD 218
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVAD 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-222 |
5.27e-40 |
|
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: 138.01 E-value: 5.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY-------SKGHAA-LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHR 72
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgAKQRAPvLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 73 NIAKYRRGLGVVFQDF------RLLKDRNIYENIAFALRVTETPTrviKKKVPAALSLVGL----AQKYksfPKELSGGE 142
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSpsavnpRMTVRQIIGEPLRHLTSLDESEQ---KARIAELLDMVGLrsedADKL---PRQLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 143 QQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEKK 221
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDV 235
|
.
gi 505341235 222 G 222
Cdd:TIGR02769 236 A 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-213 |
6.27e-40 |
|
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: 136.48 E-value: 6.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmkHRNIAKYRRG 80
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
17-216 |
1.29e-39 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 137.91 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhrNIAKYRRGLGVVFQDFRLLKDRNI 96
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR----EPRKVRRSIGIVPQYASVDEDLTG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 97 YENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEI 176
Cdd:TIGR01188 84 RENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505341235 177 MSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:TIGR01188 164 WDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRII 203
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-196 |
2.06e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 136.32 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLI--MKELNP---TEGTIIVNGQNLNRmKHRNIAK 76
Cdd:COG1117 12 IEVRNLNVYYGDKQA-LKDINLDIPENKVTALIGPSGCGKSTLLRCLnrMNDLIPgarVEGEILLDGEDIYD-PDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQdfrllkdR-N-----IYENIAFALRVTE-TPTRVIKKKVPAALSLVGL----AQKYKSFPKELSGGEQQR 145
Cdd:COG1117 90 LRRRVGMVFQ-------KpNpfpksIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERgTTVLVVTHN 196
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHN 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
2.16e-39 |
|
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: 133.50 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNiakYRRG 80
Cdd:cd03246 1 LEVENVSFRYPGAePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE---LGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIafalrvtetptrvikkkvpaalslvglaqkyksfpkeLSGGEQQRVAIARAIVNEPAILL 160
Cdd:cd03246 78 VGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMnERVITMKQGVI 215
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-215 |
3.65e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 135.87 E-value: 3.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRnvtKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRN------- 73
Cdd:PRK10619 8 VIDLH---KRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvad 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 74 ---IAKYRRGLGVVFQDFRLLKDRNIYENiafalrVTETPTRVI-------KKKVPAALSLVGLAQKYK-SFPKELSGGE 142
Cdd:PRK10619 84 knqLRLLRTRLTMVFQHFNLWSHMTVLEN------VMEAPIQVLglskqeaRERAVKYLAKVGIDERAQgKYPVHLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 143 QQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-216 |
3.66e-39 |
|
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: 134.42 E-value: 3.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhrNIAKYRRGL 81
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 162 DEPTGNLDPTNS---WEIMSLLKEanERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03265 156 DEPTIGLDPQTRahvWEYIEKLKE--EFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-217 |
3.73e-39 |
|
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: 134.66 E-value: 3.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhrnIAKYRRGL 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDrNIYENIAFAlRVTETPTRVIK--KKVPAALSLVGLAQKYKSFPKE----LSGGEQQRVAIARAIVNE 155
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLG-RPNATDEEVIEaaKEAGAHDFIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 156 PAILLADEPTGNLDPtnswEIMSLLKEANER---GTTVLVVTHNQEIVNEMnERVITMKQGVIVS 217
Cdd:cd03254 158 PKILILDEATSNIDT----ETEKLIQEALEKlmkGRTSIIIAHRLSTIKNA-DKILVLDDGKIIE 217
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
3.96e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 135.98 E-value: 3.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhRNIAKYRRG 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDK-KSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQ--DFRLLKDRnIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAI 158
Cdd:PRK13639 80 VGIVFQnpDDQLFAPT-VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 159 LLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIK 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-222 |
4.75e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 135.60 E-value: 4.75e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKG----HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAK 76
Cdd:COG1101 1 MLELKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YrrgLGVVFQD------FRLlkdrNIYENIAFALRVTETPT---RVIKKKVP------AALSLvGLAQKYKSFPKELSGG 141
Cdd:COG1101 81 Y---IGRVFQDpmmgtaPSM----TIEENLALAYRRGKRRGlrrGLTKKRRElfrellATLGL-GLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 142 EQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEA-NERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD-- 218
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDvs 232
|
....*.
gi 505341235 219 --EKKG 222
Cdd:COG1101 233 geEKKK 238
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-216 |
9.15e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 135.62 E-value: 9.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkY--- 77
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIG-Ylpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLgvvfqdfrlLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:COG4152 79 ERGL---------YPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG4152 150 LLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKV 208
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
9.95e-39 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.47 E-value: 9.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTkeYSKGHAA-LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRr 79
Cdd:COG4559 1 MLEAENLS--VRLGGRTlLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 glGVVFQDFRLlkdrniyeniAFALRVTE----------TPTRVIKKKVPAALSLVG---LAQKykSFPkELSGGEQQRV 146
Cdd:COG4559 78 --AVLPQHSSL----------AFPFTVEEvvalgraphgSSAAQDRQIVREALALVGlahLAGR--SYQ-TLSGGEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 147 AIARAIV-------NEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHnqeivnEMN------ERVITMKQG 213
Cdd:COG4559 143 QLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH------DLNlaaqyaDRILLLHQG 216
|
....*
gi 505341235 214 VIVSD 218
Cdd:COG4559 217 RLVAQ 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-218 |
4.24e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 132.01 E-value: 4.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkgHAALNgVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNlnrmkHRNIAKYRRG 80
Cdd:PRK10771 1 MLKLTDITWLYH--HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-----HTTTPPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQvCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-210 |
4.99e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 131.45 E-value: 4.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKeYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNP---TEGTIIVNGQNLNRmkhrnIAKY 77
Cdd:COG4136 1 MLSLENLTI-TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTA-----LPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQDFRLLKDRNIYENIAFALRvtETPTRVIKKK-VPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLAFALP--PTIGRAQRRArVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSL-LKEANERGTTVLVVTHNQEIVnEMNERVITM 210
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHDEEDA-PAAGRVLDL 206
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
6.23e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 133.05 E-value: 6.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhRNIAKYRRG 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR-KGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQD-FRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:PRK13636 84 VGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEmQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVI 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-218 |
7.61e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 132.90 E-value: 7.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKG-----HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGqnLNRMKHRNIA 75
Cdd:PRK13633 4 MIKCKNVSYKYESNeesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 KYRRGLGVVFQDfrllKDRNIY-----ENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIAR 150
Cdd:PRK13633 82 DIRNKAGMVFQN----PDNQIVativeEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNeRVITMKQGVIVSD 218
Cdd:PRK13633 158 ILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEAD-RIIVMDSGKVVME 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-224 |
7.69e-38 |
|
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: 131.51 E-value: 7.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY--SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRR 79
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDFRLLkDRNIYENIAFALR-VTETPTRVIKKKVPAALSLVGLAQKYKSF--PK--ELSGGEQQRVAIARAIVN 154
Cdd:cd03249 78 QIGLVSQEPVLF-DGTIAENIRYGKPdATDEEVEEAAKKANIHDFIMSLPDGYDTLvgERgsQLSGGQKQRIAIARALLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 155 EPAILLADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHNQEIVNEMnERVITMKQGVIVS----DE---KKGGY 224
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRNA-DLIAVLQNGQVVEqgthDElmaQKGVY 231
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-225 |
8.61e-38 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 134.77 E-value: 8.61e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYSKGHAALNgVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhrNIAKYRRGLGV 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-----DVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 84 VFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADE 163
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 164 PTGNLDPT----NSWEIMSLLKEAnerGTTVLVVTHNQeiVNEMnerviTMKQGVIVSDekkGGYI 225
Cdd:PRK11000 160 PLSNLDAAlrvqMRIEISRLHKRL---GRTMIYVTHDQ--VEAM-----TLADKIVVLD---AGRV 212
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-216 |
9.25e-38 |
|
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: 131.26 E-value: 9.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMK-HRnIAkyRR 79
Cdd:COG0410 3 MLEVENLHAGYGGIHV-LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPpHR-IA--RL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDFRLLKDRNIYENIAFALRvtetpTRVIKKKVPAALSLVglaqkYKSFP--KE--------LSGGEQQRVAIA 149
Cdd:COG0410 79 GIGYVPEGRRIFPSLTVEENLLLGAY-----ARRDRAEVRADLERV-----YELFPrlKErrrqragtLSGGEQQMLAIG 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIV 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-217 |
1.35e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 132.16 E-value: 1.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKG--HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhRNIAKYR 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 RGLGVVFQ--DFRLLkDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:PRK13650 81 HKIGMVFQnpDNQFV-GATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVnEMNERVITMKQGVIVS 217
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVES 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-199 |
3.50e-37 |
|
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: 128.69 E-value: 3.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 11 YSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhRNIAKYRRGLGVVFQ--DF 88
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSR-KGLLERRQRVGLVFQdpDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 89 RLLKDRnIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNL 168
Cdd:TIGR01166 80 QLFAAD-VDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|.
gi 505341235 169 DPTNSWEIMSLLKEANERGTTVLVVTHNQEI 199
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-216 |
4.43e-37 |
|
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: 129.66 E-value: 4.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSK-GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhrnIAKYRRG 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIAFALRvTETPTRVIkkkvpAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIA 149
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAYGRP-GATREEVE-----EAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 150 RAIVNEPAILLADEPTGNLDPtnswEIMSLLKEANER---GTTVLVVTHNQEIVnEMNERVITMKQGVIV 216
Cdd:cd03251 151 RALLKDPPILILDEATSALDT----ESERLVQAALERlmkNRTTFVIAHRLSTI-ENADRIVVLEDGKIV 215
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-215 |
6.27e-37 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.80 E-value: 6.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmkhrniAKYRRGLGV 83
Cdd:PRK11247 15 LNAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL--------AEAREDTRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 84 VFQDFRLLKDRNIYENIAFALRVTETPtrvikkKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADE 163
Cdd:PRK11247 86 MFQDARLLPWKKVIDNVGLGLKGQWRD------AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 164 PTGNLDPTNSWEIMSLLKEA-NERGTTVLVVTHNqeiVNE---MNERVITMKQGVI 215
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwQQHGFTVLLVTHD---VSEavaMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
7.56e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.11 E-value: 7.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhRNIAKYRR 79
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDfrllKDR-----NIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVN 154
Cdd:PRK13632 84 KIGIIFQN----PDNqfigaTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 155 EPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHN-QEIVNEmnERVITMKQGVIV 216
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISITHDmDEAILA--DKVIVFSEGKLI 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-216 |
1.11e-36 |
|
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: 127.78 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhrnIAKYRRgL 81
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD------IAARNR-I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-213 |
3.26e-36 |
|
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: 127.20 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNL-----NRMkhrniakyrrglgVVFQDFRLLK 92
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepgpDRM-------------VVFQNYSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 93 DRNIYENIAFAL-RVTETPTRVIKKK-VPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDP 170
Cdd:TIGR01184 68 WLTVRENIALAVdRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505341235 171 TNSWEIMS-LLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:TIGR01184 148 LTRGNLQEeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
3.96e-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: 133.18 E-value: 3.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmKHRNIAKYRRGL 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPL---ADADADSWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDrNIYENIAFALRVTeTPTRVIkkkvpAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIAR 150
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRLARPDA-SDAEIR-----EALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHNQEIVNEMnERVITM 210
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-221 |
5.28e-36 |
|
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: 127.12 E-value: 5.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEG-TIIVNGQNLNRMkhrNIAKYRR 79
Cdd:COG1119 3 LLELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGE---DVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDF--RLLKDRNIYENI---AFA-LRVTETPTRVIKKKVPAALSLVGLAQ-KYKSFpKELSGGEQQRVAIARAI 152
Cdd:COG1119 79 RIGLVSPALqlRFPRDETVLDVVlsgFFDsIGLYREPTDEQRERARELLELLGLAHlADRPF-GTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHN-QEIVNEMNeRVITMKQGVIVSDEKK 221
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTHHvEEIPPGIT-HVLLLKDGRVVAAGPK 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
8.28e-36 |
|
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: 124.08 E-value: 8.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhRNIAKYRR-G 80
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF---ASPRDARRaG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQdfrllkdrniyeniafalrvtetptrvikkkvpaalslvglaqkyksfpkeLSGGEQQRVAIARAIVNEPAILL 160
Cdd:cd03216 77 IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-227 |
1.49e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 126.67 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIK----LIMKELNPtEGTIIVNGQNLNRMKH--RNI 74
Cdd:PRK09984 4 IIRVEKLAKTFNQ-HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIELLGRTVQREGRlaRDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 75 AKYRRGLGVVFQDFRLLKDRNIYENIAFAlRVTETP---------TRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQR 145
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEKKGGY 224
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
...
gi 505341235 225 INE 227
Cdd:PRK09984 241 DNE 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-216 |
1.72e-35 |
|
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: 131.87 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRGL 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDrNIYENIAFAlRVTETPTRVIKKKVPAALS--LVGLAQKYKSFPKE----LSGGEQQRVAIARAIVNE 155
Cdd:COG5265 435 GIVPQDTVLFND-TIAYNIAYG-RPDASEEEVEAAARAAQIHdfIESLPDGYDTRVGErglkLSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHN-QEIVNEmnERVITMKQGVIV 216
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRlSTIVDA--DEILVLEAGRIV 571
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-223 |
1.87e-35 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 126.34 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKG--------HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHR 72
Cdd:PRK10419 3 LLNVSGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 73 NIAKYRRGLGVVFQDF------RllkdRNIYENIAFALR-VTETPTRVIKKKVPAALSLVGLAQKYKS-FPKELSGGEQQ 144
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisavnpR----KTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDkRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 145 RVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEKKGG 223
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGD 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-216 |
2.31e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 126.26 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGqnLNRMKHRNIAKYRRG 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRL-LKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:PRK13644 79 VGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMnERVITMKQGVIV 216
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIV 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-217 |
3.43e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 125.90 E-value: 3.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkHRNIAKYRRG 80
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS---EETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDfrllKDRN-----IYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:PRK13635 83 VGMVFQN----PDNQfvgatVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNeRVITMKQGVIVS 217
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQAD-RVIVMNKGEILE 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
3.59e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 126.07 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhRNIAKYRRG 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDfrllKDRNIY-----ENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:PRK13652 80 VGLVFQN----PDDQIFsptveQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVA 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-216 |
4.00e-35 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 130.21 E-value: 4.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 15 HAALNGVSVKIERGEFVFIVGDSGSGKST----LIKLImkelnPTEGTIIVNGQNLNRMKHRNIAKYRRGLGVVFQD-FR 89
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 90 LLKDR-NIYENIAFALRV-------TETPTRVIkkkvpAALSLVGL-AQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:PRK15134 374 SLNPRlNVLQIIEEGLRVhqptlsaAQREQQVI-----AVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-213 |
4.21e-35 |
|
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: 127.52 E-value: 4.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 21 VSVKIERGEFVF-------------IVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNL-NRMKHRNIAKYRRGLGVVFQ 86
Cdd:COG4148 5 VDFRLRRGGFTLdvdftlpgrgvtaLFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPPHRRRIGYVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 87 DFRLLKDRNIYENIAFALRVTETPTRVIKkkVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTG 166
Cdd:COG4148 85 EARLFPHLSVRGNLLYGRKRAPRAERRIS--FDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505341235 167 NLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:COG4148 163 ALDLARKAEILPYLERlRDELDIPILYVSHSLDEVARLADHVVLLEQG 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-216 |
4.38e-35 |
|
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: 123.52 E-value: 4.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmKHRniakyRRGLG 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA-KER-----RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 VVFQDFrllkDRNIYENIAFA-LRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03226 75 YVMQDV----DYQLFTDSVREeLLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
4.55e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 126.50 E-value: 4.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTI----IVNGQNL---------NRMKHRNIAKYRRGLGV 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKnnhelitnpYSKKIKNFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 84 VFQ--DFRLLKDrNIYENIAF---ALRVTETPTRvikKKVPAALSLVGLAQKY-KSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFgpvALGVKKSEAK---KLAKFYLNKMGLDDSYlERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
5.59e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 125.52 E-value: 5.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNL-NRMKHRNIAKYRRGLGVVFQdF--RLLKD 93
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLRKKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 94 RNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKY--KSfPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPT 171
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlaRS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505341235 172 NSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK13634 180 GRKEMMEMFYKLHkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVF 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-218 |
6.56e-35 |
|
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: 124.14 E-value: 6.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRG 80
Cdd:cd03252 1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDfRLLKDRNIYENIAFAlrvTETPTRvikKKVPAALSLVG-------LAQKYKSFPKE----LSGGEQQRVAIA 149
Cdd:cd03252 78 VGVVLQE-NVLFNRSIRDNIALA---DPGMSM---ERVIEAAKLAGahdfiseLPEGYDTIVGEqgagLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANErGTTVLVVTHNQEIVNEMNeRVITMKQGVIVSD 218
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNAD-RIIVMEKGRIVEQ 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-213 |
1.92e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 124.17 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA----ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLN-RMKHRNIAK 76
Cdd:PRK13641 3 IKFENVDYIYSPGTPmekkGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQ--DFRLLKDrNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKY--KSfPKELSGGEQQRVAIARAI 152
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKS-PFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-216 |
2.08e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 124.09 E-value: 2.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG----HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNL-NRMKHRNIAK 76
Cdd:PRK13649 3 INLQNVSYTYQAGtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQdF--RLLKDRNIYENIAFALR----VTETPTRVIKKKvpaaLSLVGLAQK-YKSFPKELSGGEQQRVAIA 149
Cdd:PRK13649 83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQnfgvSQEEAEALAREK----LALVGISESlFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLV 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-216 |
2.29e-34 |
|
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: 128.68 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRG 80
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL---RRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIAFALRVTETPTRVIKKKVPA-ALSLV-----GLAQKYKSFPKELSGGEQQRVAIARAIVN 154
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAYGRTEQADRAEIERALAAAyAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 155 EPAILLADEPTGNLDPTNSWEIMSLLkEANERGTTVLVVTHNQEIVnEMNERVITMKQGVIV 216
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAAL-ERLMQGRTTLVIAHRLSTI-EKADRIVVMDDGRIV 546
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-198 |
3.48e-34 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 122.89 E-value: 3.48e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTII-----VNGQNLNRmkhrnia 75
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpVEGPGAER------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 kyrrglGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:PRK11248 73 ------GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAAN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505341235 156 PAILLADEPTGNLDPTNSwEIMS--LLKEANERGTTVLVVTHNQE 198
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTR-EQMQtlLLKLWQETGKQVLLITHDIE 190
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-216 |
3.64e-34 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 123.02 E-value: 3.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-------SKGH-AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRN 73
Cdd:COG4167 5 LEVRNLSKTFkyrtglfRRQQfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 74 IAKYRRglgVVFQDfrllkdrniyENIAFALRVT-----ETPTRVI--------KKKVPAALSLVGLAQKYKSF-PKELS 139
Cdd:COG4167 85 RCKHIR---MIFQD----------PNTSLNPRLNigqilEEPLRLNtdltaeerEERIFATLRLVGLLPEHANFyPHMLS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 140 GGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
4.19e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 122.92 E-value: 4.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIkLIMKELN-PTEGTIIVNGQNLNRmkhRNIAKYRRG 80
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLL-LHLNGIYlPQRGRVKVMGREVNA---ENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQD-----FrllkDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:PRK13647 81 VGLVFQDpddqvF----SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEKKGGYINED 228
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
8.74e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 122.17 E-value: 8.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkHRNIAKYRR 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQ--DFRLLKDRNIYEnIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:PRK13648 84 HIGIVFQnpDNQFVGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEmNERVITMKQGVI 215
Cdd:PRK13648 163 VIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
1.07e-33 |
|
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: 126.32 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRGL 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLkDRNIYENIAFAlRVTETPtrvikKKVPAALSLVGLAQKYKSFP-----------KELSGGEQQRVAIAR 150
Cdd:TIGR02868 412 SVCAQDAHLF-DTTVRENLRLA-RPDATD-----EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHN 196
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
1.63e-33 |
|
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: 120.23 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY------SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQ----NLNRMK 70
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 71 HRNIAKYRRG-LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQK-YKSFPKELSGGEQQRVAI 148
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 149 ARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-196 |
1.71e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 121.41 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTkeYSKGHAAL-NGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRR 79
Cdd:PRK11831 7 LVDMRGVS--FTRGNRCIfDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDFRLLKDRNIYENIAFALRV-TETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAI 158
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNVAYPLREhTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 505341235 159 LLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHN 196
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHD 203
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-218 |
5.48e-33 |
|
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: 118.62 E-value: 5.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY---SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmkHRNIAKY 77
Cdd:cd03266 1 MITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-217 |
7.29e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 120.11 E-value: 7.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG----HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNL--NRMKHRNIA 75
Cdd:PRK13645 7 IILDNVSYTYAKKtpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 KYRRGLGVVFQ--DFRLLKDrNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKY-KSFPKELSGGEQQRVAIARAI 152
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYvKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIS 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-216 |
1.00e-32 |
|
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: 123.76 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEY---SKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVN-GQNLNRMKHR--- 72
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPgpd 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 73 NIAKYRRGLGVVFQDFRLLKDRNIYENIAFALRVtETPTRVIKKKVPAALSLVGLAQKY-----KSFPKELSGGEQQRVA 147
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIM-SLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-216 |
1.25e-32 |
|
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: 117.76 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIM---KELNPTEGTIIVNGQNLNRmkhrniAKYRRGLGVVFQDFRLLKDR 94
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKP------DQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 95 NIYENIAFA--LRVTETPTRVIKKKVPA--ALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDP 170
Cdd:cd03234 97 TVRETLTYTaiLRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505341235 171 TNSWEIMSLLKEANERGTTVLVVTHN--QEIVnEMNERVITMKQGVIV 216
Cdd:cd03234 177 FTALNLVSTLSQLARRNRIVILTIHQprSDLF-RLFDRILLLSSGEIV 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-216 |
2.81e-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: 116.55 E-value: 2.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhrNIAKYRRgL 81
Cdd:cd03268 1 LKTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK----NIEALRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVvfqdfrLLKDRNIYENIAF--ALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:cd03268 75 GA------LIEAPGFYPNLTAreNLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-216 |
4.71e-32 |
|
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: 121.83 E-value: 4.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLI--MKELNPTEGTIIVN----------------G 63
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskvG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 64 QNL----NRMKHRNI----------AKYRRGLGVVFQ-DFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLA 128
Cdd:TIGR03269 80 EPCpvcgGTLEPEEVdfwnlsdklrRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 129 QKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEA-NERGTTVLVVTHNQEIVNEMNERV 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKA 239
|
....*....
gi 505341235 208 ITMKQGVIV 216
Cdd:TIGR03269 240 IWLENGEIK 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-216 |
7.81e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 116.34 E-value: 7.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKyrrg 80
Cdd:COG4604 1 MIEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 lgvvfqdfRL--LKDRNiyeNIAFALRVTE------------TPTRVIKKKVPAA---LSLVGLAQKYKSfpkELSGGEQ 143
Cdd:COG4604 76 --------RLaiLRQEN---HINSRLTVRElvafgrfpyskgRLTAEDREIIDEAiayLDLEDLADRYLD---ELSGGQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 144 QRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHnqeivnEMN------ERVITMKQGVIV 216
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADELGKTVVIVLH------DINfascyaDHIVAMKDGRVV 215
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-216 |
1.06e-31 |
|
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: 114.57 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKE-----YSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNP--TEGTIIVNGQNLNRmkhrni 74
Cdd:cd03213 4 LSFRNLTVTvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 75 AKYRRGLGVVFQDFRLLKDRNIYENIAFAlrvtetptrvikkkvpAALslvglaqkyksfpKELSGGEQQRVAIARAIVN 154
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFA----------------AKL-------------RGLSGGERKRVSIALELVS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 155 EPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH--NQEIVNeMNERVITMKQGVIV 216
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpSSEIFE-LFDKLLLLSQGRVI 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-217 |
1.29e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 116.80 E-value: 1.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG----HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNL-NRMKHRNIAK 76
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQ--DFRLLKDrNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSF-PKELSGGEQQRVAIARAIV 153
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQsPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 154 NEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVS 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
1.37e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 121.09 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRG 80
Cdd:PRK11160 339 LTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIAFALrvtETPTrviKKKVPAALSLVGLAQKYKSFP----------KELSGGEQQRVAIAR 150
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLAA---PNAS---DEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGIAR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEaNERGTTVLVVTHNQEIVNEMNeRVITMKQGVIV 216
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQFD-RICVMDNGQII 552
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-213 |
1.39e-31 |
|
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: 118.29 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 21 VSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNI-AKYRRGLGVVFQDFRLLKDRNIYEN 99
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 100 IAFALRVTETPTRVIK-KKVPAALSLVGLAQKYksfPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMS 178
Cdd:TIGR02142 96 LRYGMKRARPSERRISfERVIELLGIGHLLGRL---PGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 505341235 179 LLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:TIGR02142 173 YLERlHAEFGIPILYVSHSLQEVLRLADRVVVLEDG 208
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
17-213 |
1.59e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 117.50 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGLGVVFQD-FRLLKDR- 94
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDpLASLNPRm 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 95 NIYENIAFALRV--TETPTRVIKKKVPAALSLVGL-AQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPT 171
Cdd:PRK15079 116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505341235 172 NSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK15079 196 IQAQVVNLLQQlQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-208 |
2.88e-31 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 113.48 E-value: 2.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 14 GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGqnlnrmkhrniakyRRGLGVVFQDFRLlkD 93
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--------------GARVAYVPQRSEV--P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 94 RniyeniAFALRVTET--------------PTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:NF040873 68 D------SLPLTVRDLvamgrwarrglwrrLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVI 208
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVL 190
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-216 |
3.77e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 116.60 E-value: 3.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYS------KGHA---ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLI-MKElNPTEGTIIVNGQNLNRMKH 71
Cdd:PRK11308 6 LQAIDLKKHYPvkrglfKPERlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLtMIE-TPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 72 RNIAKYRRGLGVVFQD-FRLLKDRNIYENI-AFALRVTETPTRVIKK-KVPAALSLVGL-AQKYKSFPKELSGGEQQRVA 147
Cdd:PRK11308 85 EAQKLLRQKIQIVFQNpYGSLNPRKKVGQIlEEPLLINTSLSAAERReKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDlQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-195 |
3.78e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.97 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQnlnRMKHRNIAK-YRR 79
Cdd:COG1129 4 LLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGE---PVRFRSPRDaQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDFRLLKDRNIYENIAFALRVTETPT---RVIKKKVPAALSLVGLaqkykSFP-----KELSGGEQQRVAIARA 151
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGL-----DIDpdtpvGDLSVAQQQLVEIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505341235 152 IVNEPAILLADEPTGNLDPTNS---WEIMSLLKeanERGTTVLVVTH 195
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVerlFRIIRRLK---AQGVAIIYISH 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-196 |
5.01e-31 |
|
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: 113.79 E-value: 5.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNR--MKHRNiakyRR 79
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHKRA----RL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHN 196
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHN 192
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 |
1.29e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 115.31 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNiakyRRGL 81
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA----RARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEKKGGYINE 227
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-217 |
1.80e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 114.06 E-value: 1.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA----ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRM-KHRNIA 75
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 KYRRGLGVVFQ--DFRLLKDrNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKY-KSFPKELSGGEQQRVAIARAI 152
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIIS 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-223 |
2.10e-30 |
|
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: 112.23 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMK-HRNIakyRRGL 81
Cdd:TIGR03410 2 EVSNLNVYYGQSHI-LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERA---RAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQD---FRLLkdrNIYENiafaLRVTETPTRVIKKKVPAALslvglaqkYKSFP--KE--------LSGGEQQRVAI 148
Cdd:TIGR03410 78 AYVPQGreiFPRL---TVEEN----LLTGLAALPRRSRKIPDEI--------YELFPvlKEmlgrrggdLSGGQQQQLAI 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 149 ARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEKKGG 223
Cdd:TIGR03410 143 ARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRlRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-216 |
4.66e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 116.28 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnRMKHRNIAkYRRG 80
Cdd:COG3845 5 ALELRGITKRFG-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDA-IALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRvtETPTRVIKKKVpAALSLVGLAQKYKsFP-------KELSGGEQQRVAIARAIV 153
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGLE--PTKGGRLDRKA-ARARIRELSERYG-LDvdpdakvEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 154 NEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-216 |
9.89e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 113.97 E-value: 9.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 22 SVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRG-LGVVFQDFRLLKDRNIYENI 100
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 101 AFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIM-SL 179
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdEL 207
|
170 180 190
....*....|....*....|....*....|....*..
gi 505341235 180 LKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-216 |
1.07e-29 |
|
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: 115.62 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 16 AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYrrgLGVVFQDFRLLkDRN 95
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH---IGYLPQDVELF-DGT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 96 IYENIAfalRVTE-TPTRVIkkkvpAALSLVG-------LAQKYKSFPKE----LSGGEQQRVAIARAIVNEPAILLADE 163
Cdd:COG4618 422 IAENIA---RFGDaDPEKVV-----AAAKLAGvhemilrLPDGYDTRIGEggarLSGGQRQRIGLARALYGDPRLVVLDE 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 164 PTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNeRVITMKQGVIV 216
Cdd:COG4618 494 PNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVD-KLLVLRDGRVQ 545
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-215 |
1.84e-29 |
|
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: 114.75 E-value: 1.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYrrgLGVVFQDFRLLKDrNIY 97
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH---IGYLPQDVELFPG-TVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 ENIAfalRVTETPTrviKKKVPAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIARAIVNEPAILLADEPTG 166
Cdd:TIGR01842 410 ENIA---RFGENAD---PEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 167 NLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNeRVITMKQGVI 215
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVD-KILVLQDGRI 531
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-218 |
2.48e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 110.57 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAA--LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQnlnRMKHRNIAKYR 78
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 RGLGVVFQD-FRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEmNERVITMKQGVIVSD 218
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
18-222 |
2.56e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 110.48 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhRNIAKYRRGLGVVFQDfrllKDRNIY 97
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSK-RGLLALRQQVATVFQD----PEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 -----ENIAFALRVTETPTRVIKKKVPAALSLVGlAQKYKSFPKE-LSGGEQQRVAIARAIVNEPAILLADEPTGNLDPT 171
Cdd:PRK13638 92 ytdidSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505341235 172 NSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEKKG 222
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPG 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-216 |
2.68e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 114.67 E-value: 2.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRGL 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDfRLLKDRNIYENIafalRV-----TETPTRVIKKKVPAALSLVGLAQKYKSFPKE----LSGGEQQRVAIARAI 152
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNI----RVgrpdaTDEEMRAAAERAQAHDFIERKPDGYDTVVGErgrqLSGGERQRLAIARAL 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANeRGTTVLVVTHNQEIVNEMnERVITMKQGVIV 216
Cdd:PRK13657 487 LKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNA-DRILVFDNGRVV 548
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
2.95e-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: 109.10 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSK--GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniaKYRR 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDfRLLKDRNIYENIAFALrvTETPTRVIKKKVPAALS---LVGLAQKYKSFPKE----LSGGEQQRVAIARAI 152
Cdd:cd03248 89 KVSLVGQE-PVLFARSLQDNIAYGL--QSCSFECVKEAAQKAHAhsfISELASGYDTEVGEkgsqLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANERgTTVLVVTHNQEIVnEMNERVITMKQGVI 215
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPER-RTVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-220 |
6.53e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 109.50 E-value: 6.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGH-AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNP---TEGTIIVNGQNLNRmkhRNIAKY 77
Cdd:PRK13640 6 VEFKHVSFTYPDSKkPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTA---KTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQ--DFRLLkDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:PRK13640 83 REKVGIVFQnpDNQFV-GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNeMNERVITMKQGVIVSDEK 220
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
1.44e-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: 105.86 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhRNIAKYrrg 80
Cdd:cd03247 1 LSINNVSFSYpEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLkDRNIYENIAfalrvtetptrvikkkvpaalslvglaqkyksfpKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:cd03247 77 ISVLNQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHNQEIVNEMNeRVITMKQGVIV 216
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHMD-KILFLENGKII 175
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-218 |
1.80e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.95 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLI--MKELNPT---EGTIIVNGQNLNRmKHRNIAK 76
Cdd:PRK14243 11 LRTENLNVYYGS-FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYA-PDVDPVE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQDFRLLKdRNIYENIAFALRV----------TETPTR--VIKKKVPAALSLVGLAqkyksfpkeLSGGEQQ 144
Cdd:PRK14243 89 VRRRIGMVFQKPNPFP-KSIYDNIAYGARIngykgdmdelVERSLRqaALWDEVKDKLKQSGLS---------LSGGQQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 145 RVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERgTTVLVVTHNqeivnemnervitMKQGVIVSD 218
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHN-------------MQQAARVSD 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-218 |
1.95e-28 |
|
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: 107.03 E-value: 1.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGqnlnRMKHRNIAKYRRGLGVVF-QDFRLLKDRN 95
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKFLRRIGVVFgQKTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 96 IYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWE 175
Cdd:cd03267 112 VIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505341235 176 IMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:cd03267 192 IRNFLKEYNrERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-213 |
4.89e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 107.97 E-value: 4.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNiakyRRGL 81
Cdd:PRK13537 8 IDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA----RQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-216 |
9.44e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 9.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMK--ELNP---TEGTIIVNGQNLNRMkhrNIAK 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEV-LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPearVSGEVYLDGQDIFKM---DVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQDFRLLKDRNIYENIAFALRVTE--TPTRVIKKKVPAALSLVGLAQKYK----SFPKELSGGEQQRVAIAR 150
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLWDEVKdrldAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLvVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVL-VTHFPQQAARISDYVAFLYKGQIV 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-216 |
9.56e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 110.58 E-value: 9.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSK--GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNiakYRR 79
Cdd:TIGR00958 479 IEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHY---LHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDfRLLKDRNIYENIAFALRVTE-TPTRVIKKKVPAALSLVGLAQKYKSFPKE----LSGGEQQRVAIARAIVN 154
Cdd:TIGR00958 556 QVALVGQE-PVLFSGSVRENIAYGLTDTPdEEIMAAAKAANAHDFIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVR 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 155 EPAILLADEPTGNLDPtnswEIMSLLKEANERGT-TVLVVTHNQEIVnEMNERVITMKQGVIV 216
Cdd:TIGR00958 635 KPRVLILDEATSALDA----ECEQLLQESRSRASrTVLLIAHRLSTV-ERADQILVLKKGSVV 692
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-216 |
1.12e-27 |
|
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: 104.88 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniaKYRRG 80
Cdd:cd03244 3 IEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH---DLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDfRLLKDRNIYENIAFALRVTEtptrvikKKVPAALSLVGLAQKYKSFPKEL-----------SGGEQQRVAIA 149
Cdd:cd03244 80 ISIIPQD-PVLFSGTIRSNLDPFGEYSD-------EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANeRGTTVLVVTHNQEIVNEMNeRVITMKQGVIV 216
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAF-KDCTVLTIAHRLDTIIDSD-RILVLDKGRVV 216
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-213 |
1.30e-27 |
|
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: 103.67 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTkeyskGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniAKYRRGLG 82
Cdd:cd03215 6 EVRGLS-----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR--DAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 VVFQDFR---LLKDRNIYENIAFALRvtetptrvikkkvpaalslvglaqkyksfpkeLSGGEQQRVAIARAIVNEPAIL 159
Cdd:cd03215 79 YVPEDRKregLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLVV-THNQEIVnEMNERVITMKQG 213
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLIsSELDELL-GLCDRILVMYEG 180
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-195 |
2.41e-27 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 104.02 E-value: 2.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyrrgl 81
Cdd:TIGR03740 1 LETKNLSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKI------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENiafaLRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:TIGR03740 73 GSLIESPPLYENLTAREN----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLIL 148
|
170 180 190
....*....|....*....|....*....|....
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH 195
Cdd:TIGR03740 149 DEPTNGLDPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-206 |
2.95e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.47 E-value: 2.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLI--MKELNP---TEGTIIVNGQNLNRMKhRNIA 75
Cdd:PRK14239 5 ILQVSDLSVYYNK-KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYSPR-TDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 KYRRGLGVVFQD---FRLlkdrNIYENIAFALRVT-ETPTRVIKKKVPAALSLVGLAQKYKSFPKE----LSGGEQQRVA 147
Cdd:PRK14239 83 DLRKEIGMVFQQpnpFPM----SIYENVVYGLRLKgIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERgTTVLVVTHNQEIVNEMNER 206
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDR 216
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-217 |
3.11e-27 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 106.50 E-value: 3.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 33 IVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHR-NIAKYRRGLGVVFQDFRLLKDRNIYENIAFAlrvtetpt 111
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLPPEKRRIGYVFQDARLFPHYKVRGNLRYG-------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 112 rvIKKKVPA----ALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANER 186
Cdd:PRK11144 101 --MAKSMVAqfdkIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERlAREI 178
|
170 180 190
....*....|....*....|....*....|..
gi 505341235 187 GTTVLVVTHN-QEIVnEMNERVITMKQGVIVS 217
Cdd:PRK11144 179 NIPILYVSHSlDEIL-RLADRVVVLEQGKVKA 209
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-196 |
5.69e-27 |
|
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: 103.51 E-value: 5.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 5 RNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkyRRGLGVV 84
Cdd:TIGR04406 5 ENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERA--RLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 85 FQDFRLLKDRNIYENIAFALRVTETPTR-VIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADE 163
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKDLDRaEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190
....*....|....*....|....*....|...
gi 505341235 164 PTGNLDPTNSWEIMSLLKEANERGTTVLVVTHN 196
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHN 194
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-218 |
1.00e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.40 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYS------------KG--------HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTII 60
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalKGlfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 61 VNGqnLNRMKHRNiaKYRRGLGVVF------------QD-FRLLKDrnIYeniafalrvtETPTRVIKKKVPAALSLVGL 127
Cdd:COG4586 81 VLG--YVPFKRRK--EFARRIGVVFgqrsqlwwdlpaIDsFRLLKA--IY----------RIPDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 128 AQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNER 206
Cdd:COG4586 145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNrERGTTILLTSHDMDDIEALCDR 224
|
250
....*....|..
gi 505341235 207 VITMKQGVIVSD 218
Cdd:COG4586 225 VIVIDHGRIIYD 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-196 |
1.17e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.41 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMK-HRniaKYRR 79
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmHK---RARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQD---FRLLkdrNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:COG1137 79 GIGYLPQEasiFRKL---TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHN 196
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-216 |
3.48e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.56 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 19 NGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELnPT------EGTIIVNGQNLNRMKHRNIAKYR-RGLGVVFQDfrll 91
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQE---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 92 kdrniyeniafaLRVTETPTRVIKKKVPAALSL-------------------VGL---AQKYKSFPKELSGGEQQRVAIA 149
Cdd:PRK15134 101 ------------PMVSLNPLHTLEKQLYEVLSLhrgmrreaargeilncldrVGIrqaAKRLTDYPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRElQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-195 |
6.84e-26 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 104.80 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRGL 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDrNIYENIAFALRVTETptrvikkKVPAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIAR 150
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVTLGRDISEE-------QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALAR 489
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERgTTVLVVTH 195
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREH-TTLVVIAH 533
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-205 |
7.77e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.88 E-value: 7.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKlIMKELNPTEGTIIVNGQ----NLNRMKHR-NIAK 76
Cdd:PRK14258 8 IKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRveffNQNIYERRvNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQDFRLLKdRNIYENIAFALRVTE-TPTRVIKKKVPAALSLVGL----AQKYKSFPKELSGGEQQRVAIARA 151
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 152 IVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGT-TVLVVTHNQEIVNEMNE 205
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSD 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
18-210 |
8.13e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniaKYRRGLGVVFQDFRLLKDrNIY 97
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYRQQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 ENIAFALRV-TETPTRvikKKVPAALSLVGLAQKYKSFP-KELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWE 175
Cdd:PRK10247 99 DNLIFPWQIrNQQPDP---AIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHN 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 505341235 176 IMSLLKE-ANERGTTVLVVTHNQEIVNEMNErVITM 210
Cdd:PRK10247 176 VNEIIHRyVREQNIAVLWVTHDKDEINHADK-VITL 210
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-210 |
9.04e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 102.29 E-value: 9.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA---ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNP----TEGTIIVNGQNLNRM---K 70
Cdd:COG4170 3 LLDIRNLTIEIDTPQGrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLsprE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 71 HRNIAkyRRGLGVVFQDFRLLKD--RNIYENIAFALrvtetPTRVI-----------KKKVPAALSLVGLaQKYK----S 133
Cdd:COG4170 83 RRKII--GREIAMIFQEPSSCLDpsAKIGDQLIEAI-----PSWTFkgkwwqrfkwrKKRAIELLHRVGI-KDHKdimnS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 134 FPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANE-RGTTVLVVTHNQEIVNEMNERVITM 210
Cdd:COG4170 155 YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVL 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-217 |
1.61e-25 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 100.34 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGL 81
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNI----YENIAFaLRVTETPTRVIkkkVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:PRK15056 87 EEVDWSFPVLVEDVVmmgrYGHMGW-LRRAKKRDRQI---VTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLAS 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-224 |
1.66e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVnGQNLNrmkhrniakyrrg 80
Cdd:COG0488 315 VLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK------------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLK-DRNIYENIA-FALRVTETPTR-----------VIKKKVpaalslvglaqkyksfpKELSGGEQQRVA 147
Cdd:COG0488 380 IGYFDQHQEELDpDKTVLDELRdGAPGGTEQEVRgylgrflfsgdDAFKPV-----------------GVLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPtnswEIMSLLKEA-NERGTTVLVVTHNQEIVNEMNERVITMKQGVIVsdEKKGGY 224
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDI----ETLEALEEAlDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR--EYPGGY 514
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-196 |
1.66e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.92 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMK--ELNP---TEGTIIVNGQNLNRMKHRNIaK 76
Cdd:PRK14267 5 IETVNLRVYYGSNHV-IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEearVEGEVRLFGRNIYSPDVDPI-E 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQDFRLLKDRNIYENIAFALRVTE--TPTRVIKKKVPAALSLVGLAQKYKS----FPKELSGGEQQRVAIAR 150
Cdd:PRK14267 83 VRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLVIAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLvVTHN 196
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVL-VTHS 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-199 |
2.23e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.23 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLN----RMKHRNIAK 76
Cdd:PRK09536 3 MIDVSDLSVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEalsaRAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFqDFRLlkdRNIYE------NIAFAlRVTETPTRVIKKkvpaALSLVGLAQKYKSFPKELSGGEQQRVAIAR 150
Cdd:PRK09536 82 VPQDTSLSF-EFDV---RQVVEmgrtphRSRFD-TWTETDRAAVER----AMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEI 199
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL 201
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-224 |
5.91e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 102.02 E-value: 5.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRG 80
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL---RNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIAFAlrVTETPTRV-IKKKVPAALSL---VGLAQKYKSFPKE----LSGGEQQRVAIARAI 152
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYA--RTEQYSREqIEEAARMAYAMdfiNKMDNGLDTVIGEngvlLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEAnERGTTVLVVTHNQEIVNEMNErVITMKQGVIVSD-------EKKGGY 224
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADE-ILVVEDGEIVERgthaellAQNGVY 572
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-216 |
7.14e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.58 E-value: 7.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 11 YSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMK---HRNIAKYRRGLGVVFQD 87
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 88 FRLLKDRNIYENIAFALRVTETP-TRVIKKKVPAALSLVGLAQ----KYKSFPKELSGGEQQRVAIARAIVNEPAILLAD 162
Cdd:PRK14246 99 PNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505341235 163 EPTGNLDPTNSWEIMSLLKEANERgTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-216 |
1.34e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.07 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 14 GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELnPTEGTIIVNGQNLNRMkhrNIAKYRRGLGVVFQDFRLLKD 93
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 94 rNIYENIAFAlRVTETPTRVIK--KKVPAALSLVGLAQKYKSFPKE----LSGGEQQRVAIARAIVNEPAILLADEPTGN 167
Cdd:PRK11174 438 -TLRDNVLLG-NPDASDEQLQQalENAWVSEFLPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 168 LDPTNSWEIMSLLKEANeRGTTVLVVTHNQEIVNEMNErVITMKQGVIV 216
Cdd:PRK11174 516 LDAHSEQLVMQALNAAS-RRQTTLMVTHQLEDLAQWDQ-IWVMQDGQIV 562
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-216 |
1.56e-24 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.89 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMkELNPT----EGTIIVNGQNLNRMKHRNIAKYrrglgvVFQDFRLLKD 93
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMRAISAY------VQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 94 RNIYENIAFA--LRVTETPTRVIK----KKVPAALSLVGLAQKYKSFP---KELSGGEQQRVAIARAIVNEPAILLADEP 164
Cdd:TIGR00955 114 LTVREHLMFQahLRMPRRVTKKEKrervDEVLQALGLRKCANTRIGVPgrvKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505341235 165 TGNLDPTNSWEIMSLLKEANERGTTVLVVTH--NQEIVnEMNERVITMKQGVIV 216
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpSSELF-ELFDKIILMAEGRVA 246
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-223 |
1.68e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.06 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIM--KELNPTEGTIIVNGQNLNRMKHRNIAkyRRGLGVVFQ---DFRLLK 92
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILELSPDERA--RAGIFLAFQypvEIPGVS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 93 DRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFP--KELSGGEQQRVAIARAIVNEPAILLADEPTGNLDp 170
Cdd:COG0396 94 VSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGLD- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 171 tnsweIMSL------LKEANERGTTVLVVTHNQEIVNEMN-ERVITMKQGVIVsdeKKGG 223
Cdd:COG0396 173 -----IDALrivaegVNKLRSPDRGILIITHYQRILDYIKpDFVHVLVDGRIV---KSGG 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-195 |
4.17e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.37 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNG--------QNLNRMKHRNIa 75
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpQEPPLDDDLTV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 kyrrgLGVVFQDFRLLKD-----RNIYENIAFALRVTETPTRVIKK-----------KVPAALSLVGLAQKYKSFP-KEL 138
Cdd:COG0488 79 -----LDTVLDGDAELRAleaelEELEAKLAEPDEDLERLAELQEEfealggweaeaRAEEILSGLGFPEEDLDRPvSEL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 139 SGGEQQRVAIARAIVNEPAILLADEPTGNLD-PTNSW-EimSLLKeaNERGtTVLVVTH 195
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDlESIEWlE--EFLK--NYPG-TVLVVSH 207
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
17-216 |
4.51e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 97.50 E-value: 4.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELN-P---TEGTIIVNGQNLNRMKhrniAKYRRGL-----GVVFQD 87
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRIS----EKERRNLvgaevAMIFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 88 frLLKDRNIYENIAF----ALRVTETPTRVIKK-KVPAALSLVGL---AQKYKSFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:PRK11022 98 --PMTSLNPCYTVGFqimeAIKVHQGGNKKTRRqRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLV-VTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVlITHDLALVAEAAHKIIVMYAGQVV 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-219 |
6.51e-24 |
|
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: 94.91 E-value: 6.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA---------------------ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTII 60
Cdd:cd03220 1 IELENVSKSYPTYKGgssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 61 VNGQnlnrmkhrnIAkYRRGLGVVFQdfrllKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSG 140
Cdd:cd03220 81 VRGR---------VS-SLLGLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 141 GEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSDE 219
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-218 |
1.03e-23 |
|
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: 98.66 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRGL 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI---DRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDfRLLKDRNIYENIAFALRvtetpTRVIKKKVPAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIAR 150
Cdd:TIGR01193 551 NYLPQE-PYIFSGSILENLLLGAK-----ENVSQDEIWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIALAR 624
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERgtTVLVVTHNQEIVnEMNERVITMKQGVIVSD 218
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQ 689
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
1.44e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA---------------------ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTI 59
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 60 IVNGqnlnrmkhrniakyrR-----GLGVVFQ-DF--RllkdrniyENIAFALRVTETPTRVIKKKVPAALSLVGLA--- 128
Cdd:COG1134 84 EVNG---------------RvsallELGAGFHpELtgR--------ENIYLNGRLLGLSRKEIDEKFDEIVEFAELGdfi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 129 -QKYKSFpkelSGGEQQRVAIARAIVNEPAILLADeptgnldptnswEIMS------------LLKEANERGTTVLVVTH 195
Cdd:COG1134 141 dQPVKTY----SSGMRARLAFAVATAVDPDILLVD------------EVLAvgdaafqkkclaRIRELRESGRTVIFVSH 204
|
250 260
....*....|....*....|....
gi 505341235 196 NQEIVNEMNERVITMKQGVIVSDE 219
Cdd:COG1134 205 SMGAVRRLCDRAIWLEKGRLVMDG 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
17-213 |
1.67e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 94.67 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkyRRGLGVVFQDFRLLKDRNI 96
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RMGVVRTFQHVRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 97 YENIAFA------------LRVTETPTRVIKKKVPAA---LSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:PRK11300 98 IENLLVAqhqqlktglfsgLLKTPAFRRAESEALDRAatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAElRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-216 |
2.16e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.22 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 5 RNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTII--VNGQNLNRMKHRNIAKYRRGL- 81
Cdd:PRK11701 10 RGLTKLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrMRDGQLRDLYALSEAERRRLLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 ---GVVFQDF----------------RLLK--DRNiYENI-AFAL----RVTETPTRVikkkvpaalslvglaqkyKSFP 135
Cdd:PRK11701 89 tewGFVHQHPrdglrmqvsaggnigeRLMAvgARH-YGDIrATAGdwleRVEIDAARI------------------DDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 136 KELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGV 214
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
..
gi 505341235 215 IV 216
Cdd:PRK11701 230 VV 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-216 |
2.79e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 93.79 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkyRRG 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQA-LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--REA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIA----FALRvTETPTRVikkkvpaalslvglAQKYKSFPK----------ELSGGEQQRV 146
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAmggfFAER-DQFQERI--------------KWVYELFPRlherriqragTMSGGEQQML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 147 AIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-216 |
2.81e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 94.00 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKghAALNGVSVKIERGEFVFIVGDSGSGKS----TLIKLIMKELNPTEGTIIVNGQNL--NRMKHRNIA 75
Cdd:PRK10418 5 IELRNIALQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVapCALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 kyrrglgVVFQDFRLLKD--RNIYENIAFALRVTETPTRVikKKVPAALSLVGLAQK---YKSFPKELSGGEQQRVAIAR 150
Cdd:PRK10418 83 -------TIMQNPRSAFNplHTMHTHARETCLALGKPADD--ATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK10418 154 ALLCEAPFIIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIV 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-213 |
4.13e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 90.59 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIivngqnlnrmkhrniakyrrgl 81
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 gvvfqdfrllkdrniyeniafalrvtetptrvikkKVPAALSLVGLAQkyksfpkeLSGGEQQRVAIARAIVNEPAILLA 161
Cdd:cd03221 58 -----------------------------------TWGSTVKIGYFEQ--------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505341235 162 DEPTGNLDPTNsweIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:cd03221 95 DEPTNHLDLES---IEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-216 |
4.38e-23 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.85 E-value: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYskgHAALNgVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGLGV 83
Cdd:PRK10261 330 LNRVTREV---HAVEK-VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 84 VFQD-FRLLKDR-NIYENIAFALRVTET-PTRVIKKKVPAALSLVGLAQKYK-SFPKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:PRK10261 406 IFQDpYASLDPRqTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVI 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDlQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-213 |
6.42e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 94.41 E-value: 6.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNP---TEGTIIVNGQN--------LNRMKHRNIAkyrrglgVVF 85
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREilnlpekeLNKLRAEQIS-------MIF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 86 QDfrLLKDRNIYeniafaLRVTETPTRVI-------KK-------------KVPAALslvglaQKYKSFPKELSGGEQQR 145
Cdd:PRK09473 104 QD--PMTSLNPY------MRVGEQLMEVLmlhkgmsKAeafeesvrmldavKMPEAR------KRMKMYPHEFSGGMRQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-209 |
6.79e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 92.33 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKEL--NPTEGTIIVNGQNLNRmkhrniakyrrglgvvfqdfrllkDRN 95
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR------------------------EAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 96 IYENIAfalRVTETPTRVikkkvpAALSLVGL--AQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNS 173
Cdd:COG2401 102 LIDAIG---RKGDFKDAV------ELLNAVGLsdAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 505341235 174 WEI-MSLLKEANERGTTVLVVTHNQEIVNEMN-ERVIT 209
Cdd:COG2401 173 KRVaRNLQKLARRAGITLVVATHHYDVIDDLQpDLLIF 210
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-216 |
7.30e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 93.32 E-value: 7.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYS-------KGH-AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHR 72
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwfrRQTvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 73 niakYR-RGLGVVFQD--FRLLKDRNIYENIAFALRV-TETPTRVIKKKVPAALSLVGLAQKYKSF-PKELSGGEQQRVA 147
Cdd:PRK15112 84 ----YRsQRIRMIFQDpsTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-218 |
7.34e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.13 E-value: 7.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 6 NVTKEYSKGHAALNgVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkyrRGLGVVF 85
Cdd:PRK10253 12 QLTLGYGKYTVAEN-LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 86 QDFRLLKDRNIYENIAFAlRVTETP--TRVIKKK---VPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:PRK10253 88 QNATTPGDITVQELVARG-RYPHQPlfTRWRKEDeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEAN-ERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNrEKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-213 |
1.50e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLImKEL-NPTEGTIIVNgqnlnrmkhrniakyrR 79
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAI-AGLwPYGSGRIARP----------------A 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVF--QDFRL----LKDrniyeniafALRVTETPTRVIKKKVPAALSLVGLAQ------KYKSFPKELSGGEQQRVA 147
Cdd:COG4178 425 GARVLFlpQRPYLplgtLRE---------ALLYPATAEAFSDAELREALEAVGLGHlaerldEEADWDQVLSLGEQQRLA 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANErGTTVLVVTHnQEIVNEMNERVITMKQG 213
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP-GTTVISVGH-RSTLAAFHDRVLELTGD 559
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-213 |
1.68e-22 |
|
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: 90.61 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVT----KEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGqnlnrmkhrniaky 77
Cdd:cd03250 1 ISVEDASftwdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 rrGLGVVFQdFRLLKDRNIYENIAFALRVTEtptrvikKKVPAALSLVGLAQKYKSFPK-------E----LSGGEQQRV 146
Cdd:cd03250 67 --SIAYVSQ-EPWIQNGTIRENILFGKPFDE-------ERYEKVIKACALEPDLEILPDgdlteigEkginLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 147 AIARAIVNEPAILLADEPTGNLDP-TNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNeRVITMKQG 213
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAhVGRHIFENCILGLLLNNKTRILVTHQLQLLPHAD-QIVVLDNG 203
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-217 |
1.90e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 91.49 E-value: 1.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 6 NVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniAKYRRGLGVVF 85
Cdd:PRK10895 8 NLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH--ARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 86 QDFRLLKDRNIYENIAFALRVTETPTRVIKK-KVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEP 164
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIRDDLSAEQREdRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 165 TGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-216 |
3.16e-22 |
|
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: 91.43 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGhAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQN--------LNRMKHR 72
Cdd:TIGR02323 3 LLQVSGLSKSYGGG-KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelyqLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 73 NIAkyRRGLGVVFQDFR--LLKDRNIYENIAfaLRVTETPTR---VIKKKVPAALSLVGLAQ-KYKSFPKELSGGEQQRV 146
Cdd:TIGR02323 82 RLM--RTEWGFVHQNPRdgLRMRVSAGANIG--ERLMAIGARhygNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 147 AIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGlVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-217 |
4.31e-21 |
|
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: 87.08 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmKHRNIAKYRRG 80
Cdd:cd03369 7 IEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLL--------------KDRNIYEniafALRVTETptrvikkkvpaalslvGLaqkyksfpkELSGGEQQRV 146
Cdd:cd03369 84 LTIIPQDPTLFsgtirsnldpfdeySDEEIYG----ALRVSEG----------------GL---------NLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505341235 147 AIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANErGTTVLVVTHNQEIVNEMnERVITMKQGVIVS 217
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKE 203
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-221 |
6.74e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 90.71 E-value: 6.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKEL--NPTEGTIIVNGQNLNRMKHRNIakyrrglGVVFQDFRLLKDRN 95
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPTKQILKRT-------GFVTQDDILYPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 96 IYENIAFA--LRVTETPTRVIKKKVP-AALSLVGLAQKYK-----SFPKELSGGEQQRVAIARAIVNEPAILLADEPTGN 167
Cdd:PLN03211 157 VRETLVFCslLRLPKSLTKQEKILVAeSVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505341235 168 LDPTNSWEIMSLLKEANERGTTVLVVTHnqeivnEMNERVITMKQGVIVSDEKK 221
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMH------QPSSRVYQMFDSVLVLSEGR 284
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-216 |
7.49e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYrrG 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHA-LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL--G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENiafaLRVTETPTRVI-----------KKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIA 149
Cdd:PRK09700 82 IGIIYQELSVIDELTVLEN----LYIGRHLTKKVcgvniidwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-216 |
2.19e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.14 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 16 AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNI-------AKYRR----GLGVV 84
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIelseqsaAQMRHvrgaDMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 85 FQD--FRLLKDRNIYENIAFALRV-----TETPTRVIKK-----KVPAALSLVGlaqkykSFPKELSGGEQQRVAIARAI 152
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLhqgasREEAMVEAKRmldqvRIPEAQTILS------RYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIV 216
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVlQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-220 |
2.49e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.57 E-value: 2.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYrrG 80
Cdd:PRK15439 11 LLCARSISKQYS-GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL--G 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALrvteTPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEK 220
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-195 |
3.74e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.33 E-value: 3.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTkeYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMK---HRNIA-- 75
Cdd:TIGR01189 1 LAARNLA--CSRGeRMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRdepHENILyl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 76 KYRRGLGvvfqdfrllKDRNIYENIAFALRVTETPTRVIKkkvpAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:TIGR01189 79 GHLPGLK---------PELSALENLHFWAAIHGGAQRTIE----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505341235 156 PAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH 195
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-197 |
4.59e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.45 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYrrg 80
Cdd:PRK11231 2 TLRTENLTVGYGT-KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFAL--------RVTETPTRVIKKKVpAALSLVGLAQKYKSfpkELSGGEQQRVAIARAI 152
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAYGRspwlslwgRLSAEDNARVNQAM-EQTRINHLADRRLT---DLSGGQRQRAFLAMVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH--NQ 197
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlNQ 200
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-215 |
5.06e-20 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 87.72 E-value: 5.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhRNIAKYRRGL 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDF----RLLKDRNiyeniafalrvtetpTRVIKKKVPAALSLVGLAQKYK------SFPKeLSGGEQQRVAIARA 151
Cdd:PRK10522 400 SAVFTDFhlfdQLLGPEG---------------KPANPALVEKWLERLKMAHKLEledgriSNLK-LSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 152 IVNEPAILLADEPTGNLDPTNSWEI-MSLLKEANERGTTVLVVTHNQEIVnEMNERVITMKQGVI 215
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHDDHYF-IHADRLLEMRNGQL 527
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-216 |
5.64e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTkeyskGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQnlnRMKHRNIAK-YRRGL 81
Cdd:COG1129 258 EVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK---PVRIRSPRDaIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDfR----LLKDRNIYENIAFAL-------------RVTETPTRVIKK---KVPAALSLVGlaqkyksfpkELSGG 141
Cdd:COG1129 330 AYVPED-RkgegLVLDLSIRENITLASldrlsrgglldrrRERALAEEYIKRlriKTPSPEQPVG----------NLSGG 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 142 EQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVThnqeivNEMNE------RVITMKQGVI 215
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVIS------SELPEllglsdRILVMREGRI 472
|
.
gi 505341235 216 V 216
Cdd:COG1129 473 V 473
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-223 |
7.56e-20 |
|
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: 83.73 E-value: 7.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIM--KELNPTEGTIIVNGQNLNRMKHRNIAkyRRGLGVVFQDfrllkdrn 95
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEERA--RLGIFLAFQY-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 96 iyeniafalrvtetptrvikkkvPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWE 175
Cdd:cd03217 86 -----------------------PPEIPGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 176 IMSLLKEANERGTTVLVVTHNQEIVNEMN-ERVITMKQGVIVsdeKKGG 223
Cdd:cd03217 143 VAEVINKLREEGKSVLIITHYQRLLDYIKpDRVHVLYDGRIV---KSGD 188
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-220 |
1.23e-19 |
|
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: 86.78 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA----ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRmkhRNIAKY 77
Cdd:COG4615 328 LELRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQDFRLLkDRNIyeniafALRVTETPTRV--------IKKKVP---AALSLVglaqkyksfpkELSGGEQQRV 146
Cdd:COG4615 405 RQLFSAVFSDFHLF-DRLL------GLDGEADPARArellerleLDHKVSvedGRFSTT-----------DLSQGQRKRL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 147 AIARAIVNEPAILLADEptgnldptnsW--------------EIMSLLKeanERGTTVLVVTHnqeivnemNE------- 205
Cdd:COG4615 467 ALLVALLEDRPILVFDE----------WaadqdpefrrvfytELLPELK---ARGKTVIAISH--------DDryfdlad 525
|
250
....*....|....*
gi 505341235 206 RVITMKQGVIVSDEK 220
Cdd:COG4615 526 RVLKMDYGKLVELTG 540
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-196 |
2.04e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 2.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 20 GVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYrrgLGvvFQDFrlLKDR-NIYE 98
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY---LG--HRNA--MKPAlTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 99 NIAFALRVTETPTRVIkkkvPAALSLVGLAQ----KYksfpKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSW 174
Cdd:PRK13539 93 NLEFWAAFLGGEELDI----AAALEAVGLAPlahlPF----GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 505341235 175 EIMSLLKEANERGTTVLVVTHN 196
Cdd:PRK13539 165 LFAELIRAHLAQGGIVIAATHI 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-198 |
2.19e-19 |
|
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: 84.14 E-value: 2.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSK-GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNpTEGTIIVNGQNLNRMkhrNIAKYRRG 80
Cdd:cd03289 3 MTVKDLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSV---PLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQD-------FRLLKDRNIYENIAFALRVT-ETPTRVIKKKVPAALSLVGLAQKYKsfpkeLSGGEQQRVAIARAI 152
Cdd:cd03289 79 FGVIPQKvfifsgtFRKNLDPYGKWSDEEIWKVAeEVGLKSVIEQFPGQLDFVLVDGGCV-----LSHGHKQLMCLARSV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANErGTTVLVVTHNQE 198
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIE 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-218 |
2.36e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.99 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 14 GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEG-----TIIVNGQNLnrMKHRNIAKYRRGLGVVFQDF 88
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 89 RLLKdRNIYENIAFALRVTE-TPTRVIKKKVPAALSLVGL----AQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADE 163
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 164 PTGNLDPTNSWEIMSLLKEANERgTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEE 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-213 |
2.92e-19 |
|
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: 86.22 E-value: 2.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYSK-GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmkHRNIAKYRRGLG 82
Cdd:TIGR01257 931 VKNLVKIFEPsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 VVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLAD 162
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505341235 163 EPTGNLDPTNSWEIMSLLKEANErGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQG 1136
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-217 |
3.23e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.97 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIkLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGLGvvfQDFRLLKDRNIY 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLL-ARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLS---QQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 ENIAFALRVTETPTRVIKkkVPAAL-SLVGLAQKYKSFPKELSGGEQQRVAIARAI------VN-EPAILLADEPTGNLD 169
Cdd:COG4138 88 QYLALHQPAGASSEAVEQ--LLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptINpEGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505341235 170 PTNSWEIMSLLKEANERGTTVLVVTHNqeivneMN------ERVITMKQGVIVS 217
Cdd:COG4138 166 VAQQAALDRLLRELCQQGITVVMSSHD------LNhtlrhaDRVWLLKQGKLVA 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-216 |
3.28e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 3.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakYRRGLG 82
Cdd:COG3845 259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER--RRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 VVFQDfR----LLKDRNIYENIAFAL---------------RVTETPTRVIKK---KVPAALSLVGLaqkyksfpkeLSG 140
Cdd:COG3845 337 YIPED-RlgrgLVPDMSVAENLILGRyrrppfsrggfldrkAIRAFAEELIEEfdvRTPGPDTPARS----------LSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 141 GEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHN-QEIVnEMNERVITMKQGVIV 216
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDlDEIL-ALSDRIAVMYEGRIV 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-212 |
6.06e-19 |
|
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: 81.39 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 14 GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMK---HRNIAKYRRGLGVvfqdfrl 90
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiARGLLYLGHAPGI------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 91 lKDR-NIYENIAFALRVTETPTrvikkkVPAALSLVGLAqKYKSFP-KELSGGEQQRVAIARAIVNEPAILLADEPTGNL 168
Cdd:cd03231 85 -KTTlSVLENLRFWHADHSDEQ------VEEALARVGLN-GFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505341235 169 DPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQ 212
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGF 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-216 |
1.08e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.99 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 15 HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKhrnIAKYRRGLGVVFQDFRLLKDr 94
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 95 NIYENIAFAlRVTETPTRVikkKVPAALSLVG-----LAQKYKSFPKE----LSGGEQQRVAIARAIVNEPAILLADEPT 165
Cdd:PRK10789 404 TVANNIALG-RPDATQQEI---EHVARLASVHddilrLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505341235 166 GNLDPTNSWEIMSLLKEANErGTTVLVVTHNQEIVNEMNErVITMKQGVIV 216
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGE-GRTVIISAHRLSALTEASE-ILVMQHGHIA 528
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-216 |
1.11e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.93 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA---ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKelnptegtiiVNGQNL----NRMKHRN 73
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGwvkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG----------VTKDNWrvtaDRMRFDD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 74 I------AKYRRGL-----GVVFQDFRLLKD------RNIYENIA-------FALRVTETPTRVIKkkvpaALSLVGLAQ 129
Cdd:PRK15093 73 IdllrlsPRERRKLvghnvSMIFQEPQSCLDpservgRQLMQNIPgwtykgrWWQRFGWRKRRAIE-----LLHRVGIKD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 130 KY---KSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANER-GTTVLVVTHNQEIVNEMNE 205
Cdd:PRK15093 148 HKdamRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHDLQMLSQWAD 227
|
250
....*....|.
gi 505341235 206 RVITMKQGVIV 216
Cdd:PRK15093 228 KINVLYCGQTV 238
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-213 |
1.13e-18 |
|
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: 84.11 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKlIMKELNPT---EGTIIVNGQNLnrmKHRNIAKY 77
Cdd:TIGR02633 1 LLEMKGIVKTFG-GVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPL---KASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 -RRGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRV----IKKKVPAALSLVGLAQKYKSFP-KELSGGEQQRVAIARA 151
Cdd:TIGR02633 76 eRAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMaynaMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 152 IVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-217 |
1.73e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 81.37 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAkyrRGLGV 83
Cdd:PRK10575 14 LRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA---RKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 84 VFQDFRLLKDRNIYENIAF-------ALRVTETPTRvikKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEP 156
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIgrypwhgALGRFGAADR---EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 157 AILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRlSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-195 |
1.40e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.54 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEysKGHAAL-NGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRniakYRR 79
Cdd:PRK13538 1 MLEARNLACE--RDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GL-------GVvfqdfrllKDR-NIYENIAFALRVTETPTRvikKKVPAALSLVGLAqKYKSFP-KELSGGEQQRVAIAR 150
Cdd:PRK13538 75 DLlylghqpGI--------KTElTALENLRFYQRLHGPGDD---EALWEALAQVGLA-GFEDVPvRQLSAGQQRRVALAR 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505341235 151 AIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH 195
Cdd:PRK13538 143 LWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-195 |
2.73e-17 |
|
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: 76.04 E-value: 2.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKlIMKELNP-TEGTIIvngqnlnrmKHRNiakyrrg 80
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLWPwGSGRIG---------MPEG------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 lgvvfqdfrllkdrniyENIAFalrvtetptrvikkkvpaalslvgLAQK-YksFP-------------KELSGGEQQRV 146
Cdd:cd03223 64 -----------------EDLLF------------------------LPQRpY--LPlgtlreqliypwdDVLSGGEQQRL 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 147 AIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKeanERGTTVLVVTH 195
Cdd:cd03223 101 AFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK---ELGITVISVGH 146
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-195 |
6.83e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 6.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKlIMKELNPT---EGTIIVNGQNLnrmKHRNIAKY 77
Cdd:PRK13549 5 LLEMKNITKTFG-GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFEGEEL---QASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 -RRGLGVVFQDFRLLKDRNIYENIaFaLRVTETPTRVIK--------KKVPAALSL-VGLAQKYksfpKELSGGEQQRVA 147
Cdd:PRK13549 80 eRAGIAIIHQELALVKELSVLENI-F-LGNEITPGGIMDydamylraQKLLAQLKLdINPATPV----GNLGLGQQQLVE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH 195
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-217 |
8.55e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.51 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 21 VSVKIERGEFVFIVGDSGSGKSTLIKLiMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGLGvvfQDfrllkdrniyENI 100
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLAR-MAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLS---QQ----------QTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 101 AFALRV---------TETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVN-EPAI------LLADEP 164
Cdd:PRK03695 81 PFAMPVfqyltlhqpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 165 TGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-213 |
1.01e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQnlnRMKHRNI-AKYRRGL 81
Cdd:PRK11288 6 SFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ---EMRFASTtAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFRLLKDRNIYENIAFAlrvtETPTR--VIKKK-----VPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVN 154
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLG----QLPHKggIVNRRllnyeAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 155 EPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK11288 158 NARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-218 |
1.02e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 17 ALNGVSVKIERGE-FVFIvGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkHRNIAKyRRGLGVVFQDFRLLKDRN 95
Cdd:NF033858 281 AVDHVSFRIRRGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD---AGDIAT-RRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 96 IYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPT---N 172
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVardM 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505341235 173 SWEIMSLLkeANERGTTVLVVTHNqeivneMNE-----RVITMKQG-VIVSD 218
Cdd:NF033858 436 FWRLLIEL--SREDGVTIFISTHF------MNEaercdRISLMHAGrVLASD 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-192 |
1.65e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.15 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYS--KGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNgqNLNRMKHRNIAKYRR 79
Cdd:PTZ00265 383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDfRLLKDRNIYENIAFAL------------------------------------------------------- 104
Cdd:PTZ00265 461 KIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 105 ---RVTETPTRVIKKKVPAALSLVGLAQKYKSF----PKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIM 177
Cdd:PTZ00265 540 nyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250
....*....|....*..
gi 505341235 178 SLLK--EANERGTTVLV 192
Cdd:PTZ00265 620 KTINnlKGNENRITIII 636
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-217 |
4.08e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 4.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQnlnrmkhrniakyrRG 80
Cdd:PRK09544 4 LVSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--------------LR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLlkDRNIYENIAFALRVTETptrVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILL 160
Cdd:PRK09544 69 IGYVPQKLYL--DTTLPLTVNRFLRLRPG---TKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 161 ADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK09544 144 LDEPTQGVDVNGQVALYDLIDQlRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCS 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-191 |
4.43e-16 |
|
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: 76.87 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSK-GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNpTEGTIIVNGQNLNRMkhrNIAKYRRG 80
Cdd:TIGR01271 1218 MDVQGLTAKYTEaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSV---TLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLL-----KDRNIYENIAFA--LRVTETptrvikkkvpaalslVGLAQKYKSFPKE-----------LSGGE 142
Cdd:TIGR01271 1294 FGVIPQKVFIFsgtfrKNLDPYEQWSDEeiWKVAEE---------------VGLKSVIEQFPDKldfvlvdggyvLSNGH 1358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 143 QQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVL 191
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVIL 1407
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-215 |
3.15e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.43 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGqnlnrmkhRNIAKY--- 77
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG--------REIGAYglr 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 --RRGLGVVFQDfRLLKDRNIYENIAFALRVTETptrvikkKVPAALSLVGLAQKYKSFPKEL-----------SGGEQQ 144
Cdd:PTZ00243 1381 elRRQFSMIPQD-PVLFDGTVRQNVDPFLEASSA-------EVWAALELVGLRERVASESEGIdsrvleggsnySVGQRQ 1452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 145 RVAIARAIVNE-PAILLADEPTGNLDPTNSWEIMSLLKEANErGTTVLVVTHNQEIVNEMnERVITMKQGVI 215
Cdd:PTZ00243 1453 LMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFS-AYTVITIAHRLHTVAQY-DKIIVMDHGAV 1522
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-176 |
3.49e-15 |
|
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: 74.18 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIivngqnlnrmKHRNIAKYRrglgvvfQDFRLLKDRNIY 97
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------KHSGRISFS-------PQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 ENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKE----LSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNS 173
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
...
gi 505341235 174 WEI 176
Cdd:TIGR01271 585 KEI 587
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-217 |
7.21e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.06 E-value: 7.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 25 IERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNgQNL--NRMKH---RNIAkyrrglGVVFqDF---------RL 90
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLivARLQQdppRNVE------GTVY-DFvaegieeqaEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 91 LKDrniYENIAfaLRVTETPT-RVIKK------------------KVPAALSLVGL-AQKYKSfpkELSGGEQQRVAIAR 150
Cdd:PRK11147 98 LKR---YHDIS--HLVETDPSeKNLNElaklqeqldhhnlwqlenRINEVLAQLGLdPDAALS---SLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 151 AIVNEPAILLADEPTGNLD-PTNSWeIMSLLKeaNERGTTVLvVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDiETIEW-LEGFLK--TFQGSIIF-ISHDRSFIRNMATRIVDLDRGKLVS 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-195 |
8.67e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 70.26 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 11 YSKGHAALNG-VSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGLGVVFQDFR 89
Cdd:PRK13543 19 FSRNEEPVFGpLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 90 LLkdrniyENIAF-----ALRVTETPTrvikkkvpAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEP 164
Cdd:PRK13543 99 TL------ENLHFlcglhGRRAKQMPG--------SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 505341235 165 TGNLDPTNSWEIMSLLKEANERGTTVLVVTH 195
Cdd:PRK13543 165 YANLDLEGITLVNRMISAHLRGGGAALVTTH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-228 |
1.02e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.34 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQ--NLNRMKHRNIAkyr 78
Cdd:PRK10762 4 LLQLKGIDKAFP-GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKevTFNGPKSSQEA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 rGLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAA----LSLVGLAQKYKSFPKELSGGEQQRVAIARAIVN 154
Cdd:PRK10762 80 -GIGIIHQELNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEadklLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 155 EPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHN-QEIVnEMNERVITMKQGVIVsDEKKGGYINED 228
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRlKEIF-EICDDVTVFRDGQFI-AEREVADLTED 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-228 |
1.77e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLikliMKELN---PT---EGTIIVNGQnlnRMKHRNI 74
Cdd:NF040905 1 ILEMRGITKTFP-GVKALDDVNLSVREGEIHALCGENGAGKSTL----MKVLSgvyPHgsyEGEILFDGE---VCRFKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 75 -AKYRRGLGVVFQDFRLLKDRNIYENIAFAlrvTETPTR-VI-----KKKVPAALSLVGLAQKYKSFPKELSGGEQQRVA 147
Cdd:NF040905 73 rDSEALGIVIIHQELALIPYLSIAENIFLG---NERAKRgVIdwnetNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 148 IARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG-VIVSDEKKGGYIN 226
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGrTIETLDCRADEVT 229
|
..
gi 505341235 227 ED 228
Cdd:NF040905 230 ED 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-208 |
2.27e-14 |
|
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: 69.74 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 11 YSKGHAALNGVSVKIERGEF-----VFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRrglGVVf 85
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYE---GTV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 86 QDFRLLKDRNIYENIAFAlrvtetpTRVIKKkvpaalslVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPT 165
Cdd:cd03237 79 RDLLSSITKDFYTHPYFK-------TEIAKP--------LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505341235 166 GNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVI 208
Cdd:cd03237 144 AYLDVEQRLMASKVIRRfAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-176 |
3.99e-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: 69.50 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 14 GHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIivngqnlnrmKHRNIAKYRrglgvvfQDFRLLKD 93
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------KHSGRISFS-------SQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 94 RNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKE----LSGGEQQRVAIARAIVNEPAILLADEPTGNLD 169
Cdd:cd03291 112 GTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
....*..
gi 505341235 170 PTNSWEI 176
Cdd:cd03291 192 VFTEKEI 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-213 |
4.59e-14 |
|
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: 68.51 E-value: 4.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 11 YSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGLGVVFQDFRL 90
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 91 LKDRNIYENIAFalrvtETPTRviKKKVPAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIARAIVNEPAIL 159
Cdd:cd03290 90 LLNATVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 160 LADEPTGNLDPTNSWEIMS--LLKEANERGTTVLVVTHNQEIVNEMnERVITMKQG 213
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHA-DWIIAMKDG 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-202 |
5.12e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.05 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYsKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhRNIAKYRRG 80
Cdd:PRK13540 1 MLDVIELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKkkvpaaLSLVGLAQKYKSFP-KELSGGEQQRVAIARAIVNEPAIL 159
Cdd:PRK13540 76 LCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITE------LCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNE 202
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNK 192
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
18-213 |
1.47e-13 |
|
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: 66.50 E-value: 1.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIM--KELNPTEGTIIVNGQNLNrmkhrniAKYRRGLGVVFQDFRLLKDRN 95
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLD-------KNFQRSTGYVEQQDVHSPNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 96 IYENIAFAlrvtetptrvikkkvpAALslvglaqkyksfpKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWE 175
Cdd:cd03232 96 VREALRFS----------------ALL-------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505341235 176 IMSLLKEANERGTTVLVVTH--NQEIVnEMNERVITMKQG 213
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHqpSASIF-EKFDRLLLLKRG 185
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-195 |
2.79e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.42 E-value: 2.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYskGHAAL-NGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVnGQNLNrmkhrniakyrrg 80
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK------------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQdFR--LLKDRNIYENIAFALRVtetpTRVIKKKVPA-----ALSLVGLAQKYKSfpKELSGGEQQRVAIARAIV 153
Cdd:TIGR03719 387 LAYVDQ-SRdaLDPNKTVWEEISGGLDI----IKLGKREIPSrayvgRFNFKGSDQQKKV--GQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505341235 154 NEPAILLADEPTGNLDPtnswEIMSLLKEANER-GTTVLVVTH 195
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDV----ETLRALEEALLNfAGCAVVISH 498
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-215 |
2.83e-13 |
|
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: 68.43 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKG-HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRG 80
Cdd:TIGR00957 1285 VEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrniyeniafALRVTETP-TRVIKKKVPAALSLVGLAQKYKSFP-----------KELSGGEQQRVAI 148
Cdd:TIGR00957 1362 ITIIPQDPVLFSG---------SLRMNLDPfSQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCL 1432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 149 ARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANErGTTVLVVTHNQEIVNEMNeRVITMKQGVI 215
Cdd:TIGR00957 1433 ARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE-DCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-213 |
3.44e-13 |
|
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: 68.50 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTKEYSKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLnrmkHRNIAKYRR 79
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----LTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQdF----RLLKDRniyENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNE 155
Cdd:TIGR01257 2013 NMGYCPQ-FdaidDLLTGR---EHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 156 PAILLADEPTGNLDPTNS---WE-IMSLLKEanerGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARrmlWNtIVSIIRE----GRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-215 |
4.10e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRN--------IAKYRRGLGVVFqdfr 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRDGLVL---- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 90 llkDRNIYENIAF-ALRVTETPTRVIKK----------------KVPAALSLVGLaqkyksfpkeLSGGEQQRVAIARAI 152
Cdd:PRK10762 344 ---GMSVKENMSLtALRYFSRAGGSLKHadeqqavsdfirlfniKTPSMEQAIGL----------LSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVI 215
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-216 |
9.60e-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: 64.59 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYSKG---HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPT---EGTIIVNGQNLNRMKHrniaKY 77
Cdd:cd03233 6 WRNISFTTGKGrskIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE----KY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 78 RRGLGVVFQDfrllkDRNIYEniafaLRVTETptrvikkkVPAALSLVGLAqkyksFPKELSGGEQQRVAIARAIVNEPA 157
Cdd:cd03233 82 PGEIIYVSEE-----DVHFPT-----LTVRET--------LDFALRCKGNE-----FVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTH--NQEIVNeMNERVITMKQGVIV 216
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTmADVLKTTTFVSLYqaSDEIYD-LFDKVLVLYEGRQI 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-228 |
9.88e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.61 E-value: 9.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 21 VSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNiakyRRGLGVVF-----QDFRLLKDRN 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 96 IYENIAfALRVTETPTRVIKKKVPAALS---------LVGLAQKYKSfpkeLSGGEQQRVAIARAIVNEPAILLADEPTG 166
Cdd:PRK15439 358 LAWNVC-ALTHNRRGFWIKPARENAVLEryrralnikFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 167 NLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIvSDEKKGGYINED 228
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI-SGALTGAAINVD 493
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
33-195 |
2.54e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 33 IVGDSGSGKSTLIKLIMKELNPTEGTIIV---------------NGQNLNRMKHRNIAKYRRGL---------------- 81
Cdd:PTZ00265 1199 IVGETGSGKSTVMSLLMRFYDLKNDHHIVfknehtndmtneqdyQGDEEQNVGMKNVNEFSLTKeggsgedstvfknsgk 1278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 ----GVVFQDFRLLKDRN---------------IYENIAFAlrvTETPTRVIKKKVP--AALS--LVGLAQKYKS----F 134
Cdd:PTZ00265 1279 illdGVDICDYNLKDLRNlfsivsqepmlfnmsIYENIKFG---KEDATREDVKRACkfAAIDefIESLPNKYDTnvgpY 1355
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 135 PKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDpTNSWEIM--SLLKEANERGTTVLVVTH 195
Cdd:PTZ00265 1356 GKSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIekTIVDIKDKADKTIITIAH 1417
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-226 |
4.78e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKEL-NPTEGTIIVNGQNLNRmkhRNIAK-YRRGLGVVFQDFR---LLK 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFINGKPVDI---RNPAQaIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 93 DRNIYENIAFA-LRVTETPTRVIKKK----VPAALSLVGLAQKYKSFP-KELSGGEQQRVAIARAIVNEPAILLADEPTG 166
Cdd:TIGR02633 353 ILGVGKNITLSvLKSFCFKMRIDAAAelqiIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 167 NLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGvivsdEKKGGYIN 226
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG-----KLKGDFVN 487
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-216 |
4.94e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 4.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYSKghAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELN----PTEGTIIVNGQNLNRMKhrniaKYR 78
Cdd:TIGR00956 64 KLKKFRDTKTF--DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVITYDGITPEEIK-----KHY 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 RGlGVVFQ-----DFRLLkdrNIYENIAFALRVTETPTRV--------IKKKVPAALSLVGLAQKYKS-----FPKELSG 140
Cdd:TIGR00956 137 RG-DVVYNaetdvHFPHL---TVGETLDFAARCKTPQNRPdgvsreeyAKHIADVYMATYGLSHTRNTkvgndFVRGVSG 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 141 GEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTH--NQEIVnEMNERVITMKQGVIV 216
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTsANILDTTPLVAIYqcSQDAY-ELFDKVIVLYEGYQI 290
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-198 |
7.61e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.88 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKElNPT--EGTIIVNGQnlnrmkhrniakyRR 79
Cdd:PRK10938 261 IVLNNGVVSYND-RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HPQgySNDLTLFGR-------------RR 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDFRllkdRNI-YENIAFAL--RVTETPTRVI------------------KKKVPAALSLVGLAQKYKSFP-KE 137
Cdd:PRK10938 326 GSGETIWDIK----KHIgYVSSSLHLdyRVSTSVRNVIlsgffdsigiyqavsdrqQKLAQQWLDILGIDKRTADAPfHS 401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 138 LSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTN-----SWeIMSLLKEANergTTVLVVTHNQE 198
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNrqlvrRF-VDVLISEGE---TQLLFVSHHAE 463
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-224 |
2.11e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVnGQNLNrmkhrnIAkYrrglg 82
Cdd:PRK11147 321 EMENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLE------VA-Y----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 vvFQDFR--LLKDRNIYENIAfalrvtETPTRVIKKKVPAalSLVGLAQKYKSFPKE-------LSGGEQQRVAIARAIV 153
Cdd:PRK11147 387 --FDQHRaeLDPEKTVMDNLA------EGKQEVMVNGRPR--HVLGYLQDFLFHPKRamtpvkaLSGGERNRLLLARLFL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 154 NEPAILLADEPTGNLDPtnswEIMSLLKE--ANERGtTVLVVTHNQEIV-NEMNERVITMKQGVIvsDEKKGGY 224
Cdd:PRK11147 457 KPSNLLILDEPTNDLDV----ETLELLEEllDSYQG-TVLLVSHDRQFVdNTVTECWIFEGNGKI--GRYVGGY 523
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-215 |
3.67e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGhAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIivngqnlnrmKHRNIAKyrrgL 81
Cdd:PRK15064 320 LEVENLTKGFDNG-PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENAN----I 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQD----FRllKDRNIYENIAFALRVTETPTRV-------------IKKKVpaalslvglaqkyksfpKELSGGEQQ 144
Cdd:PRK15064 385 GYYAQDhaydFE--NDLTLFDWMSQWRQEGDDEQAVrgtlgrllfsqddIKKSV-----------------KVLSGGEKG 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505341235 145 RVAIARAIVNEPAILLADEPTGNLDpTNSWEIMSLLKEaNERGtTVLVVTHNQEIVNEMNERVITMK-QGVI 215
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMD-MESIESLNMALE-KYEG-TLIFVSHDREFVSSLATRIIEITpDGVV 514
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-218 |
3.67e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 3.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 13 KGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQnlnRMKHRN-IAKYRRGLGVVFQDFR-- 89
Cdd:PRK11288 264 KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK---PIDIRSpRDAIRAGIMLCPEDRKae 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 90 -LLKDRNIYENIAFALR--------------VTETPTRVIKK---KVPAALSLVGLaqkyksfpkeLSGGEQQRVAIARA 151
Cdd:PRK11288 341 gIIPVHSVADNINISARrhhlragclinnrwEAENADRFIRSlniKTPSREQLIMN----------LSGGNQQKAILGRW 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 152 IVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:PRK11288 411 LSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-217 |
4.02e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.72 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTkeySKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQnlnRMKHRN-IAKYRRGL 81
Cdd:PRK09700 267 EVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSpLDAVKKGM 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 GVVFQDFR---LLKDRNIYENIAFAlrvtetptRVIKK-KVPAALSLVG--------------LAQKYKSFPK---ELSG 140
Cdd:PRK09700 341 AYITESRRdngFFPNFSIAQNMAIS--------RSLKDgGYKGAMGLFHevdeqrtaenqrelLALKCHSVNQnitELSG 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 141 GEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVS 217
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-195 |
4.48e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 3 ELRNVTKE--YSKGH-AALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNP---TEGTIIVNGQNLNrmkhrniAK 76
Cdd:TIGR00956 761 HWRNLTYEvkIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD-------SS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRGLGVVFQDFRLLKDRNIYENIAFALRVTEtPTRVIKKK----VPAALSLVGLaQKYKS----FPKE-LSGGEQQRVA 147
Cdd:TIGR00956 834 FQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQ-PKSVSKSEkmeyVEEVIKLLEM-ESYADavvgVPGEgLNVEQRKRLT 911
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 148 IARAIVNEPAILL-ADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH 195
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-215 |
8.31e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNgqnlnrmkhRNIAKYRRGLGVVFqdfrllkDRNIY 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI---------RGSVAYVPQVSWIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 ENIAFALRVTetPTRVIKkkvpaALSLVGLAQKYKSFPKE-----------LSGGEQQRVAIARAIVNEPAILLADEPTG 166
Cdd:PLN03232 697 ENILFGSDFE--SERYWR-----AIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505341235 167 NLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMnERVITMKQGVI 215
Cdd:PLN03232 770 ALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMI 817
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-194 |
9.97e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 9.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKgHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLI--MKELNptEGTIIVNGQNLNRMKHRN-----I 74
Cdd:NF033858 2 ARLEGVSHRYGK-TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagARKIQ--QGRVEVLGGDMADARHRRavcprI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 75 AKYRRGLGvvfqdfrllkdRNIY------ENIAF-----ALRVTETPTRVikkkvpAALSL-VGLAqkykSFPK----EL 138
Cdd:NF033858 79 AYMPQGLG-----------KNLYptlsvfENLDFfgrlfGQDAAERRRRI------DELLRaTGLA----PFADrpagKL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 139 SGGEQQRVAIARAIVNEPAILLADEPTGNLDPTnS----WEIMSLLKEANErGTTVLVVT 194
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDPL-SrrqfWELIDRIRAERP-GMSVLVAT 195
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-218 |
1.06e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 13 KGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPT--------EGTIIVNGQNLNRMKHRNIAKYRRGLGVV 84
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 85 FQDFRLLKDRNIYENIAF--ALRVTETpTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVN-------- 154
Cdd:PRK13547 92 AQPAFAFSAREIVLLGRYphARRAGAL-THRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaa 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 155 -EPAILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSD 218
Cdd:PRK13547 171 qPPRYLLLDEPTAALDLAHQHRLLDTVRRlARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-215 |
3.33e-10 |
|
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: 59.57 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHA-ALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQnlnrmkhrniakyrrg 80
Cdd:TIGR00957 637 ITVHNATFTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------------- 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQDFRLLKDrNIYENIAFALRVTEtptrvikKKVPAALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIA 149
Cdd:TIGR00957 701 VAYVPQQAWIQND-SLRENILFGKALNE-------KYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLA 772
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 150 RAIVNEPAILLADEPTGNLDPTNSWEI-------MSLLKeanerGTTVLVVTHNQEIVNEMnERVITMKQGVI 215
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIfehvigpEGVLK-----NKTRILVTHGISYLPQV-DVIIVMSGGKI 839
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-206 |
4.05e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.23 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 27 RGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTII-VNGQNLNrmkhrniakyrrglgvvfqdfrllkdrniyeniafalr 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDIL-------------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 106 vtetptrvikkkvpAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMS------L 179
Cdd:smart00382 43 --------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlL 108
|
170 180
....*....|....*....|....*..
gi 505341235 180 LKEANERGTTVLVVTHNQEIVNEMNER 206
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLR 135
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-227 |
4.61e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.79 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 19 NGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKEL-NPTEGTIIVNGQNLnrmKHRNIAK-YRRGLGVVFQDFR---LLKD 93
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYpGRWEGEIFIDGKPV---KIRNPQQaIAQGIAMVPEDRKrdgIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 94 RNIYENIAFA-LRVTETPTRV------------IKK-KVPAALSLVGLAQkyksfpkeLSGGEQQRVAIARAIVNEPAIL 159
Cdd:PRK13549 356 MGVGKNITLAaLDRFTGGSRIddaaelktilesIQRlKVKTASPELAIAR--------LSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIvsdekKGGYINE 227
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL-----KGDLINH 490
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
10-195 |
6.02e-10 |
|
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: 58.26 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 10 EYSKGHAALNGVSVKIE-----RGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNgqnlnrMKhrnIA---KYrrgl 81
Cdd:COG1245 343 EYPDLTKSYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LK---ISykpQY---- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 82 gvVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKkvpaaLSLVGLAQKYKsfpKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:COG1245 410 --ISPDYDGTVEEFLRSANTDDFGSSYYKTEIIKP-----LGLEKLLDKNV---KDLSGGELQRVAIAACLSRDADLYLL 479
|
170 180 190
....*....|....*....|....*....|....*
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTH 195
Cdd:COG1245 480 DEPSAHLDVEQRLAVAKAIRRfAENRGKTAMVVDH 514
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-195 |
7.72e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 7.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYskGHAAL-NGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVnGQNLNrmkhrniakyrrg 80
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK------------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQdFR--LLKDRNIYENIAFALRVtetpTRVIKKKVP-----AALSLVGLAQKYKSfpKELSGGEQQRVAIARAIV 153
Cdd:PRK11819 389 LAYVDQ-SRdaLDPNKTVWEEISGGLDI----IKVGNREIPsrayvGRFNFKGGDQQKKV--GVLSGGERNRLHLAKTLK 461
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505341235 154 NEPAILLADEPTGNLDPtnswEIMSLLKEA-NERGTTVLVVTH 195
Cdd:PRK11819 462 QGGNVLLLDEPTNDLDV----ETLRALEEAlLEFPGCAVVISH 500
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
10-208 |
1.01e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 10 EYSKGHAALNGVSVKIE-----RGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVN------GQNLNRMKHRNIAKYR 78
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPDYDGTVEDLL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 RGLGVVFqdfrllkDRNIYEN-IAFALRVTetptRVIKKKVpaalslvglaqkyksfpKELSGGEQQRVAIARAIVNEPA 157
Cdd:PRK13409 422 RSITDDL-------GSSYYKSeIIKPLQLE----RLLDKNV-----------------KDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505341235 158 ILLADEPTGNLDPTNSWEIMSLLKE-ANERGTTVLVVTHNQEIVNEMNERVI 208
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRiAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-200 |
2.76e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 55.34 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLiklimkelnpTEGTIIVNGQNlnrmkhrniaKYRRGLGVVFQDFRLLKDRNIY 97
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQR----------RYVESLSAYARQFLGQMDKPDV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 ENIAfALrvteTPTRVIKKKVPAA-------------------LSLVGLAQK----------YKSFPKE---LSGGEQQR 145
Cdd:cd03270 71 DSIE-GL----SPAIAIDQKTTSRnprstvgtvteiydylrllFARVGIRERlgflvdvglgYLTLSRSaptLSGGEAQR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 146 VAIARAIVNE--PAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIV 200
Cdd:cd03270 146 IRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTI 202
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
18-200 |
2.81e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 55.70 E-value: 2.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLI----------KLIMKELNPTEGTIIVNGQNLNRMKH-----------RNIAK 76
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDRIEGLEHIDKVIVidqspigrtprSNPAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 77 YRRglgvVFQDFRLL-------------------KDRNIYE----NIAFALRVTETPTRvIKKKVpAALSLVGLAqkY-- 131
Cdd:cd03271 91 YTG----VFDEIRELfcevckgkrynretlevryKGKSIADvldmTVEEALEFFENIPK-IARKL-QTLCDVGLG--Yik 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 132 --KSFPkELSGGEQQRVAIARAIVNE---PAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIV 200
Cdd:cd03271 163 lgQPAT-TLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVI 235
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2-202 |
3.12e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-------------------SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVN 62
Cdd:PRK13546 5 VNIKNVTKEYriyrtnkermkdalipkhkNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 63 GQnlnrmkhrniakyrrgLGVVFQDFRLLKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGE 142
Cdd:PRK13546 85 GE----------------VSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 143 QQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNE 202
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQ 208
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
15-199 |
3.56e-09 |
|
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: 54.25 E-value: 3.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 15 HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKElnptegtiivngqNLNRMKHRNIAKYRRGLGVVFQDFRLLKDR 94
Cdd:cd03238 8 VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYA-------------SGKARLISFLPKFSRNKLIFIDQLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 95 NiyeniafalrvtetptrvikkkvpaaLSLVGLAQKYKSfpkeLSGGEQQRVAIARAIVNEP--AILLADEPTGNLDPTN 172
Cdd:cd03238 75 G--------------------------LGYLTLGQKLST----LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQD 124
|
170 180
....*....|....*....|....*..
gi 505341235 173 SWEIMSLLKEANERGTTVLVVTHNQEI 199
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDV 151
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-213 |
6.00e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.51 E-value: 6.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 4 LRNVTKEYSkGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNiaKYRRGLGV 83
Cdd:PRK10982 1 MSNISKSFP-GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 84 VFQDFRLLKDRNIYENIAF------ALRVTETPTRVIKKKVPAALSLvglaqkyKSFPKE----LSGGEQQRVAIARAIV 153
Cdd:PRK10982 78 VHQELNLVLQRSVMDNMWLgryptkGMFVDQDKMYRDTKAIFDELDI-------DIDPRAkvatLSVSQMQMIEIAKAFS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 154 NEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK10982 151 YNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-220 |
6.09e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.13 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEYSKGHAaLNGVSVKIERGEFVFIVGDSGSGKSTLiKLIMKELNPTEG-------TIIVNGQNLNRM--KHR 72
Cdd:NF000106 14 VEVRGLVKHFGEVKA-VDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGrrpwrf*TWCANRRALRRTig*HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 73 NIAKYRRglgvvfqdfrllKDRNIYENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAI 152
Cdd:NF000106 92 PVR*GRR------------ESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 153 VNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIVSDEK 220
Cdd:NF000106 160 IGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-216 |
6.59e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.65 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIM--KELNPTEGTIIVNGQNLNRMKHRNIAkyRRGLGVVFQ--------- 86
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPEERA--HLGIFLAFQypieipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 87 --DF-RL-LKDRNIYEN------IAFalrvtetpTRVIKKKvpaaLSLVGLAQKY--KSFPKELSGGEQQRVAIARAIVN 154
Cdd:CHL00131 101 naDFlRLaYNSKRKFQGlpeldpLEF--------LEIINEK----LKLVGMDPSFlsRNVNEGFSGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 155 EPAILLADEPTGNLD----PTNSWEIMSLLKEANergtTVLVVTHNQEIVNEMN-ERVITMKQGVIV 216
Cdd:CHL00131 169 DSELAILDETDSGLDidalKIIAEGINKLMTSEN----SIILITHYQRLLDYIKpDYVHVMQNGKII 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-213 |
1.52e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVTkeySKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNL-NRMKHRNIakyRR 79
Cdd:PRK10982 250 ILEVRNLT---SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInNHNANEAI---NH 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 80 GLGVVFQDFRllkDRNIYEN--IAFA-----LRVTETPTRVIK-KKVPAALSLVGLAQKYKSfPKE------LSGGEQQR 145
Cdd:PRK10982 324 GFALVTEERR---STGIYAYldIGFNslisnIRNYKNKVGLLDnSRMKSDTQWVIDSMRVKT-PGHrtqigsLSGGNQQK 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQG 213
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
33-169 |
1.60e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 33 IVGDSGSGKSTLIKLIMKELNPTEGTIIVNgqnlnrmkhrniAKYRRGlgvVFQDFRLlkDrniyeniafALRVTETPTR 112
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRS------------AKVRMA---VFSQHHV--D---------GLDLSSNPLL 593
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 113 --------VIKKKVPAALSLVGLAQKYKSFPK-ELSGGEQQRVAIARAIVNEPAILLADEPTGNLD 169
Cdd:PLN03073 594 ymmrcfpgVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-215 |
1.64e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVngqnlnrmkHRNIAKYRRGLGVVFqdfrllkDRNIY 97
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------IRGTVAYVPQVSWIF-------NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 ENIAFALrvTETPTRVIKkkvpaALSLVGLAQKYKSFPK-----------ELSGGEQQRVAIARAIVNEPAILLADEPTG 166
Cdd:PLN03130 697 DNILFGS--PFDPERYER-----AIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505341235 167 NLDPTNSWEIM-SLLKEANERGTTVLVVthNQEIVNEMNERVITMKQGVI 215
Cdd:PLN03130 770 ALDAHVGRQVFdKCIKDELRGKTRVLVT--NQLHFLSQVDRIILVHEGMI 817
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
7-196 |
2.47e-08 |
|
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: 52.75 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 7 VTKEYSKGHAALNGVSVkIERGEFVFIVGDSGSGKSTLIKLIMKELNPtegtiivngqNLNRMKH----RNIAKYRRGlg 82
Cdd:cd03236 6 PVHRYGPNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGKLKP----------NLGKFDDppdwDEILDEFRG-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 VVFQDF--RLLKDRniyeniafaLRVTETPTRV--------------IKKK--------VPAALSLVGLAQKYKSfpkEL 138
Cdd:cd03236 73 SELQNYftKLLEGD---------VKVIVKPQYVdlipkavkgkvgelLKKKdergkldeLVDQLELRHVLDRNID---QL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 139 SGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHN 196
Cdd:cd03236 141 SGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-195 |
3.01e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 32 FIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNrmkhrNIAKYRrgLGVVFQDFRLLKDRNIYENIAFALRVTETPT 111
Cdd:PRK13541 30 YIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN-----NIAKPY--CTYIGHNLGLKLEMTVFENLKFWSEIYNSAE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 112 rvikkKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVL 191
Cdd:PRK13541 103 -----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVL 177
|
....
gi 505341235 192 VVTH 195
Cdd:PRK13541 178 LSSH 181
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-227 |
5.05e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 15 HAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKYRRGLgvvfqdfrllkdr 94
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 95 niyENIAFALRVTETPTRVIKKKVPAALSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSW 174
Cdd:PRK13545 104 ---ENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505341235 175 EIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGVIvsdeKKGGYINE 227
Cdd:PRK13545 181 KCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQV----KEYGDIKE 229
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-211 |
1.10e-07 |
|
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: 49.67 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 27 RGEFVFIVGDSGSGKSTLIKLIMkelnptegtIIVNGQNLNRMKHRNIAkyrRGLGVVFQDFRLlkdrniyeniafalrv 106
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG---------LALGGAQSATRRRSGVK---AGCIVAAVSAEL---------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 107 tetptrvikkkvpaALSLVGLaqkyksfpkelSGGEQQRVAIA-----RAIVNEPAILLaDEPTGNLDPTNSWEIMSLLK 181
Cdd:cd03227 72 --------------IFTRLQL-----------SGGEKELSALAlilalASLKPRPLYIL-DEIDRGLDPRDGQALAEAIL 125
|
170 180 190
....*....|....*....|....*....|
gi 505341235 182 EANERGTTVLVVTHNQEiVNEMNERVITMK 211
Cdd:cd03227 126 EHLVKGAQVIVITHLPE-LAELADKLIHIK 154
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
138-195 |
1.14e-07 |
|
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: 51.47 E-value: 1.14e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 138 LSGGEQQRVAIARAIVNEPAILLADEPTGNLDP-TNSWeimsLLKEANERGTTVLVVTH 195
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAeSVAW----LERHLQEYPGTVVAVTH 216
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-220 |
1.27e-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: 50.68 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIakyRRGLGVVFQDFRLLKDrniy 97
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL---RSRLSIILQDPILFSG---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 eNIAFALrvtETPTRVIKKKVPAALSLVGLAQKYKSFPKEL-----------SGGEQQRVAIARAIVNEPAILLADEPTG 166
Cdd:cd03288 110 -SIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505341235 167 NLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEmnERVITMKQGVIVSDEK 220
Cdd:cd03288 186 SIDMATENILQKVVMTAFADRTVVTIAHRVSTILDA--DLVLVLSRGILVECDT 237
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-208 |
1.69e-07 |
|
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: 49.49 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 25 IERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIivngqnlnrmkhrniakyrrglgvvfqdfrllkdrniyeniafal 104
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND--------------------------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 105 rvtetptrvikkkvpaalSLVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAN 184
Cdd:cd03222 57 ------------------EWDGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS 118
|
170 180
....*....|....*....|....*
gi 505341235 185 ERGT-TVLVVTHNQEIVNEMNERVI 208
Cdd:cd03222 119 EEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
21-201 |
1.89e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 1.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 21 VSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTI-IVNGQNLNRMKHRNIAkyrrglgvvFQDFRLL-------- 91
Cdd:PRK15064 20 ISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQDQFA---------FEEFTVLdtvimght 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 92 --------KDRnIYENIAFA----LRVTETPTRVIKKKVPAA-------LSLVGLAQKYKSFP-KELSGGEQQRVAIARA 151
Cdd:PRK15064 91 elwevkqeRDR-IYALPEMSeedgMKVADLEVKFAEMDGYTAearagelLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505341235 152 IVNEPAILLADEPTGNLD-PTNSWeimsLLKEANERGTTVLVVTHNQEIVN 201
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLDiNTIRW----LEDVLNERNSTMIIISHDRHFLN 216
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
136-195 |
2.09e-07 |
|
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: 50.94 E-value: 2.09e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 136 KELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTH 195
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
120-201 |
5.11e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 5.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 120 AALSLVGLAQKYKSfpKELSGGEQQRVAIARAIVNEPAILLADEPTGNLD-PTNSWEIMSLLKEANergtTVLVVTHNQE 198
Cdd:PLN03073 329 AGLSFTPEMQVKAT--KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDlHAVLWLETYLLKWPK----TFIVVSHARE 402
|
...
gi 505341235 199 IVN 201
Cdd:PLN03073 403 FLN 405
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-169 |
7.29e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 7.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIivngqnlnrmkhrNIAKYRRgLGVVFQdfrllkdrniy 97
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAKGIK-LGYFAQ----------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 98 ENIAFaLRVTETPTRVIKKKVPAALS------LVGL---AQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNL 168
Cdd:PRK10636 383 HQLEF-LRADESPLQHLARLAPQELEqklrdyLGGFgfqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
.
gi 505341235 169 D 169
Cdd:PRK10636 462 D 462
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-208 |
9.05e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 9.05e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 138 LSGGEQQRVAIARAIVNEPA--ILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNeMNERVI 208
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMIS-LADRII 548
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-195 |
1.37e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 25 IERGEFVFIVGDSGSGKSTLIKLIMKELNPtegtiivngqNLNRMKH-----RNIAKYRrglGVVFQD-FRLLKDRNIye 98
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIP----------NLGDYEEepswdEVLKRFR---GTELQNyFKKLYNGEI-- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 99 niafalRVTETPT------RVIKKKVPAALSLV---GLAQKYKSF----------PKELSGGEQQRVAIARAIVNEPAIL 159
Cdd:PRK13409 161 ------KVVHKPQyvdlipKVFKGKVRELLKKVderGKLDEVVERlglenildrdISELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*.
gi 505341235 160 LADEPTGNLDPTNSWEIMSLLKEANErGTTVLVVTH 195
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEH 269
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-200 |
1.71e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.24 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIivngqnlnrMKHRNIAKYRRGLGVVFQDFR---LLKDR 94
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERSIAYVPQQAWIMNATVRgniLFFDE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 95 NIYENIAFALRVTETPTRVikkkvpAALSlVGLAQKYKSFPKELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSW 174
Cdd:PTZ00243 747 EDAARLADAVRVSQLEADL------AQLG-GGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGE 819
|
170 180
....*....|....*....|....*.
gi 505341235 175 EIMSLLKEANERGTTVLVVTHNQEIV 200
Cdd:PTZ00243 820 RVVEECFLGALAGKTRVLATHQVHVV 845
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-195 |
2.33e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.81 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 2 IELRNVTKEY-SKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkhrNIAKYRRG 80
Cdd:PLN03130 1238 IKFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 81 LGVVFQD--------------FRLLKDRNIYENIAFA-LRvtetptRVIKKKvpaalSLvGLAQKYKSFPKELSGGEQQR 145
Cdd:PLN03130 1315 LGIIPQApvlfsgtvrfnldpFNEHNDADLWESLERAhLK------DVIRRN-----SL-GLDAEVSEAGENFSVGQRQL 1382
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEaNERGTTVLVVTH 195
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE-EFKSCTMLIIAH 1431
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
138-195 |
2.45e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.45e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 138 LSGGEQQRVAIARAIVNEPAILLADEPTGNLDP-TNSWeimsLLKEANERGTTVLVVTH 195
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVAW----LEQFLHDYPGTVVAVTH 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-199 |
3.18e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 22 SVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMKHRNIAKyrrglgVVFQDFrllKDRNiyeniA 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK------LVSDEW---QRNN-----T 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 102 FALRVTE-----TPTRVIKKKVPAALSLVGLAQKY-------KSFpKELSGGEQQRVAIARAIVNEPAILLADEPTGNLD 169
Cdd:PRK10938 89 DMLSPGEddtgrTTAEIIQDEVKDPARCEQLAQQFgitalldRRF-KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190
....*....|....*....|....*....|.
gi 505341235 170 PTNSWEIMSLLKEANERGTT-VLVVTHNQEI 199
Cdd:PRK10938 168 VASRQQLAELLASLHQSGITlVLVLNRFDEI 198
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-205 |
4.02e-06 |
|
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: 46.06 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 33 IVGDSGSGKSTLIKLIMKELNPTEGTiivngqNLNRMKH-RNIAKYRRGLGVVFQDFRLLKDR--------NIYENIAFa 103
Cdd:cd03240 27 IVGQNGAGKTTIIEALKYALTGELPP------NSKGGAHdPKLIREGEVRAQVKLAFENANGKkytitrslAILENVIF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 104 lrvtetptrvikkkVPAALSLVGLAQKyksfPKELSGGEQQ------RVAIARAIVNEPAILLADEPTGNLDPTNSW--- 174
Cdd:cd03240 100 --------------CHQGESNWPLLDM----RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEesl 161
|
170 180 190
....*....|....*....|....*....|..
gi 505341235 175 -EIMSLLKEanERGTTVLVVTHNQEIVNEMNE 205
Cdd:cd03240 162 aEIIEERKS--QKNFQLIVITHDEELVDAADH 191
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
138-216 |
5.93e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.32 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 138 LSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVvthnqeIVNEMNE------RVITMK 211
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIV------ISSELPEllgmcdRIYVMN 478
|
....*
gi 505341235 212 QGVIV 216
Cdd:NF040905 479 EGRIT 483
|
|
| Rad50_Sulf |
NF041034 |
DNA double-strand break repair ATPase Rad50; |
138-199 |
1.50e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 468963 [Multi-domain] Cd Length: 872 Bit Score: 45.47 E-value: 1.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 138 LSGGEQ------QRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEI 199
Cdd:NF041034 780 LSGGERisialaLRLAIAKSLMDEIGFMILDEPTVHLDEERKKELIDIIRSSMEIVPQIIVVTHDEEL 847
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
18-212 |
1.72e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQ-NLNRMKHRNIAKYRRGLGVVF---QDFRLLK- 92
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAWVNQETPALPQPALEYVIdgdREYRQLEa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 93 ------DRNIYENIAFA---LRVTETPTrvIKKKVPAALSLVGLAQKYKSFP-KELSGGEQQRVAIARAIVNEPAILLAD 162
Cdd:PRK10636 97 qlhdanERNDGHAIATIhgkLDAIDAWT--IRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505341235 163 EPTGNLDPTNSWEIMSLLKeaNERGTTVLvVTHNQEIVNEMNERVITMKQ 212
Cdd:PRK10636 175 EPTNHLDLDAVIWLEKWLK--SYQGTLIL-ISHDRDFLDPIVDKIIHIEQ 221
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-217 |
1.93e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLIKLIM--KELNPTEGTIIVNGQNLNRMKHRNIAKY-------------RRGLg 82
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQETFARISGYceqndihspqvtvRESL- 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 83 vVFQDF-RLLKDRNIYENIAFALRVTETPTRVIKKKvpaalSLVGLAQKyksfpKELSGGEQQRVAIARAIVNEPAILLA 161
Cdd:PLN03140 975 -IYSAFlRLPKEVSKEEKMMFVDEVMELVELDNLKD-----AIVGLPGV-----TGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 162 DEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEI-VNEMNERVITMKQG--VIVS 217
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIdIFEAFDELLLMKRGgqVIYS 1102
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
24-214 |
4.59e-05 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 43.03 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 24 KIERGEFVFIVGDSGSGKSTLIKLIMKEL-------NPTEGTIIVNGQNLNRMK-----HRNIAKYR--RGLGVVFQDFR 89
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITYALygktpryGRQENLRSVFAPGEDTAEvsftfQLGGKKYRveRSRGLDYDQFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 90 llkdRNIY----ENIAFALRVTETptrvikkkvpaalslvglaqkyksfpkeLSGGEQQRVAIARA------IVNEPAI- 158
Cdd:cd03279 104 ----RIVLlpqgEFDRFLARPVST----------------------------LSGGETFLASLSLAlalsevLQNRGGAr 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 159 ---LLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMNERVITMKQGV 214
Cdd:cd03279 152 leaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVIKTPG 210
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-211 |
9.47e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 42.68 E-value: 9.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGeFVFIVGDSGSGKSTLIKLI-------------------MKELNPTEGTIIVN-GQNLNRMKHR----- 72
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALrlllgpsssrkfdeedfylGDDPDLPEIEIELTfGSLLSRLLRLllkee 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 73 -------NIAKYRRGLGVVFQDFR-LLKDR--NIYENIAFALRVTETPTRVIKKKVpaalsLVGLAQKYKSFPKELSGGE 142
Cdd:COG3593 93 dkeeleeALEELNEELKEALKALNeLLSEYlkELLDGLDLELELSLDELEDLLKSL-----SLRIEDGKELPLDRLGSGF 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505341235 143 QQRVAIA--RAIV-----NEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMN-ERVITMK 211
Cdd:COG3593 168 QRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPlENIRRLR 244
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
137-201 |
9.75e-05 |
|
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: 9.75e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 137 ELSGGEQQ---RVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVN 201
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
18-53 |
1.18e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 1.18e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLI-----KLIMKELN 53
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLInetlyKALARKLN 665
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
19-49 |
1.34e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 38.74 E-value: 1.34e-04
10 20 30
....*....|....*....|....*....|.
gi 505341235 19 NGVSVKIERGEFVFIVGDSGSGKSTLIKLIM 49
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQ 43
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-200 |
1.70e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 1.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505341235 138 LSGGEQQRVAIARAIVN---EPAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIV 200
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV 875
|
|
| AAA_16 |
pfam13191 |
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ... |
27-60 |
2.60e-04 |
|
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.
Pssm-ID: 433025 [Multi-domain] Cd Length: 167 Bit Score: 40.18 E-value: 2.60e-04
10 20 30
....*....|....*....|....*....|....
gi 505341235 27 RGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTII 60
Cdd:pfam13191 23 RPPSVLLTGEAGTGKTTLLRELLRALERDGGYFL 56
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
18-200 |
3.59e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLI----------KLIMKELNPTEGTIIVNGQNLNRMKH---------------- 71
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIndtlypalanRLNGAKTVPGRYTSIEGLEHLDKVIHidqspigrtprsnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 72 --------RNI------AKYR-------------------RGLGVVFQDFRLLKD--------------RNIYE------ 98
Cdd:TIGR00630 704 ytgvfdeiRELfaetpeAKVRgytpgrfsfnvkggrceacQGDGVIKIEMHFLPDvyvpcevckgkrynRETLEvkykgk 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 99 NIAFALRVTETPTRVIKKKVPA------ALSLVGL-----AQKYKSfpkeLSGGEQQRVAIARAI---VNEPAILLADEP 164
Cdd:TIGR00630 784 NIADVLDMTVEEAYEFFEAVPSisrklqTLCDVGLgyirlGQPATT----LSGGEAQRIKLAKELskrSTGRTLYILDEP 859
|
250 260 270
....*....|....*....|....*....|....*.
gi 505341235 165 TGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIV 200
Cdd:TIGR00630 860 TTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI 895
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-213 |
4.67e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.77 E-value: 4.67e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505341235 138 LSGGEQQRVAIARAIVNE--PAILLADEPTGNLDPTNSWEIMSLLKEANERGTTVLVVTHNQEIVNEMnERVITMKQG 213
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAA-DYVIDIGPG 565
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
137-195 |
6.54e-04 |
|
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: 40.50 E-value: 6.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505341235 137 ELSGGEQQRVAIARAIVNEPAILLADEPTGNLDPTNSWEIMSLLKEAnerGTTVLVVTH 195
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-53 |
6.76e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.39 E-value: 6.76e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTLI-----KLIMKELN 53
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVndilyPALARKLN 661
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
12-54 |
7.00e-04 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.77 E-value: 7.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 505341235 12 SKGH-AALNGVSVKIERGE-FVFIVGDSGSGKSTLIKLIMKELNP 54
Cdd:COG3267 25 SPSHrEALARLEYALAQGGgFVVLTGEVGTGKTTLLRRLLERLPD 69
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-216 |
2.57e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 37.85 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 1 MIELRNVtKEYSKGHAALNGVSVKIERGEFVFIVGDSGSGKSTLIKLIM--KELNPTEGTIIVNGQNLNRMKHRNiakyR 78
Cdd:PRK09580 1 MLSIKDL-HVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 79 RGLGvVFQDFRLLKDRNIYENiAFALRVTETPTRVIKKKVP-----------AALSLVGLAQKY--KSFPKELSGGEQQR 145
Cdd:PRK09580 76 AGEG-IFMAFQYPVEIPGVSN-QFFLQTALNAVRSYRGQEPldrfdfqdlmeEKIALLKMPEDLltRSVNVGFSGGEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505341235 146 VAIARAIVNEPAILLADEPTGNLDpTNSWEIMSLLKEANERGT-TVLVVTHNQEIVNEMN-ERVITMKQGVIV 216
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLD-IDALKIVADGVNSLRDGKrSFIIVTHYQRILDYIKpDYVHVLYQGRIV 225
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
18-44 |
2.90e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 2.90e-03
10 20
....*....|....*....|....*..
gi 505341235 18 LNGVSVKIERGEFVFIVGDSGSGKSTL 44
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| COG4928 |
COG4928 |
Predicted P-loop ATPase, KAP-like [General function prediction only]; |
33-62 |
3.04e-03 |
|
Predicted P-loop ATPase, KAP-like [General function prediction only];
Pssm-ID: 443956 Cd Length: 386 Bit Score: 37.97 E-value: 3.04e-03
10 20 30
....*....|....*....|....*....|
gi 505341235 33 IVGDSGSGKSTLIKLIMKELNPTEGTIIVN 62
Cdd:COG4928 34 LDGEWGSGKTSFLNLIEKELESNEKVIVVY 63
|
|
| type_II_IV_secretion_ATPases |
cd19477 |
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP ... |
25-87 |
3.86e-03 |
|
type II/type IV hexameric secretion ATPases; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410885 [Multi-domain] Cd Length: 168 Bit Score: 36.99 E-value: 3.86e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505341235 25 IERGEFVFIVGDSGSGKSTLIKLIMKELNPTEGTIIV-NGQNLNRMKHRNIAKYRRGLGVVFQD 87
Cdd:cd19477 7 IAIGKNVIVCGGTGSGKTTYIKSILEFIPKEERIISIeDTEEIVFKHHKNYTQLFFGGNITSAD 70
|
|
| T7SS_EccC_b |
TIGR03925 |
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit ... |
21-90 |
3.96e-03 |
|
type VII secretion protein EccCb; This model represents the C-terminal domain or EccCb subunit of the type VII secretion protein EccC as found in the Actinobacteria. Type VII secretion is defined more broadly as including secretion systems for ESAT-6-like proteins in the Firmicutes as well as in the Actinobacteria, but this family does not show close homologs in the Firmicutes. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 274859 [Multi-domain] Cd Length: 566 Bit Score: 38.05 E-value: 3.96e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505341235 21 VSVKIERGEFVFIVGDSGSGKSTLIKLIMKEL----NPTEGTIIVngqnlnrmkhrniAKYRRGL-GVVFQDFRL 90
Cdd:TIGR03925 356 VYVDFAESPHLLIFGDSESGKTTLLRTIARGIvrrySPDQARLVV-------------VDYRRTLlGAVPEDYLA 417
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
30-60 |
5.85e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 36.74 E-value: 5.85e-03
10 20 30
....*....|....*....|....*....|.
gi 505341235 30 FVFIVGDSGSGKSTLIKLIMKELNPTEGTII 60
Cdd:COG0572 9 IIGIAGPSGSGKTTFARRLAEQLGADKVVVI 39
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
31-132 |
7.77e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 36.19 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505341235 31 VFIVGDSGSGKSTLIKLIMKELNPTEGTIIVNGQNLNRMkHRN----IAKYRRGLGVVFQDF-RLLKDRNIYE------N 99
Cdd:pfam06414 14 ILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFREL-HPHyrelQAADPKTASEYTQPDaSRWVEKLLQHaiengyN 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 505341235 100 IAF--ALRVTETP---TRVIKKK----------VPAALSLVGLAQKYK 132
Cdd:pfam06414 93 IILegTLRSPDVAkkiARALKAAgyrvevaavaAPPELSWLGVLDRYE 140
|
|
| HerA |
COG0433 |
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase ... |
14-61 |
9.56e-03 |
|
Archaeal DNA helicase HerA or a related bacterial ATPase, contains HAS-barrel and ATPase domains [Replication, recombination and repair];
Pssm-ID: 440202 [Multi-domain] Cd Length: 388 Bit Score: 36.51 E-value: 9.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 505341235 14 GHAALNGVSVKIERGEF----VFIVGDSGSGKSTLIKLIMKELNPTEGTIIV 61
Cdd:COG0433 29 GKLLSPGVPVYLDLDKLlnrhILILGATGSGKSNTLQVLLEELSRAGVPVLV 80
|
|
| DEXSc_Pif1_like |
cd18037 |
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like ... |
25-54 |
9.73e-03 |
|
DEAD-box helicase domain of Pif1; Pif1 and other members of this family are RecD-like helicases involved in maintaining genome stability through unwinding double-stranded DNAs (dsDNAs), DNA/RNA hybrids, and G quadruplex (G4) structures. The members of Pif1 helicase subfamily studied so far all appear to contribute to telomere maintenance. Pif1 is a member of the DEAD-like helicases superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.
Pssm-ID: 350795 [Multi-domain] Cd Length: 183 Bit Score: 35.69 E-value: 9.73e-03
10 20 30
....*....|....*....|....*....|
gi 505341235 25 IERGEFVFIVGDSGSGKSTLIKLIMKELNP 54
Cdd:cd18037 9 VLDGKNVFFTGSAGTGKSYLLRRIIRALPS 38
|
|
| |
