|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-215 |
2.15e-112 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 320.46 E-value: 2.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRN 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
2.77e-97 |
|
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: 281.83 E-value: 2.77e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRN 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
1.01e-72 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 219.91 E-value: 1.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPE---ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLL 77
Cdd:COG1136 4 LLELRNLTKSYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RR-NIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQP 156
Cdd:COG1136 84 RRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 157 RILLADEPTGNVDPQLARR-LLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRLE 216
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEvLELLRELNRELGTTIVMVTHDPELAARAD-RVIRLRDGRIV 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
1.02e-70 |
|
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: 214.66 E-value: 1.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPE---ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLR 78
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 R-NIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 158 ILLADEPTGNVDPQLARR-LLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRL 215
Cdd:cd03255 161 IILADEPTGNLDSETGKEvMELLRELNKEAGTTIVVVTHDPELAEYAD-RIIELRDGKI 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
7.55e-66 |
|
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: 202.25 E-value: 7.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNI 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 162 DEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-216 |
4.97e-55 |
|
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: 175.31 E-value: 4.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPE---ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLL 77
Cdd:COG4181 8 IIELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 R-RNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDviELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQP 156
Cdd:COG4181 88 RaRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 157 RILLADEPTGNVDPQLARR-LLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRLE 216
Cdd:COG4181 166 AILFADEPTGNLDAATGEQiIDLLFELNRERGTTLVLVTHDPALAARCD-RVLRLRAGRLV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-171 |
1.42e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 172.18 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGP---EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLL 77
Cdd:COG1135 1 MIELENLSKTFPTKGgpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170
....*....|....
gi 1426272298 158 ILLADEPTGNVDPQ 171
Cdd:COG1135 161 VLLCDEATSALDPE 174
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-215 |
1.53e-52 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 168.51 E-value: 1.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRN 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-216 |
2.79e-52 |
|
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: 168.14 E-value: 2.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGP---EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLL 77
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 158 ILLADEPTGNVDPQLARRLLRLLLEL-NRLGTAVVIATHDLGLMDQVDARRMVLSGGRLE 216
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-171 |
3.69e-51 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 166.03 E-value: 3.69e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGP---EILRDVSFHLPERsfQFLS--GPSGAGKTTLLRLL--FmsLKPTRGLITIFGKdrskitrtE 73
Cdd:COG1116 7 ALELRGVSKRFPTGGggvTALDDVSLTVAAG--EFVAlvGPSGCGKSTLLRLIagL--EKPTSGEVLVDGK--------P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 74 LPLLRRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALI 153
Cdd:COG1116 75 VTGPGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170
....*....|....*...
gi 1426272298 154 EQPRILLADEPTGNVDPQ 171
Cdd:COG1116 155 NDPEVLLMDEPFGALDAL 172
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-216 |
1.66e-50 |
|
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: 163.07 E-value: 1.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrTELPLLRRNI 81
Cdd:cd03259 1 LELKGLSKTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-----TGVPPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 162 DEPTGNVDPQL-ARRLLRLLLELNRLGTAVVIATHD----LGLMDQVdarrMVLSGGRLE 216
Cdd:cd03259 155 DEPLSALDAKLrEELREELKELQRELGITTIYVTHDqeeaLALADRI----AVMNEGRIV 210
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-219 |
5.29e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 166.04 E-value: 5.29e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FmsLKPTRGLITIFGKDrskITRteLPLLR 78
Cdd:COG3842 5 ALELENVSKRYG-DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF--ETPDSGRILLDGRD---VTG--LPPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRI 158
Cdd:COG3842 77 RNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 159 LLADEPTGNVDPQL-ARRLLRLLLELNRLGTAVVIATHdlglmDQVDARRM-----VLSGGRL-------EIYD 219
Cdd:COG3842 157 LLLDEPLSALDAKLrEEMREELRRLQRELGITFIYVTH-----DQEEALALadriaVMNDGRIeqvgtpeEIYE 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-215 |
8.70e-50 |
|
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: 161.73 E-value: 8.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLLRRNI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKD---ITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQD-----FrlldHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQP 156
Cdd:COG1122 78 GLVFQNpddqlF----APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 157 RILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-215 |
1.01e-49 |
|
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: 162.07 E-value: 1.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRN 80
Cdd:COG1127 5 MIEVRNLTKSFG-DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGR-DESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRIL 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 160 LADEPTGNVDPQLARRLLRL-LLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELiRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
1.40e-49 |
|
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: 160.71 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 3 RFENVGHRYGMGPE-ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLLRRNI 81
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKD---LTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRL-LDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:cd03225 78 GLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-217 |
1.07e-48 |
|
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: 159.20 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNI 81
Cdd:cd03261 1 IELRGLTKSFG-GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGR-DESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 161 ADEPTGNVDPQLARRLLRL-LLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLEI 217
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLiRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-170 |
1.11e-48 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 159.00 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSkITRTELPLLRRN 80
Cdd:COG1126 1 MIEIENLHKSFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVAL-PLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRIL 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170
....*....|.
gi 1426272298 160 LADEPTGNVDP 170
Cdd:COG1126 159 LFDEPTSALDP 169
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-171 |
2.12e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 158.68 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRN 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALplrvrGR--DESTYRS-----------DVIELLKWVGLGERMHVLPPILSGGEKQRAA 147
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLA-----GRlgRTSTWRSllglfppedreRALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180
....*....|....*....|....
gi 1426272298 148 IARALIEQPRILLADEPTGNVDPQ 171
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPK 180
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-171 |
6.60e-47 |
|
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: 154.17 E-value: 6.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGP---EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrsKITRTelpllR 78
Cdd:cd03293 1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE---PVTGP-----G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRI 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170
....*....|...
gi 1426272298 159 LLADEPTGNVDPQ 171
Cdd:cd03293 153 LLLDEPFSALDAL 165
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-219 |
9.24e-47 |
|
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: 153.93 E-value: 9.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRteLPLLRRNI 81
Cdd:cd03300 1 IELENVSKFYG-GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD---ITN--LPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 162 DEPTGNVDPQLARRLLR-LLLELNRLGTAVVIATHD----LGLMDQVdarrMVLSGGRL-------EIYD 219
Cdd:cd03300 155 DEPLGALDLKLRKDMQLeLKRLQKELGITFVFVTHDqeeaLTMSDRI----AVMNKGKIqqigtpeEIYE 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-171 |
9.91e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 157.27 E-value: 9.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRY-GMGPEI--LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLL 77
Cdd:PRK11153 1 MIELKNISKVFpQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170
....*....|....
gi 1426272298 158 ILLADEPTGNVDPQ 171
Cdd:PRK11153 161 VLLCDEATSALDPA 174
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-219 |
1.28e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 157.16 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRL---LfmsLKPTRGLITIFGKDRskitrTELPLL 77
Cdd:COG3839 3 SLELENVSKSYG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMiagL---EDPTSGEILIGGRDV-----TDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 158 ILLADEPTGNVDPQL-ARRLLRLLLELNRLGTAVVIATHdlglmDQVDARRM-----VLSGGRL-------EIYD 219
Cdd:COG3839 154 VFLLDEPLSNLDAKLrVEMRAEIKRLHRRLGTTTIYVTH-----DQVEAMTLadriaVMNDGRIqqvgtpeELYD 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-215 |
1.45e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.68 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPE-RSFQFLsGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRRN 80
Cdd:COG1131 1 IEVRGLTKRYG-DKTALDGVSLTVEPgEIFGLL-GPNGAGKTTTIRMLLGLLRPTSGEVRVLGED----VARDPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
5.80e-45 |
|
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: 148.83 E-value: 5.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKiTRTELPLLRRNI 81
Cdd:cd03262 1 IEIKNLHKSFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVAL-PLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
1.17e-44 |
|
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: 145.87 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLLRRNIGVVFQDFRLLDHLTTY 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 98 ENVALPLRVRGRDESTYRSDVIELLKWVGLG----ERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-204 |
5.56e-44 |
|
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: 146.22 E-value: 5.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRN-IGV 83
Cdd:TIGR03608 2 KNISKKFG-DKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 84 VFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADE 163
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1426272298 164 PTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVD 204
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQAD 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-215 |
7.65e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 146.78 E-value: 7.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPeILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFG---KDRSKITRtelpLL 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDER----LI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVAL-PLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQP 156
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 157 RILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
9.78e-44 |
|
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: 144.64 E-value: 9.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRtELPLLRRNI 81
Cdd:cd03229 1 LELKNVSKRYG-QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLED-ELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPlrvrgrdestyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 162 DEPTGNVDPQLARRLLRL-LLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:cd03229 125 DEPTSALDPITRREVRALlKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-170 |
1.28e-43 |
|
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: 146.17 E-value: 1.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENValpLRVRGRDESTYRS-----------DVIELLKWVGLGERMHVLPPILSGGEKQRAAIAR 150
Cdd:cd03256 81 GMIFQQFNLIERLSVLENV---LSGRLGRRSTWRSlfglfpkeekqRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180
....*....|....*....|
gi 1426272298 151 ALIEQPRILLADEPTGNVDP 170
Cdd:cd03256 158 ALMQQPKLILADEPVASLDP 177
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
5.32e-42 |
|
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: 142.25 E-value: 5.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPE---ILRDVSFHLPE-RSFQfLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPL 76
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrvpVLKDVSLEVAPgESFG-LVGESGSGKSTLLRALAGLERPWSGEVTFDGRP---VTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 LRRNIGVVFQD--------FRLLDHLttyenvALPLRVRGRDEStyRSDVIELLKWVGLGER-MHVLPPILSGGEKQRAA 147
Cdd:COG1124 77 FRRRVQMVFQDpyaslhprHTVDRIL------AEPLRIHGLPDR--EERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 148 IARALIEQPRILLADEPTGNVDP--QlARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLE 216
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVsvQ-AEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-215 |
6.82e-42 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 141.92 E-value: 6.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRRN 80
Cdd:COG4555 1 MIEVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
7.12e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 7.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRNI 81
Cdd:COG4619 1 LELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---RRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHlTTYENVALPLRVRGRDEStyRSDVIELLKWVGLGErmHVLP-PI--LSGGEKQRAAIARALIEQPRI 158
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPP--DILDkPVerLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 159 LLADEPTGNVDPQLARR-LLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG4619 152 LLLDEPTSALDPENTRRvEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
2.22e-41 |
|
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: 146.59 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGP----EILRDVSFHLPERsfQFLS--GPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTEL 74
Cdd:COG1123 260 LLEVRNLSKRYPVRGkggvRAVDDVSLTLRRG--ETLGlvGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 75 PLLRRNIGVVFQD-FRLLD-HLTTYENVALPLRVRGR-DESTYRSDVIELLKWVGLGER-MHVLPPILSGGEKQRAAIAR 150
Cdd:COG1123 338 RELRRRVQMVFQDpYSSLNpRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 151 ALIEQPRILLADEPTGNVDP-------------QlarrllrlllelNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVsvqaqilnllrdlQ------------RELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-171 |
5.74e-41 |
|
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: 139.40 E-value: 5.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEiLRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKitrteLPLLRRNI 81
Cdd:cd03296 3 IEVRNVSKRFGDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-----VPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGR----DESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170
....*....|....
gi 1426272298 158 ILLADEPTGNVDPQ 171
Cdd:cd03296 157 VLLLDEPFGALDAK 170
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-216 |
6.37e-41 |
|
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: 138.54 E-value: 6.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrTELPLLRRNI 81
Cdd:cd03301 1 VELENVTKRFG-NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-----TDLPPKDRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 162 DEPTGNVDPQLARRLLR-LLLELNRLGTAVVIATHdlglmDQVDARRM-----VLSGGRLE 216
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAeLKRLQQRLGTTTIYVTH-----DQVEAMTMadriaVMNDGQIQ 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-216 |
8.49e-41 |
|
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: 139.01 E-value: 8.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrTELPLLRRNIGVVFQDFRLLDHLTTY 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-----TNLPPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 98 ENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQL-ARRL 176
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1426272298 177 LRLLLELNRLGTAVVIATHDLglmdqVDARRM-----VLSGGRLE 216
Cdd:cd03299 170 EELKKIRKEFGVTVLHVTHDF-----EEAWALadkvaIMLNGKLI 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
8.89e-41 |
|
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: 138.79 E-value: 8.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRY---GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLL 77
Cdd:cd03257 1 LLEVKNLSVSFptgGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQD-FRLLD-HLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLG---ERMHVLPPILSGGEKQRAAIARAL 152
Cdd:cd03257 81 RKEIQMVFQDpMSSLNpRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 153 IEQPRILLADEPTGNVDP-------------QlarrllrlllelNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03257 161 ALNPKLLIADEPTSALDVsvqaqildllkklQ------------EELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-219 |
1.06e-40 |
|
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: 138.97 E-value: 1.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLLRRNI 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGED---IREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGER--MHVLPPILSGGEKQRAAIARALIEQPRIL 159
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 160 LADEPTGNVDP-QLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLEIYD 219
Cdd:cd03295 158 LMDEPFGALDPiTRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-215 |
2.75e-40 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 137.84 E-value: 2.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKD---RSKITRTELPLLR 78
Cdd:COG4161 3 IQLKNINCFYG-SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDFRLLDHLTTYEN-VALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 158 ILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-215 |
1.32e-39 |
|
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: 135.39 E-value: 1.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL-----FMSLKPTRGLITIFGKDRSKITRTELpL 76
Cdd:cd03260 1 IELRDLNVYYG-DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKDIYDLDVDVL-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 LRRNIGVVFQDFRLLdHLTTYENVALPLRVRGRDESTYRSDVIE-LLKWVGLGERMH--VLPPILSGGEKQRAAIARALI 153
Cdd:cd03260 79 LRRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEELDERVEeALRKAALWDEVKdrLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 154 EQPRILLADEPTGNVDPQLARRLLRLLLELNRLgTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
3.85e-39 |
|
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: 132.51 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElplLRRN 80
Cdd:cd03228 1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDhLTTYENvalplrvrgrdestyrsdviellkwvglgermhvlppILSGGEKQRAAIARALIEQPRILL 160
Cdd:cd03228 78 IAYVPQDPFLFS-GTIREN-------------------------------------ILSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIaTHDLGLMDQVDaRRMVLSGGR 214
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVI-AHRLSTIRDAD-RIIVLDDGR 171
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-215 |
5.12e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 134.37 E-value: 5.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGpEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKD---RSKITRTELPLLR 78
Cdd:PRK11124 3 IQLNGINCFYGAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDFRLLDHLTTYEN-VALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 158 ILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-169 |
1.34e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.04 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRRNI 81
Cdd:COG1118 3 IEVRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD----LFTNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
....*...
gi 1426272298 162 DEPTGNVD 169
Cdd:COG1118 158 DEPFGALD 165
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-215 |
1.53e-38 |
|
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: 139.27 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGP-EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLfMSLKP----TRGLITIFGKDrskITRTELP 75
Cdd:COG1123 4 LLEVRDLSVRYPGGDvPAVDGVSLTIAPGETVALVGESGSGKSTLALAL-MGLLPhggrISGEVLLDGRD---LLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 76 LLRRNIGVVFQDFRL-LDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIE 154
Cdd:COG1123 80 LRGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 155 QPRILLADEPTGNVDPQLARR-LLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
6-216 |
6.40e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.48 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 6 NVGHRYGMG---PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLR-RNI 81
Cdd:PRK11629 10 NLCKRYQEGsvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 162 DEPTGNVDPQLARRL-LRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRLE 216
Cdd:PRK11629 170 DEPTGNLDARNADSIfQLLGELNRLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRLT 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
1.21e-37 |
|
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: 128.52 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 3 RFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLLRRNIG 82
Cdd:cd00267 1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKD---IAKLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 83 VVFQdfrlldhlttyenvalplrvrgrdestyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIEQPRILLAD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 163 EPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-170 |
3.36e-37 |
|
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: 130.46 E-value: 3.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRN-IGVVFQDFRLLDHLTT 96
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 97 YENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDP 170
Cdd:cd03294 120 LENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-171 |
7.39e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 135.29 E-value: 7.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FMslKPTRGLITIFGKDRSKITRTELpllRR 79
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLlrFY--DPTSGRILIDGVDIRDLTLESL---RR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDFRLLdHLTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAI 148
Cdd:COG1132 415 QIGVVPQDTFLF-SGTIRENIRY-----GRPDAT-DEEVEEAAKAAQAHEFIEALPdgydtVVgergvnLSGGQRQRIAI 487
|
170 180
....*....|....*....|...
gi 1426272298 149 ARALIEQPRILLADEPTGNVDPQ 171
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTE 510
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
33-215 |
9.40e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 128.36 E-value: 9.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLR-RNIGVVFQDFRLLDHLTTYENVALPLRVRGRDE 111
Cdd:PRK10584 41 LIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQSFMLIPTLNALENVELPALLRGESS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 112 STYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQL-ARRLLRLLLELNRLGTAV 190
Cdd:PRK10584 121 RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgDKIADLLFSLNREHGTTL 200
|
170 180
....*....|....*....|....*
gi 1426272298 191 VIATHDLGLMDQVDaRRMVLSGGRL 215
Cdd:PRK10584 201 ILVTHDLQLAARCD-RRLRLVNGQL 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
1.28e-36 |
|
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: 126.36 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRRNI 81
Cdd:cd03230 1 IEVRNLSKRYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKD----IKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENValplrvrgrdestyrsdviellkwvglgermhvlppILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 162 DEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-215 |
2.99e-36 |
|
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: 133.34 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRNI 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLdHLTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIAR 150
Cdd:COG4988 414 AWVPQNPYLF-AGTIRENLRL-----GRPDAS-DEELEAALEAAGLDEFVAALPdgldtPLgeggrgLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 151 ALIEQPRILLADEPTGNVDPQlARRLLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRL 215
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAE-TEAEILQALRRLAKGRTVILITHRLALLAQAD-RILVLDDGRI 549
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-215 |
3.37e-36 |
|
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: 126.72 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTelplLRRNI 81
Cdd:cd03265 1 IEVENLVKKYG-DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 162 DEPTGNVDPQLARRL-LRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03265 156 DEPTIGLDPQTRAHVwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-215 |
6.88e-36 |
|
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: 133.42 E-value: 6.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRN 80
Cdd:COG2274 474 IELENVSFRYpGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLdHLTTYENVALplrvrGRDESTYrSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIA 149
Cdd:COG2274 551 IGVVLQDVFLF-SGTIRENITL-----GDPDATD-EEIIEAARLAGLHDFIEALPmgydtVVgeggsnLSGGQRQRLAIA 623
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 150 RALIEQPRILLADEPTGNVDPQlARRLLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRL 215
Cdd:COG2274 624 RALLRNPRILILDEATSALDAE-TEAIILENLRRLLKGRTVIIIAHRLSTIRLAD-RIIVLDKGRI 687
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-215 |
1.01e-35 |
|
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: 126.31 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRN 80
Cdd:COG1120 1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---ARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVAL---PLRVRGRDEStyRSD---VIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIE 154
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALgryPHLGLFGRPS--AEDreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 155 QPRILLADEPTGNVDPQ-LARRLLRLLLELNRLGTAVVIATHDLGLM----DQVdarrMVLSGGRL 215
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAhQLEVLELLRRLARERGRTVVMVLHDLNLAaryaDRL----VLLKDGRI 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-215 |
1.16e-35 |
|
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: 125.63 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRteLP---LLRRNI 81
Cdd:cd03219 4 RGLTKRFG-GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED---ITG--LPpheIARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRG----------RDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARA 151
Cdd:cd03219 78 GRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 152 LIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-212 |
3.71e-35 |
|
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: 123.80 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 3 RFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKItrtelpllRRNIG 82
Cdd:cd03235 1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE--------RKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 83 VVFQdFRLLDH---LTTYENVALPLRVR----GRDESTYRSDVIELLKWVGLGERMHvlPPI--LSGGEKQRAAIARALI 153
Cdd:cd03235 72 YVPQ-RRSIDRdfpISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELAD--RQIgeLSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 154 EQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLG-LMDQVD-----ARRMVLSG 212
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEYFDrvlllNRTVVASG 213
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-214 |
1.29e-34 |
|
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: 122.20 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRRN 80
Cdd:COG4133 2 MLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP----IRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDEStyRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDlgLMDQVDARRMVLSGGR 214
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ--PLELAAARVLDLGDFK 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-215 |
2.44e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskitrteLPLLRRN 80
Cdd:COG1121 6 AIELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP--------PRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDH--LTTYENVALPL--------RVRGRDestyRSDVIELLKWVGLGERMHVlpPI--LSGGEKQRAAI 148
Cdd:COG1121 77 IGYVPQRAEVDWDfpITVRDVVLMGRygrrglfrRPSRAD----REAVDEALERVGLEDLADR--PIgeLSGGQQQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 149 ARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-213 |
2.46e-34 |
|
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: 121.21 E-value: 2.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 3 RFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRtelpllRRNIG 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 83 VVFQDFRllDHLTTyENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLAD 162
Cdd:cd03226 75 YVMQDVD--YQLFT-DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 163 EPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGG 213
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-215 |
7.26e-34 |
|
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: 121.18 E-value: 7.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITrteLPLLRRNI 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHlTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLPP-----------ILSGGEKQRAAIAR 150
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIRY-----GRPDAT-DEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 151 ALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVDaRRMVLSGGRL 215
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVNAD-KIIVLKDGRI 213
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-199 |
7.51e-34 |
|
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: 119.84 E-value: 7.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 11 YGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrSKITRTELPLLRRNIGVVFQDFRl 90
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEP-LDYSRKGLLERRQRVGLVFQDPD- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 lDHL---TTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGN 167
Cdd:TIGR01166 79 -DQLfaaDVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157
|
170 180 190
....*....|....*....|....*....|..
gi 1426272298 168 VDPQLARRLLRLLLELNRLGTAVVIATHDLGL 199
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGMTVVISTHDVDL 189
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-215 |
3.69e-33 |
|
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: 118.87 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElplLRRNI 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHlTTYENVALplrvrGRDESTyRSDVIELLKWVG---------------LGERMHVlppiLSGGEKQRA 146
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRL-----GRPNAT-DEEVIEAAKEAGahdfimklpngydtvLGENGGN----LSQGERQLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 147 AIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVDaRRMVLSGGRL 215
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTIKNAD-KILVLDDGKI 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-164 |
5.90e-33 |
|
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: 121.36 E-value: 5.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGK---DRSKitRTELPLLRRNIGVVFQDFRLLDHLTT 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSAR--GIFLPPHRRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 97 YENVALPLRVRGRDESTYR-SDVIELLkwvGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:COG4148 95 RGNLLYGRKRAPRAERRISfDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-214 |
8.82e-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: 117.92 E-value: 8.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVG------HRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITI---FGK-DRSKIT 70
Cdd:COG4778 4 LLEVENLSktftlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 71 -RTELPLLRRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPI-LSGGEKQRAAI 148
Cdd:COG4778 84 pREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPAtFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 149 ARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-215 |
9.79e-33 |
|
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: 116.38 E-value: 9.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRNIGVV 84
Cdd:cd03214 3 ENLSVGYG-GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 85 FQDFRLLDhlttyenvALPLRVRGRDEstyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:cd03214 79 PQALELLG--------LAHLADRPFNE--------------------------LSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 165 TGNVDP-QLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03214 125 TSHLDIaHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-215 |
1.77e-32 |
|
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: 116.84 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEI-LRDVSFHLPERS-FQFLsGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRR 79
Cdd:cd03263 1 LQIRNLTKTYKKGTKPaVDDLSLNVYKGEiFGLL-GHNGAGKTTTLKMLTGELRPTSGTAYINGYS----IRTDRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRIL 159
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 160 LADEPTGNVDPQlARRLLRLLLELNRLGTAVVIATHDlglMDQVDA---RRMVLSGGRL 215
Cdd:cd03263 156 LLDEPTSGLDPA-SRRAIWDLILEVRKGRSIILTTHS---MDEAEAlcdRIAIMSDGKL 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-170 |
2.01e-32 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.16 E-value: 2.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmgPEILRdVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrTELPLLRRN 80
Cdd:COG3840 1 MLRLDDLTYRYG--DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-----TALPPAERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170
....*....|
gi 1426272298 161 ADEPTGNVDP 170
Cdd:COG3840 153 LDEPFSALDP 162
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-215 |
5.41e-32 |
|
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: 121.80 E-value: 5.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRN 80
Cdd:COG4987 334 LELEDVSFRYpGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---RRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIA 149
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRL-----ARPDAT-DEELWAALERVGLGDWLAALPdgldtWLgeggrrLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 150 RALIEQPRILLADEPTGNVDPQlARRLLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRL 215
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAA-TEQALLADLLEALAGRTVLLITHRLAGLERMD-RILVLEDGRI 547
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-164 |
1.13e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.51 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrTELPLLRRNI 81
Cdd:PRK09452 15 VELRGISKSFD-GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-----THVPAENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
...
gi 1426272298 162 DEP 164
Cdd:PRK09452 169 DES 171
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-170 |
1.73e-31 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 114.21 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGpEILRDVSFHLPERSFQFLsGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTelplLRRNI 81
Cdd:cd03264 1 LQLENLTKRYGKK-RALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
....*....
gi 1426272298 162 DEPTGNVDP 170
Cdd:cd03264 155 DEPTAGLDP 163
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-169 |
2.21e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 115.34 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMG---PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrskitRTELPLL 77
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV------PVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRniGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170
....*....|..
gi 1426272298 158 ILLADEPTGNVD 169
Cdd:COG4525 155 FLLMDEPFGALD 166
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
16-171 |
5.34e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 116.34 E-value: 5.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElpllrRNIGVVFQDFRLLDHLT 95
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 96 TYENVALPLRVRGRDE----STYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQ 171
Cdd:PRK10851 91 VFDNIAFGLTVLPRRErpnaAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
10-216 |
2.01e-30 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 112.75 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 10 RYGMGpEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKI----------TRTELPLLRR 79
Cdd:PRK10619 14 RYGEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDFRLLDHLTTYENV-ALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPI-LSGGEKQRAAIARALIEQPR 157
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 158 ILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLE 216
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
3.78e-30 |
|
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: 109.61 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRN 80
Cdd:cd03246 1 LEVENVSFRYpGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENvalplrvrgrdestyrsdviellkwvglgermhvlppILSGGEKQRAAIARALIEQPRILL 160
Cdd:cd03246 78 VGYLPQDDELFSG-SIAEN-------------------------------------ILSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRL 215
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-196 |
4.81e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 116.75 E-value: 4.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRR-NIGVVFQDFRLLDHL 94
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRReHFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 95 TTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLAR 174
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180
....*....|....*....|..
gi 1426272298 175 RLLRLLLELNRLGTAVVIATHD 196
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTHD 203
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-169 |
2.52e-29 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 109.24 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITrteLPLLRRN 80
Cdd:cd03251 1 VEFKNVTFRYpGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIA 149
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAY-----GRPGAT-REEVEEAARAANAHEFIMELPegydtVIgergvkLSGGQRQRIAIA 150
|
170 180
....*....|....*....|
gi 1426272298 150 RALIEQPRILLADEPTGNVD 169
Cdd:cd03251 151 RALLKDPPILILDEATSALD 170
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-169 |
3.92e-29 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 109.38 E-value: 3.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLItIFGkdrskitRTELPLLRRNIGVV 84
Cdd:PRK11247 16 NAVSKRYG-ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG-------TAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 85 FQDFRLLDHLTTYENVALPLRvrgrdeSTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
....*
gi 1426272298 165 TGNVD 169
Cdd:PRK11247 161 LGALD 165
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-219 |
4.03e-29 |
|
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: 108.15 E-value: 4.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLPErSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLI----TIFGKDRSKItrtELPLLRRNIGVVFQDFRLLDHLT 95
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngTVLFDSRKKI---NLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 96 TYENVALPLRVRGRDESTYRSDviELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD-PQLAR 174
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVD--ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDrALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1426272298 175 RLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLEIYD 219
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-215 |
6.20e-29 |
|
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: 107.30 E-value: 6.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLlrRNI 81
Cdd:cd03268 1 LKTNDLTKTYG-KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS---YQKNIEAL--RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDEStyrsDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 162 DEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-215 |
8.82e-29 |
|
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: 108.20 E-value: 8.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRteLP---LL 77
Cdd:COG0411 4 LLEVRGLTKRFG-GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRD---ITG--LPphrIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVALPLRVRG---------------RDESTYRSDVIELLKWVGLGERMHVLPPILSGGE 142
Cdd:COG0411 78 RLGIARTFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 143 KQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRL-LLELNRLGTAVVIATHDLGL-MDQVDaRRMVLSGGRL 215
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELiRRLRDERGITILLIEHDMDLvMGLAD-RIVVLDFGRV 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-169 |
1.10e-28 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 110.19 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 6 NVGHRYGMGpEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrTELPLLRRNIGVVF 85
Cdd:PRK11432 11 NITKRFGSN-TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-----THRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 86 QDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLG--ERMHVlpPILSGGEKQRAAIARALIEQPRILLADE 163
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAgfEDRYV--DQISGGQQQRVALARALILKPKVLLFDE 162
|
....*.
gi 1426272298 164 PTGNVD 169
Cdd:PRK11432 163 PLSNLD 168
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-214 |
1.15e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.28 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRNI 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRllDHL---TTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRI 158
Cdd:PRK13647 82 GLVFQDPD--DQVfssTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 159 LLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
1.29e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.15 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYG-MGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLLRR 79
Cdd:PRK13632 7 MIKVENVSFSYPnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGIT---ISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQ--DFRLLDhLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:PRK13632 84 KIGIIFQnpDNQFIG-ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 158 ILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIA-THDlglMDQV---DaRRMVLSGGRL 215
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHD---MDEAilaD-KVIVFSEGKL 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
35-215 |
2.68e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 106.76 E-value: 2.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKTTLLRLLFMSLKPTRGLITI----------FGKDRSKITRtelplLRRNIGVVFQDFRLLDHLTTYENVAL-P 103
Cdd:PRK11264 36 GPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKGLIRQ-----LRQHVGFVFQNFNLFPHRTVLENIIEgP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 104 LRVRG--RDESTYRSDviELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLL 181
Cdd:PRK11264 111 VIVKGepKEEATARAR--ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIR 188
|
170 180 190
....*....|....*....|....*....|....
gi 1426272298 182 ELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK11264 189 QLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-165 |
6.28e-28 |
|
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: 105.21 E-value: 6.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGMGPeILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELP-LLRRNIGV 83
Cdd:cd03224 4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD---ITGLPPHeRARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 84 VFQDFRLLDHLTTYENVALPLRVRGRDESTYRSD-VIELLKwvGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLAD 162
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLGAYARRRAKRKARLErVYELFP--RLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
...
gi 1426272298 163 EPT 165
Cdd:cd03224 158 EPS 160
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-165 |
7.48e-28 |
|
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: 110.29 E-value: 7.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElplLRRNI 81
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS---LRAAI 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLL-DhlTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLPP-----------ILSGGEKQRAAIA 149
Cdd:COG5265 435 GIVPQDTVLFnD--TIAYNIAY-----GRPDAS-EEEVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIA 506
|
170
....*....|....*.
gi 1426272298 150 RALIEQPRILLADEPT 165
Cdd:COG5265 507 RTLLKNPPILIFDEAT 522
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-216 |
1.49e-27 |
|
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: 107.12 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFEnvgHRYGmgpEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGK---DRSKitRTELPLLR 78
Cdd:TIGR02142 3 ARFS---KRLG---DFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRK--GIFLPPEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDFRLLDHLTTYENVALPL-RVRGRDESTYRSDVIELLkwvGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:TIGR02142 75 RRIGYVFQEARLFPHLSVRGNLRYGMkRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 158 ILLADEPTGNVD-PQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLE 216
Cdd:TIGR02142 152 LLLMDEPLAALDdPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
18-215 |
1.49e-27 |
|
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: 104.11 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQF-----------LSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrTELPLLRRNIGVVFQ 86
Cdd:cd03298 3 LDKIRFSYGEQPMHFdltfaqgeitaIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-----TAAPPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 87 DFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTG 166
Cdd:cd03298 78 ENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1426272298 167 NVDPQLARRLLRLLLEL-NRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03298 158 ALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-171 |
8.49e-27 |
|
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: 103.28 E-value: 8.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSkiTRTELPLLRRN 80
Cdd:TIGR04520 1 IEVENVSFSYpESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQD---------------FRLldhlttyENVALPlrvrgRDEstYRSDVIELLKWVGLGERMHVLPPILSGGEKQR 145
Cdd:TIGR04520 79 VGMVFQNpdnqfvgatveddvaFGL-------ENLGVP-----REE--MRKRVDEALKLVGMEDFRDREPHLLSGGQKQR 144
|
170 180
....*....|....*....|....*.
gi 1426272298 146 AAIARALIEQPRILLADEPTGNVDPQ 171
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPK 170
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-215 |
1.33e-26 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 102.59 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPllrRNI 81
Cdd:TIGR03873 2 LRLSRVSWSAG-GRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARA---RRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVAL---PLRVRGRDESTYRSDVI-ELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:TIGR03873 78 ALVEQDSDTAVPLTVRDVVALgriPHRSLWAGDSPHDAAVVdRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPK 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 158 ILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:TIGR03873 158 LLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-215 |
1.38e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEI----LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTE-LPL 76
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 LRRNIGVVFQ--DFRLLDHlTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPI-LSGGEKQRAAIARALI 153
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 154 EQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-169 |
1.48e-26 |
|
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: 101.85 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPE--ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKItrtELPLLRR 79
Cdd:cd03249 1 IEFKNVSFRYPSRPDvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL---NLRWLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDFRLLDhLTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLP-----------PILSGGEKQRAAI 148
Cdd:cd03249 78 QIGLVSQEPVLFD-GTIAENIRY-----GKPDAT-DEEVEEAAKKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAI 150
|
170 180
....*....|....*....|.
gi 1426272298 149 ARALIEQPRILLADEPTGNVD 169
Cdd:cd03249 151 ARALLRNPKILLLDEATSALD 171
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-169 |
1.93e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.43 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL------FMSLKPTRGLITIFGKDrskITRTELPLLRRNIGVVFQDFRL 90
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlieiYDSKIKVDGKVLYFGKD---IFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 LDHLTTYENVALPLRVRG-RDESTYRSDVIELLKWVGLG----ERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGiKEKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
....
gi 1426272298 166 GNVD 169
Cdd:PRK14246 182 SMID 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-171 |
1.98e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.91 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FMSLKP---TRGLITIFGKDrskITRTELPLLRRNIGVVFQDFRL 90
Cdd:PRK14247 17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPearVSGEVYLDGQD---IFKMDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 LDHLTTYENVALPLR----VRGRDESTYRsdVIELLK----WVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLAD 162
Cdd:PRK14247 94 IPNLSIFENVALGLKlnrlVKSKKELQER--VRWALEkaqlWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
....*....
gi 1426272298 163 EPTGNVDPQ 171
Cdd:PRK14247 172 EPTANLDPE 180
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
17-170 |
2.20e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.54 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQDFRLLDHLTT 96
Cdd:PRK11831 22 IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNV 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 97 YENVALPLRVRGR-DESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDP 170
Cdd:PRK11831 102 FDNVAYPLREHTQlPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-165 |
2.84e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 103.27 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQD-FRLLD-HLTTY 97
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDpYASLNpRMTVG 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 98 ENVALPLRVRG-RDESTYRSDVIELLKWVGLG-ERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:COG4608 116 DIIAEPLRIHGlASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPV 185
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-170 |
2.96e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.20 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmgpeilrdvsfHLPERsFQF---------LSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskiTR 71
Cdd:PRK10771 1 MLKLTDITWLYH-----------HLPMR-FDLtvergervaILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDH---TT 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 72 TelPLLRRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARA 151
Cdd:PRK10771 66 T--PPSRRPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARC 143
|
170
....*....|....*....
gi 1426272298 152 LIEQPRILLADEPTGNVDP 170
Cdd:PRK10771 144 LVREQPILLLDEPFSALDP 162
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-170 |
3.53e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 101.27 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL-FMS-LKP---TRGLITIFGKD-RSKitRTELP 75
Cdd:COG1117 12 IEVRNLNVYYG-DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnRMNdLIPgarVEGEILLDGEDiYDP--DVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 76 LLRRNIGVVFQD---FRLldhlTTYENVALPLRVRG-RDESTYRSDVIELLKWVGLGE----RMHVLPPILSGGEKQRAA 147
Cdd:COG1117 89 ELRRRVGMVFQKpnpFPK----SIYDNVAYGLRLHGiKSKSELDEIVEESLRKAALWDevkdRLKKSALGLSGGQQQRLC 164
|
170 180
....*....|....*....|...
gi 1426272298 148 IARALIEQPRILLADEPTGNVDP 170
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDP 187
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-170 |
4.67e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 101.07 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGpEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FMSLKP---TRGLITIFGKD--RSKITRTEL 74
Cdd:PRK14267 5 IETVNLRVYYGSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEearVEGEVRLFGRNiySPDVDPIEV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 75 pllRRNIGVVFQDFRLLDHLTTYENVALPLR----VRGRDESTYRsdVIELLK----WVGLGERMHVLPPILSGGEKQRA 146
Cdd:PRK14267 84 ---RREVGMVFQYPNPFPHLTIYDNVAIGVKlnglVKSKKELDER--VEWALKkaalWDEVKDRLNDYPSNLSGGQRQRL 158
|
170 180
....*....|....*....|....
gi 1426272298 147 AIARALIEQPRILLADEPTGNVDP 170
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDP 182
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-197 |
4.96e-26 |
|
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: 104.75 E-value: 4.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRNI 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHlTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLPP-----------ILSGGEKQRAAIAR 150
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRL-----ARPDAT-DEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1426272298 151 ALIEQPRILLADEPTGNVDPqLARRLLRLLLELNRLGTAVVIATHDL 197
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDA-ETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-215 |
6.23e-26 |
|
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: 100.25 E-value: 6.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGM-GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLLRRN 80
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD---LALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENVALPlrvrgrDESTYRSDVIELLKWVGLGERMHVLP-----------PILSGGEKQRAAIA 149
Cdd:cd03252 78 VGVVLQENVLFNR-SIRDNIALA------DPGMSMERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 150 RALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVDaRRMVLSGGRL 215
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIA-HRLSTVKNAD-RIIVMEKGRI 214
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-169 |
7.83e-26 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.54 E-value: 7.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrskitRTELPLLRRn 80
Cdd:PRK11248 1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK------PVEGPGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 iGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
....*....
gi 1426272298 161 ADEPTGNVD 169
Cdd:PRK11248 152 LDEPFGALD 160
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-215 |
7.87e-26 |
|
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: 99.75 E-value: 7.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEI---LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTelplL 77
Cdd:cd03266 1 MITADALTKRFRDVKKTvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVALPLRVRG--RDESTYRSDviELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQ 155
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGlkGDELTARLE--ELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 156 PRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03266 155 PPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
5-215 |
8.19e-26 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.92 E-value: 8.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGMG--------PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPL 76
Cdd:PRK10419 7 SGLSHHYAHGglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 LRRNIGVVFQD-FRLLD-HLTTYENVALPLR-VRGRDESTYRSDVIELLKWVGLG-ERMHVLPPILSGGEKQRAAIARAL 152
Cdd:PRK10419 87 FRRDIQMVFQDsISAVNpRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 153 IEQPRILLADEPTGNVDPQL-ARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDLVLqAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-204 |
1.17e-25 |
|
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: 103.52 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTelpLLRRNI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD---SWRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHlTTYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIAR 150
Cdd:TIGR02857 399 AWVPQHPFLFAG-TIAENIRL-----ARPDAS-DAEIREALERAGLDEFVAALPqgldtPIgeggagLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 151 ALIEQPRILLADEPTGNVDPQlARRLLRLLLELNRLGTAVVIATHDLGLMDQVD 204
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAE-TEAEVLEALRALAQGRTVLLVTHRLALAALAD 524
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-215 |
3.82e-25 |
|
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: 97.85 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIfgkDRSKITRTELpllrRNIGVV 84
Cdd:TIGR03740 4 KNLSKRFG-KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF---DGHPWTRKDL----HKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 85 FQDFRLLDHLTTYENVALPLRVRGRDESTyrsdVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:TIGR03740 76 IESPPLYENLTARENLKVHTTLLGLPDSR----IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 165 TGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-170 |
4.49e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 101.26 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRN-IGVVFQDFRLLDHLTT 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 97 YENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDP 170
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-215 |
5.03e-25 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.26 E-value: 5.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRrn 80
Cdd:COG4559 1 MLEAENLSVRLG-GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 iGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALI------- 153
Cdd:COG4559 78 -AVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 154 EQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRL 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-169 |
6.23e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.96 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFH-LPERSFQfLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRN 80
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEaKPGQTVA-IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRN 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENvalpLRVrGR----DESTYR-------SDVIELlKWVGL----GERMHVLppilSGGEKQR 145
Cdd:PRK13657 411 IAVVFQDAGLFNR-SIEDN----IRV-GRpdatDEEMRAaaeraqaHDFIER-KPDGYdtvvGERGRQL----SGGERQR 479
|
170 180
....*....|....*....|....
gi 1426272298 146 AAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALD 503
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-215 |
1.77e-24 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 97.15 E-value: 1.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRrn 80
Cdd:PRK13548 2 MLEARNLSVRLG-GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 iGVVFQDFRLLDHLTTYENVAL---PLRVRGRDESTYRSDVIELLKWVGLGERMHvlpPILSGGEKQRAAIARALI---- 153
Cdd:PRK13548 79 -AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGRDY---PQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 154 --EQPRILLADEPTGNVDP-QLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLaHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-215 |
1.87e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 97.39 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYgmgPE----ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpll 77
Cdd:PRK13635 6 IRVEHISFRY---PDaatyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQ--DFRLLDhlTTYEN-VALPLRVRG--RDESTYRSDviELLKWVGLGERMHVLPPILSGGEKQRAAIARAL 152
Cdd:PRK13635 80 RRQVGMVFQnpDNQFVG--ATVQDdVAFGLENIGvpREEMVERVD--QALRQVGMEDFLNREPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 153 IEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIA-THDLGLMDQVDaRRMVLSGGRL 215
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEAAQAD-RVIVMNKGEI 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
2.05e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrsKITRTELPLLRRN 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYE-NVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRIL 159
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEqDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 160 LADEPTGNVDPQ-LARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK13652 160 VLDEPTAGLDPQgVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-170 |
2.67e-24 |
|
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: 96.31 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGL-ITIFGKDRskiTRTELPLLRR 79
Cdd:COG1119 3 LLELRNVTVRRG-GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERR---GGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDF--RLLDHLTTYENVA--------LPLRVRGRDESTyrsdVIELLKWVGLGERMHVLPPILSGGEKQRAAIA 149
Cdd:COG1119 79 RIGLVSPALqlRFPRDETVLDVVLsgffdsigLYREPTDEQRER----ARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180
....*....|....*....|.
gi 1426272298 150 RALIEQPRILLADEPTGNVDP 170
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDL 175
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-165 |
3.21e-24 |
|
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: 95.82 E-value: 3.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRteLP---LL 77
Cdd:COG0410 3 MLEVENLHAGYG-GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED---ITG--LPphrIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVALPLRVRGRdestyRSDVIELLKWVG-----LGERMHVLPPILSGGEKQRAAIARAL 152
Cdd:COG0410 77 RLGIGYVPEGRRIFPSLTVEENLLLGAYARRD-----RAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRAL 151
|
170
....*....|...
gi 1426272298 153 IEQPRILLADEPT 165
Cdd:COG0410 152 MSRPKLLLLDEPS 164
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-169 |
3.38e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.18 E-value: 3.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIfGKDRSkitrTELPLLRRNI 81
Cdd:PRK11000 4 VTLRNVTKAYG-DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRM----NDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDV---IELLKWVGLGERmhvLPPILSGGEKQRAAIARALIEQPRI 158
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDR---KPKALSGGQRQRVAIGRTLVAEPSV 154
|
170
....*....|.
gi 1426272298 159 LLADEPTGNVD 169
Cdd:PRK11000 155 FLLDEPLSNLD 165
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-215 |
7.54e-24 |
|
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: 94.58 E-value: 7.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPER--------SFQF-------LSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRNIG 82
Cdd:cd03245 5 FRNVSFSYPNQeipaldnvSLTIragekvaIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 83 VVFQDFRLLdHLTTYENVALplrvrGRDESTYRsDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIARA 151
Cdd:cd03245 82 YVPQDVTLF-YGTLRDNITL-----GAPLADDE-RILRAAELAGVTDFVNKHPngldlQIgergrgLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 152 LIEQPRILLADEPTGNVDpQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRL 215
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD-MNSEERLKERLRQLLGDKTLIIITHRPSLLDLVD-RIIVMDSGRI 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
20-219 |
9.00e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 97.21 E-value: 9.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKItrtelPLLRRNIGVVFQDFRLLDHLTTYEN 99
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV-----PPYQRPINMMFQSYALFPHMTVEQN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 100 VALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRL 179
Cdd:PRK11607 112 IAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1426272298 180 LL-ELNRLGTAVVIATHdlglmDQVDARRMvlsGGRLEIYD 219
Cdd:PRK11607 192 VVdILERVGVTCVMVTH-----DQEEAMTM---AGRIAIMN 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-215 |
1.27e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 95.14 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrSKITRTELPLLRRN 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP-IKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRllDHL---TTYENVAL-PLRVrGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQP 156
Cdd:PRK13639 80 VGIVFQNPD--DQLfapTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 157 RILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-171 |
1.33e-23 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.70 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKP---TRGLITIFGKDRskitrTELPLL 77
Cdd:COG4136 1 MLSLENLTITLG-GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-----TALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENV--ALPLRVRGRDEstyRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQ 155
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLafALPPTIGRAQR---RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170
....*....|....*.
gi 1426272298 156 PRILLADEPTGNVDPQ 171
Cdd:COG4136 152 PRALLLDEPFSKLDAA 167
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-165 |
3.46e-23 |
|
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: 96.68 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTL----LRLLfmslkPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQD-FRLLD 92
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFGSLS 376
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 93 -HLTTYENVALPLRV--RGRDESTYRSDVIELLKWVGL-GERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:COG4172 377 pRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
16-218 |
3.58e-23 |
|
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: 91.84 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKP--TRGLITIFGKDRSKITrtelplLRRNIGVVFQDFRLLDH 93
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRS------FRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 94 LTTYENVALPLRVRGrdestyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLA 173
Cdd:cd03213 97 LTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1426272298 174 RRLLRLLLELNRLGTAVVIATH-----DLGLMDQVdarrMVLSGGRLeIY 218
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHqpsseIFELFDKL----LLLSQGRV-IY 192
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-169 |
3.97e-23 |
|
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: 92.91 E-value: 3.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrsKITRtelPLLRRNigVVFQDFRLLDHLTTY 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITE---PGPDRM--VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 98 ENVALPLR--VRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:TIGR01184 73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-215 |
4.04e-23 |
|
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: 94.35 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKP---TRGLITIFGKDRSKITRTELPLLR-RNIGVVFQD-FRLLD 92
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRgREIQMIFQDpMTSLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 93 -HLTTYENVALPLRV-RGRDESTYRSDVIELLKWVGL---GERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGN 167
Cdd:COG0444 101 pVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPTTA 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 168 VDP-------------QlarrllrlllelNRLGTAVVIATHDLGLMDQVdARR-MVLSGGRL 215
Cdd:COG0444 181 LDVtiqaqilnllkdlQ------------RELGLAILFITHDLGVVAEI-ADRvAVMYAGRI 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-171 |
1.22e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 92.80 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMG----PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPL- 76
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVD---ITDKKVKLs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 -LRRNIGVVFQ--DFRLLDHlTTYENVALPLRVRGRDESTYRSDVIELLKWVGLG-ERMHVLPPI-LSGGEKQRAAIARA 151
Cdd:PRK13637 80 dIRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKDKSPFeLSGGQKRRVAIAGV 158
|
170 180
....*....|....*....|
gi 1426272298 152 LIEQPRILLADEPTGNVDPQ 171
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPK 178
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
3.79e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLItIFGKDRSKITRTELPLLRRN 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDfrlLDH----LTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQP 156
Cdd:PRK13636 84 VGMVFQD---PDNqlfsASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 157 RILLADEPTGNVDPQ-LARRLLRLLLELNRLGTAVVIATHDLGLM----DQV---DARRMVLSGGRLEIY 218
Cdd:PRK13636 161 KVLVLDEPTAGLDPMgVSEIMKLLVEMQKELGLTIIIATHDIDIVplycDNVfvmKEGRVILQGNPKEVF 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-170 |
3.91e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 90.02 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLpeRSFQFLS--GPSGAGKTTLLRLL---FMSLKPTRGLITIFGKDRSKitrtelPLLRRNIGVVFQDFRLL 91
Cdd:cd03234 22 ILNDVSLHV--ESGQVMAilGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKP------DQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 92 DHLTTYENVA----LPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGN 167
Cdd:cd03234 94 PGLTVRETLTytaiLRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
...
gi 1426272298 168 VDP 170
Cdd:cd03234 174 LDS 176
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-164 |
1.34e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.09 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGK---DRSKitRTELPLLRRNIGVVFQDFRLLDHltt 96
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLPPEKRRIGYVFQDARLFPH--- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 97 YenvalplRVRG-------RDESTYRSDVIELLkwvGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:PRK11144 91 Y-------KVRGnlrygmaKSMVAQFDKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEP 155
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
16-170 |
1.37e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.45 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FMSLKP---TRGLITIFGKDRSKiTRTELPLLRRNIGVVFQDFRL 90
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYS-PRTDTVDLRKEIGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 LDhLTTYENVALPLRVRG-RDESTYRSDVIELLK----WVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:PRK14239 98 FP-MSIYENVVYGLRLKGiKDKQVLDEAVEKSLKgasiWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPT 176
|
....*
gi 1426272298 166 GNVDP 170
Cdd:PRK14239 177 SALDP 181
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-215 |
1.75e-21 |
|
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: 91.70 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITrteLPLLRRN 80
Cdd:TIGR02203 331 VEFRNVTFRYpGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENVALplrvrGRDESTYRSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIA 149
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPlgldtPIgengvlLSGGQRQRLAIA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 150 RALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVDaRRMVLSGGRL 215
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA-HRLSTIEKAD-RIVVMDDGRI 545
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-170 |
1.96e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 88.55 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLpeRSFQF--LSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRteLPLLR 78
Cdd:COG1137 3 TLEAENLVKSYG-KRTVVKDVSLEV--NQGEIvgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGED---ITH--LPMHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 R---NIGVVFQD---FRlldHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARAL 152
Cdd:COG1137 75 RarlGIGYLPQEasiFR---KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|....*...
gi 1426272298 153 IEQPRILLADEPTGNVDP 170
Cdd:COG1137 152 ATNPKFILLDEPFAGVDP 169
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-169 |
2.20e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 88.23 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElplLRRN 80
Cdd:PRK10247 7 LLQLQNVGYLAG-DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENVALPLRVRGR--DESTYRSDvielLKWVGLGERMhVLPPI--LSGGEKQRAAIARALIEQP 156
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIFPWQIRNQqpDPAIFLDD----LERFALPDTI-LTKNIaeLSGGEKQRISLIRNLQFMP 156
|
170
....*....|...
gi 1426272298 157 RILLADEPTGNVD 169
Cdd:PRK10247 157 KVLLLDEITSALD 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-215 |
2.33e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.40 E-value: 2.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRY-----GMgPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITI-FGKDRSKITRTEl 74
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGV-VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKPG- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 75 PLLR----RNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIeLLKWVGLGER-----MHVLPPILSGGEKQR 145
Cdd:TIGR03269 357 PDGRgrakRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVI-TLKMVGFDEEkaeeiLDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 146 AAIARALIEQPRILLADEPTGNVDP-QLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPiTKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-171 |
2.44e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 89.31 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEI----LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITR-TELPL 76
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerraLYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 LRRNIGVVFQ--DFRLLDHlTTYENVAL-PLRVrGRDESTYRSDVIELLKWVGLGERMHVLPPI-LSGGEKQRAAIARAL 152
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVL 160
|
170
....*....|....*....
gi 1426272298 153 IEQPRILLADEPTGNVDPQ 171
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPK 179
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-219 |
4.58e-21 |
|
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: 87.39 E-value: 4.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFG----KDRSKitrtelplLRRNIGVVF-QDFRL 90
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwKRRKK--------FLRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 LDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD- 169
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDv 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1426272298 170 PQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLeIYD 219
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL-LYD 235
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-169 |
5.19e-21 |
|
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: 90.57 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELpllRRNI 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHlTTYENVALplrvrGRDESTYRSDVIELLKWV-----------GLGERMHVLPPILSGGEKQRAAIAR 150
Cdd:TIGR01193 551 NYLPQEPYIFSG-SILENLLL-----GAKENVSQDEIWAACEIAeikddienmplGYQTELSEEGSSISGGQKQRIALAR 624
|
170
....*....|....*....
gi 1426272298 151 ALIEQPRILLADEPTGNVD 169
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLD 643
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
5.38e-21 |
|
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: 87.14 E-value: 5.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPE--ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrsKITRTELPLLRR 79
Cdd:cd03248 12 VKFQNVTFAYPTRPDtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGK---PISQYEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDFRLLDHlTTYENVALPL------RVRGRDESTYRSDVIELLK---WVGLGERmhvlPPILSGGEKQRAAIAR 150
Cdd:cd03248 89 KVSLVGQEPVLFAR-SLQDNIAYGLqscsfeCVKEAAQKAHAHSFISELAsgyDTEVGEK----GSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 151 ALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVDaRRMVLSGGRL 215
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA-HRLSTVERAD-QILVLDGGRI 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-170 |
8.33e-21 |
|
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: 86.83 E-value: 8.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRteLPLLRR-- 79
Cdd:cd03218 1 LRAENLSKRYG-KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQD---ITK--LPMHKRar 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 -NIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRI 158
Cdd:cd03218 75 lGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170
....*....|..
gi 1426272298 159 LLADEPTGNVDP 170
Cdd:cd03218 155 LLLDEPFAGVDP 166
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-216 |
8.68e-21 |
|
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: 89.81 E-value: 8.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElplLRRN 80
Cdd:COG4618 331 LSVENLTVVPpGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREE---LGRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENVAlplRVRGRDestyRSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIA 149
Cdd:COG4618 408 IGYLPQDVELFDG-TIAENIA---RFGDAD----PEKVVAAAKLAGVHEMILRLPdgydtRIgeggarLSGGQRQRIGLA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 150 RALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRLE 216
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVD-KLLVLRDGRVQ 545
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-218 |
9.86e-21 |
|
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: 86.18 E-value: 9.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNI 81
Cdd:cd03269 1 LEVENVTKRFG-RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVvFQDFRLLDHLTTYEnvalplRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03269 80 GL-YPKMKVIDQLVYLA------QLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 162 DEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLEIY 218
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-203 |
1.05e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYG----MGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRT-ELP 75
Cdd:PRK13643 1 MIKFEKVNYTYQpnspFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 76 LLRRNIGVVFQ--DFRLLDHlTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPI-LSGGEKQRAAIARAL 152
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 153 IEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHdlgLMDQV 203
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH---LMDDV 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-171 |
1.25e-20 |
|
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: 89.48 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FMSLKPTRGLI-------------------- 59
Cdd:TIGR03269 1 IEVKNLTKKFD-GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 60 ----------TIFGKDRSKITRTELPLLRRNIGVVFQ-DFRLLDHLTTYENV--ALPLRVRGRDESTYRSdvIELLKWVG 126
Cdd:TIGR03269 80 epcpvcggtlEPEEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVleALEEIGYEGKEAVGRA--VDLIEMVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1426272298 127 LGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQ 171
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQ 202
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
1.48e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 87.45 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEI----LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPL- 76
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 --------------------LRRNIGVVFQ--DFRLLDHlTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVL 134
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 135 PPI-LSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGG 213
Cdd:PRK13651 162 SPFeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
....*.
gi 1426272298 214 RLeIYD 219
Cdd:PRK13651 242 KI-IKD 246
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-214 |
2.00e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.58 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRtelpLLRRNI 81
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARAR----LARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1426272298 162 DEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-170 |
2.56e-20 |
|
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: 85.40 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKitrteLPLLRR---NI 81
Cdd:TIGR04406 5 ENLIKSYK-KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITH-----LPMHERarlGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIE-LLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:TIGR04406 79 GYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEaLLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFIL 158
|
170
....*....|
gi 1426272298 161 ADEPTGNVDP 170
Cdd:TIGR04406 159 LDEPFAGVDP 168
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-216 |
3.55e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.94 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPE--ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrsKITRTELPLLR 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQ--DFRLLDhLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQP 156
Cdd:PRK13650 81 HKIGMVFQnpDNQFVG-ATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1426272298 157 RILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIA-THDLglmDQV--DARRMVLSGGRLE 216
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISiTHDL---DEValSDRVLVMKNGQVE 219
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-219 |
4.58e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.82 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElpllrRN 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 161 ADEPTGNVDP-------------QlarrllrlllelNRLGTAVVIATHdlglmDQVDA-----RRMVLSGGR-------L 215
Cdd:PRK11650 158 FDEPLSNLDAklrvqmrleiqrlH------------RRLKTTSLYVTH-----DQVEAmtladRVVVMNGGVaeqigtpV 220
|
....
gi 1426272298 216 EIYD 219
Cdd:PRK11650 221 EVYE 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
11-170 |
5.52e-20 |
|
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: 84.50 E-value: 5.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 11 YGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELplLRRNIGVVFQDFRL 90
Cdd:TIGR03410 10 YG-QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER--ARAGIAYVPQGREI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 LDHLTTYENVALPLRVRGRDESTYRSDVIEL---LKwvglgERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGN 167
Cdd:TIGR03410 87 FPRLTVEENLLTGLAALPRRSRKIPDEIYELfpvLK-----EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEG 161
|
...
gi 1426272298 168 VDP 170
Cdd:TIGR03410 162 IQP 164
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-215 |
6.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.04 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRteLPLLRRN 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQD------FRLLDHLTTY--ENVALP-LRVRGRdestyrsdVIELLKWVGLGERMHVLPPILSGGEKQRAAIARA 151
Cdd:PRK13644 79 VGIVFQNpetqfvGRTVEEDLAFgpENLCLPpIEIRKR--------VDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 152 LIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDaRRMVLSGGRL 215
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDAD-RIIVMDRGKI 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-218 |
7.86e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.18 E-value: 7.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEI----LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKD-RSKITRTELPL 76
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 LRRNIGVVFQ--DFRLLDHlTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPI-LSGGEKQRAAIARALI 153
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFeLSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 154 EQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHdlgLMDQV----------DARRMVLSGGRLEIY 218
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH---LMDDVanyadfvyvlEKGKLVLSGKPKDIF 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-169 |
7.94e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 85.79 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLpERSfQFLS--GPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQD-FRLLDHL 94
Cdd:PRK11308 31 LDGVSFTL-ERG-KTLAvvGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpYGSLNPR 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 95 TTYENV-ALPLRVRGR-DESTYRSDVIELLKWVGL-GERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK11308 109 KKVGQIlEEPLLINTSlSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-215 |
8.93e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.43 E-value: 8.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPllrRNIGVVFQDFRL---LDH 93
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RRVASVPQDTSLsfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 94 LTTYENVALPLRVR-GRDESTYRSDVIELLKWVGLGErmHVLPPI--LSGGEKQRAAIARALIEQPRILLADEPTGNVDP 170
Cdd:PRK09536 95 RQVVEMGRTPHRSRfDTWTETDRAAVERAMERTGVAQ--FADRPVtsLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1426272298 171 QLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK09536 173 NHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-169 |
1.63e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 86.31 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTelpLLRRNI 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS---VLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHlTTYENVALplrvrGRDESTYRsdVIELLKWVGLGERMHVLPP-----------ILSGGEKQRAAIAR 150
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVTL-----GRDISEEQ--VWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALAR 489
|
170
....*....|....*....
gi 1426272298 151 ALIEQPRILLADEPTGNVD 169
Cdd:PRK10790 490 VLVQTPQILILDEATANID 508
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-214 |
2.11e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.47 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHL-PERSFQFLsGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRRN 80
Cdd:PRK13537 8 IDFRNVEKRYG-DKLVVDGLSFHVqRGECFGLL-GPNGAGKTTTLRMLLGLTHPDAGSISLCGEP----VPSRARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:PRK13537 82 VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-219 |
3.74e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.12 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 4 FENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIfgkdRSKITrtelpllrrnIGV 83
Cdd:COG0488 1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----PKGLR----------IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 84 VFQDFRLLDHLTTYENVALPLRVRGR--------------------------------DESTYRSDVIELLKWVGLGERM 131
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDAELRAleaeleeleaklaepdedlerlaelqeefealGGWEAEARAEEILSGLGFPEED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 132 HVLPP-ILSGGEKQRAAIARALIEQPRILLADEPTGNVD--------------PqlarrllrlllelnrlGTAVVIaTHD 196
Cdd:COG0488 146 LDRPVsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDlesiewleeflknyP----------------GTVLVV-SHD 208
|
250 260
....*....|....*....|....
gi 1426272298 197 LGLMDQVdARRMV-LSGGRLEIYD 219
Cdd:COG0488 209 RYFLDRV-ATRILeLDRGKLTLYP 231
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
4.21e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 82.88 E-value: 4.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGliTIFGKDrSKITRTELPLLRR 79
Cdd:PRK13648 7 IIVFKNVSFQYqSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNN-QAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQD---------------FRLLDHLTTYENValplrvrgrdestyRSDVIELLKWVGLGERMHVLPPILSGGEKQ 144
Cdd:PRK13648 84 HIGIVFQNpdnqfvgsivkydvaFGLENHAVPYDEM--------------HRRVSEALKQVDMLERADYEPNALSGGQKQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 145 RAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIA-THDL 197
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISiTHDL 203
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-215 |
4.41e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPeILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGK--DRSKitrTELPLLR 78
Cdd:PRK13638 1 MLATSDLWFRYQDEP-VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSK---RGLLALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDfrlLDHLTTY----ENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIE 154
Cdd:PRK13638 77 QQVATVFQD---PEQQIFYtdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 155 QPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-214 |
4.47e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 82.67 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGmgPEI-LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELP------LL 77
Cdd:PRK11701 10 RGLTKLYG--PRKgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSeaerrrLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFR--LLDHLTTYENVALPLRVRG-RDESTYRSDVIELLKWVGLG-ERMHVLPPILSGGEKQRAAIARALI 153
Cdd:PRK11701 88 RTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGaRHYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 154 EQPRILLADEPTGNVDPQLARRLL-RLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLdLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-169 |
4.60e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.76 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 7 VGHRYgmgpeILRDVSFHLPERSFQFLSGPSGAGKTT----LLRLLfmslkPTRGLITIFGKDRSKITRTELPLLRRNIG 82
Cdd:PRK15134 296 VDHNV-----VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 83 VVFQD--FRLLDHLTTYENVALPLRVRGRDESTYRSD--VIELLKWVGLG-ERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:PRK15134 366 VVFQDpnSSLNPRLNVLQIIEEGLRVHQPTLSAAQREqqVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPS 445
|
170
....*....|..
gi 1426272298 158 ILLADEPTGNVD 169
Cdd:PRK15134 446 LIILDEPTSSLD 457
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-170 |
8.80e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 8.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMgPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELP-LLRR 79
Cdd:PRK11614 5 MLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD---ITDWQTAkIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTYR-SDVIELLKwvGLGERMHVLPPILSGGEKQRAAIARALIEQPRI 158
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERiKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170
....*....|..
gi 1426272298 159 LLADEPTGNVDP 170
Cdd:PRK11614 159 LLLDEPSLGLAP 170
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
18-171 |
1.09e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 83.54 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrskitrtELPL------LRRNIGVVFQDFRLL 91
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK--------PVRIrsprdaIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 92 DHLTTYENVAL---PLRVRGRDESTYRSDVIELLKWVGLgermHVLP--PI--LSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:COG3845 93 PNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGL----DVDPdaKVedLSVGEQQRVEILKALYRGARILILDEP 168
|
....*..
gi 1426272298 165 TGNVDPQ 171
Cdd:COG3845 169 TAVLTPQ 175
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-219 |
1.29e-18 |
|
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: 80.53 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMG-PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKItrtELPLLRRN 80
Cdd:cd03369 7 IEVENLSVRYAPDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENValplrvrgrDESTYRSD--VIELLKWVGLGERmhvlppiLSGGEKQRAAIARALIEQPRI 158
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNL---------DPFDEYSDeeIYGALRVSEGGLN-------LSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 159 LLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVDaRRMVLSGGRLEIYD 219
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIA-HRLRTIIDYD-KILVMDAGEVKEYD 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-171 |
1.61e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 81.29 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRteLPLLRR--NIGVVFQDFRL--LD 92
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD---VTK--LPEYKRakYIGRVFQDPMMgtAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 93 HLTTYENVALPLRvRGRD-------ESTYRSDVIELLKWVGLG--ERMHVLPPILSGGEKQRAAIARALIEQPRILLADE 163
Cdd:COG1101 96 SMTIEENLALAYR-RGKRrglrrglTKKRRELFRELLATLGLGleNRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLDE 174
|
....*...
gi 1426272298 164 PTGNVDPQ 171
Cdd:COG1101 175 HTAALDPK 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-210 |
2.00e-18 |
|
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: 79.71 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITrtelPLLRRNIGVVFQDFRLLDH 93
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQR----DEPHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 94 LTTYENvalpLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLA 173
Cdd:TIGR01189 88 LSALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 1426272298 174 RRLLRLLLELNRLGTAVVIATH-DLGLmdqVDARRMVL 210
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTHqDLGL---VEARELRL 198
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
33-171 |
2.26e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 80.83 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLfmslkptRGLITifgKDRSKITRTEL--------PLLRRNI-------GVVFQDFRLLDHLTTY 97
Cdd:PRK09984 35 LLGPSGSGKSTLLRHL-------SGLIT---GDKSAGSHIELlgrtvqreGRLARDIrksrantGYIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 98 ENV---ALPLRVRGRDESTY-----RSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK09984 105 ENVligALGSTPFWRTCFSWftreqKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLD 184
|
..
gi 1426272298 170 PQ 171
Cdd:PRK09984 185 PE 186
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-171 |
2.52e-18 |
|
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: 79.85 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMG-PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKItrtELPLLRRN 80
Cdd:cd03244 3 IEFKNVSLRYRPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENVAlPLrvrgrDESTyRSDVIELLKWVGLGERMHVLPPIL-----------SGGEKQRAAIA 149
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLD-PF-----GEYS-DEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180
....*....|....*....|..
gi 1426272298 150 RALIEQPRILLADEPTGNVDPQ 171
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPE 173
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-165 |
2.56e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.37 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELplLRRN 80
Cdd:COG1129 4 LLEMRGISKSFG-GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDA--QAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVAL--PLRVRGR-DESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPR 157
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLgrEPRRGGLiDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160
|
....*...
gi 1426272298 158 ILLADEPT 165
Cdd:COG1129 161 VLILDEPT 168
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-213 |
3.77e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.14 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITR---TELpll 77
Cdd:PRK09700 5 YISMAGIGKSFG-PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklaAQL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 rrNIGVVFQDFRLLDHLTTYENV---ALPLR----VRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIAR 150
Cdd:PRK09700 81 --GIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1426272298 151 ALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGG 213
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-199 |
3.81e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskITRTELPLLRRNIGvvFQDFrLLDH 93
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYLG--HRNA-MKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 94 LTTYENVALPLRVRGRDEStyrsDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLA 173
Cdd:PRK13539 88 LTVAENLEFWAAFLGGEEL----DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....*..
gi 1426272298 174 RRLLRLLLELNRLGTAVVIATH-DLGL 199
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIAATHiPLGL 190
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-215 |
7.12e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.84 E-value: 7.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPE-ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKP---TRGLITIFGkdrskITRTELPL- 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG-----ITLTAKTVw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 -LRRNIGVVFQ--DFRLLDhLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALI 153
Cdd:PRK13640 81 dIREKVGIVFQnpDNQFVG-ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 154 EQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIA-THDL---GLMDQVdarrMVLSGGRL 215
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISiTHDIdeaNMADQV----LVLDDGKL 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
35-215 |
7.65e-18 |
|
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: 81.60 E-value: 7.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDESTY 114
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKD----IETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEA 1038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 115 RSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPqLARRLLRLLLELNRLGTAVVIAT 194
Cdd:TIGR01257 1039 QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP-YSRRSIWDLLLKYRSGRTIIMST 1117
|
170 180
....*....|....*....|.
gi 1426272298 195 HDLGLMDQVDARRMVLSGGRL 215
Cdd:TIGR01257 1118 HHMDEADLLGDRIAIISQGRL 1138
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
9.52e-18 |
|
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: 77.08 E-value: 9.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELplLRRNI 81
Cdd:cd03216 1 LELRGITKRFG-GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA--RRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQdfrlldhlttyenvalplrvrgrdestyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03216 78 AMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 162 DEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-199 |
1.17e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.27 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 10 RYGMGPeILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrtelpllrrnIGVVFQDFR 89
Cdd:NF040873 1 GYGGRP-VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR--------------VAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 90 LLDHL--TTYENVAL-------PLRVRGRDEstyRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:NF040873 66 VPDSLplTVRDLVAMgrwarrgLWRRLTRDD---RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190
....*....|....*....|....*....|....*....
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGL 199
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-219 |
1.35e-17 |
|
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: 77.96 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrtelPLLRRNIGvvfqdfrLLDHLTT 96
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS--------SLLGLGGG-------FNPELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 97 YENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVlpPI--LSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLAR 174
Cdd:cd03220 102 RENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL--PVktYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1426272298 175 RLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLEIYD 219
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-170 |
1.92e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 78.29 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPEIlRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FMSLKPT---RGLITIFGKD--RSKITRTEL 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNlyAPDVDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 75 pllRRNIGVVFQDFRLLDHlTTYENVALPLRVRGrdestYRSDVIELLK--------WVGLGERMHVLPPILSGGEKQRA 146
Cdd:PRK14243 90 ---RRRIGMVFQKPNPFPK-SIYDNIAYGARING-----YKGDMDELVErslrqaalWDEVKDKLKQSGLSLSGGQQQRL 160
|
170 180
....*....|....*....|....
gi 1426272298 147 AIARALIEQPRILLADEPTGNVDP 170
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDP 184
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-170 |
4.79e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.44 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPE-----ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELp 75
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 76 lLRRNIGVVFQ--DFRLLDHLTTyENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALI 153
Cdd:PRK13633 83 -IRNKAGMVFQnpDNQIVATIVE-EDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170
....*....|....*..
gi 1426272298 154 EQPRILLADEPTGNVDP 170
Cdd:PRK13633 161 MRPECIIFDEPTAMLDP 177
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-170 |
5.79e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 77.00 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMgPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL-----FMSLKPTRGLITIFGKDRSKiTRTELPL 76
Cdd:PRK14258 8 IKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIYE-RRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 LRRNIGVVFQDFRLLDhLTTYENVALPLRVRGRDESTYRSDVIE-LLK----WVGLGERMHVLPPILSGGEKQRAAIARA 151
Cdd:PRK14258 86 LRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVEsALKdadlWDEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170
....*....|....*....
gi 1426272298 152 LIEQPRILLADEPTGNVDP 170
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDP 183
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-215 |
7.49e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 7.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYgMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKitrteLPL---LRRNI 81
Cdd:PRK10895 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-----LPLharARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVALPLRVRGRDESTYRSD-VIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILL 160
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-215 |
1.48e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 21 VSFHLPERSFQFLSGPSGAGKTTLLRLL--FMslkPTRGLITIFGKDRSKItrtELPLLRRNIGVVFQDFRLLdHLTTYE 98
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALlgFL---PYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLP-HGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 99 NVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLP-----PI------LSGGEKQRAAIARALIEQPRILLADEPTGN 167
Cdd:PRK11174 442 NVLL-----GNPDAS-DEQLQQALENAWVSEFLPLLPqgldtPIgdqaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 168 VDPQLARRLLRLLLELNRLGTAVVIaTH---DLGLMDQVdarrMVLSGGRL 215
Cdd:PRK11174 516 LDAHSEQLVMQALNAASRRQTTLMV-THqleDLAQWDQI----WVMQDGQI 561
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-216 |
1.49e-16 |
|
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: 74.27 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPE-ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTelplLRRN 80
Cdd:cd03247 1 LSINNVSFSYPEQEQqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENvalplrvrgrdestyrsdviellkwvgLGERmhvlppiLSGGEKQRAAIARALIEQPRILL 160
Cdd:cd03247 77 ISVLNQRPYLFDT-TLRNN---------------------------LGRR-------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 161 ADEPTGNVDPQLARRLLRLLLELNRLGTaVVIATHDLGLMDQVDaRRMVLSGGRLE 216
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKT-LIWITHHLTGIEHMD-KILFLENGKII 175
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
16-170 |
1.75e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 75.64 E-value: 1.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERsfQFLS--GPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrsKITRTELPLLRRNIGVVFQD--FRLL 91
Cdd:COG4167 27 EAVKPVSFTLEAG--QTLAiiGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGDYKYRCKHIRMIFQDpnTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 92 DHLTTYENVALPLRVRGR-DESTYRSDVIELLKWVGL-GERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:COG4167 102 PRLNIGQILEEPLRLNTDlTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
|
.
gi 1426272298 170 P 170
Cdd:COG4167 182 M 182
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-165 |
1.90e-16 |
|
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: 77.03 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKT----TLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLR-RNIGVVFQD-FR 89
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQEpMT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 90 LLDHLTTYEN-VALPLRV-RGRDESTYRSDVIELLKWVGLGE---RMHVLPPILSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:COG4172 104 SLNPLHTIGKqIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEP 183
|
.
gi 1426272298 165 T 165
Cdd:COG4172 184 T 184
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-215 |
3.76e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.13 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL-FMSLKPT----RGLITIFGkdRSKITRTELPLLRRNIGVVFQDF 88
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnRMNDKVSgyrySGDVLLGG--RSIFNYRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 89 RLLDhLTTYENVALPLRV-----RGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADE 163
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAhklvpRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 164 PTGNVDPQLARRLLRLLLELNRLGTaVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLT-VIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
33-215 |
5.09e-16 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 73.73 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKitrtelplLRRNIGVVFQDFRLL-DHLTTYENVAL--------P 103
Cdd:TIGR03771 11 LLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGK--------GWRHIGYVPQRHEFAwDFPISVAHTVMsgrtghigW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 104 LRVRGRDESTYRSDVIELLKWVGLGERmhvlpPI--LSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLL 181
Cdd:TIGR03771 83 LRRPCVADFAAVRDALRRVGLTELADR-----PVgeLSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFI 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1426272298 182 ELNRLGTAVVIATHDLG-LMDQVDarRMVLSGGRL 215
Cdd:TIGR03771 158 ELAGAGTAILMTTHDLAqAMATCD--RVVLLNGRV 190
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-165 |
8.38e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 74.35 E-value: 8.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFG----KDRSKitrtelplLRRNIGVVF-QDFRLLD 92
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRRKE--------FARRIGVVFgQRSQLWW 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 93 HLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVlpPI--LSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:COG4586 110 DLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT--PVrqLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-170 |
1.20e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 73.19 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLL----RLlfmsLKPTRGLITIFGKDrskITRTELPL 76
Cdd:COG4604 1 MIEIKNVSKRYG-GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLsmisRL----LPPDSGEVLVDGLD---VATTPSRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 77 LRRNIGVVFQDfrlldhlttyENVALPLRVR-----GR-----------DEsTYRSDVIELLKWVGLGERmhvlpPI--L 138
Cdd:COG4604 73 LAKRLAILRQE----------NHINSRLTVRelvafGRfpyskgrltaeDR-EIIDEAIAYLDLEDLADR-----YLdeL 136
|
170 180 190
....*....|....*....|....*....|..
gi 1426272298 139 SGGEKQRAAIARALIEQPRILLADEPTGNVDP 170
Cdd:COG4604 137 SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
1.38e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.72 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLP--ERSFqfLSGPSGAGKTTLLRLLFMSLKPTRGLITIfGKdrskitrtelpllR 78
Cdd:COG0488 315 VLELEGLSKSYG-DKTLLDDLSLRIDrgDRIG--LIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-------------T 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDFRLLD-HLTTYENVAlplrvRGRDESTyRSDVIELLKWVGL-GERmhVLPPI--LSGGEKQRAAIARALIE 154
Cdd:COG0488 378 VKIGYFDQHQEELDpDKTVLDELR-----DGAPGGT-EQEVRGYLGRFLFsGDD--AFKPVgvLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 155 QPRILLADEPTGNVD--------------PqlarrllrlllelnrlGTAVVIaTHDLGLMDQVDARRMVLSGGRLEIYD 219
Cdd:COG0488 450 PPNVLLLDEPTNHLDietlealeealddfP----------------GTVLLV-SHDRYFLDRVATRILEFEDGGVREYP 511
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-169 |
2.75e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQD--FRLLDHLTTY 97
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 98 ENVALPLRVR----GRDEstYRSDVIELLKWVGLGERM-HVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK15079 119 EIIAEPLRTYhpklSRQE--VKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-169 |
3.07e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.07 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMgPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGlitifgkdrsKITRTelPLLRrn 80
Cdd:PRK09544 4 LVSLENVSVSFGQ-RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRN--GKLR-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLldhlttyeNVALPLRV----RGRdESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQP 156
Cdd:PRK09544 69 IGYVPQKLYL--------DTTLPLTVnrflRLR-PGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170
....*....|...
gi 1426272298 157 RILLADEPTGNVD 169
Cdd:PRK09544 140 QLLVLDEPTQGVD 152
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-216 |
5.55e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.22 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPE--ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKItrtELPLLRR 79
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDFRLLDHlTTYENVALPLRVRGRDESTYRSDVIELLKWVG---------LGERMHvlppILSGGEKQRAAIAR 150
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMefpngydteVGEKGS----QLSGGQKQRIAIAR 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 151 ALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRlgTAVVIAtHDLGLMDQVDaRRMVLSGGRLE 216
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQESRSRASR--TVLLIA-HRLSTVERAD-QILVLKKGSVV 692
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-214 |
9.91e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.39 E-value: 9.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL-FMSLKPTR--GLITIFGKdrskitRTELPLLRRNIGVVFQDFRLLD 92
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALaFRSPKGVKgsGSVLLNGM------PIDAKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 93 HLTTYENVALPLRVR-GRD--ESTYRSDVIELLKWVGLGERMHVLPPI------LSGGEKQRAAIARALIEQPRILLADE 163
Cdd:TIGR00955 113 TLTVREHLMFQAHLRmPRRvtKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 164 PTGNVDPQLARRLLRLLLELNRLGTAVVIATHD-----LGLMDQVdarrMVLSGGR 214
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQpsselFELFDKI----ILMAEGR 244
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-215 |
1.33e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 71.03 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITI----FGKDRSKITRTELPL---------LRRNIGV 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITNPYskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 84 VFQ--DFRLLDhlTTYEN------VALplrvrGRDESTYRSDVIELLKWVGLGER-MHVLPPILSGGEKQRAAIARALIE 154
Cdd:PRK13631 121 VFQfpEYQLFK--DTIEKdimfgpVAL-----GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 155 QPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-217 |
1.76e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 70.52 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPE-RSFQFLsGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSkitrtelPLLRR 79
Cdd:COG4152 1 MLELKGLTKRFG-DKTAVDDVSFTVPKgEIFGLL-GPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVV------FQDFRLLDHLttyenVALpLRVRGRDESTYRSDVIELLKWVGLGERMHVlpPI--LSGGEKQRAAIARA 151
Cdd:COG4152 72 RIGYLpeerglYPKMKVGEQL-----VYL-ARLKGLSKAEAKRRADEWLERLGLGDRANK--KVeeLSKGNQQKVQLIAA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 152 LIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDlglMDQVD---------AR-RMVLSGGRLEI 217
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQ---MELVEelcdriviiNKgRKVLSGSVDEI 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-203 |
2.49e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.19 E-value: 2.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGP----EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGL-----ITIFGKDRSKITRT 72
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTvtvddITITHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 73 elplLRRNIGVVFQ--DFRLLDHLTTYENVALPlRVRGRDESTYRSDVIELLKWVGLGERMHVLPPI-LSGGEKQRAAIA 149
Cdd:PRK13646 83 ----VRKRIGMVFQfpESQLFEDTVEREIIFGP-KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFqMSGGQMRKIAIV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 150 RALIEQPRILLADEPTGNVDPQLARR-LLRLLLELNRLGTAVVIATHDlglMDQV 203
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQvMRLLKSLQTDENKTIILVSHD---MNEV 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-169 |
3.85e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGP--EILRDVSFHLPE-RSFQFLsGPSGAGKTTLLRLLFMSLKPTRGLITIfgKDRSKITRTELPLLR 78
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdvEIYKDLNFTLTEgKTYAFV-GESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDFRLL---------------------------DHLTTYENVALP-----------------------LRVRG 108
Cdd:PTZ00265 460 SKIGVVSQDPLLFsnsiknnikyslyslkdlealsnyyneDGNDSQENKNKRnscrakcagdlndmsnttdsnelIEMRK 539
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 109 RDESTYRSDVIELLKWVGLGERMHVLP-----------PILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PTZ00265 540 NYQTIKDSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-215 |
4.33e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPeILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPllrRN 80
Cdd:PRK11231 2 TLRTENLTVGYGTKR-ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQdfrlldHLTTYENVA------------LPL--RVRGRDESTYRSdVIELLKWVGLGERmhvlpPI--LSGGEKQ 144
Cdd:PRK11231 78 LALLPQ------HHLTPEGITvrelvaygrspwLSLwgRLSAEDNARVNQ-AMEQTRINHLADR-----RLtdLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 145 RAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLglmDQvdARR-----MVLSGGRL 215
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDL---NQ--ASRycdhlVVLANGHV 216
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-206 |
5.23e-14 |
|
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: 67.90 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 21 VSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKitrtELPLLRRNIGVVFQDFRLLDHLTTYENv 100
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDF----QRDSIARGLLYLGHAPGIKTTLSVLEN- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 101 alpLRVRGRDESTyrSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLL 180
Cdd:cd03231 94 ---LRFWHADHSD--EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170 180
....*....|....*....|....*..
gi 1426272298 181 LELNRLGTAVVIATH-DLGLMDQVDAR 206
Cdd:cd03231 169 AGHCARGGMVVLTTHqDLGLSEAGARE 195
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-215 |
5.41e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.27 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQD-FRLLD-HLTTY 97
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpYASLDpRQTVG 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 98 ENVALPLRVRGR-DESTYRSDVIELLKWVGL-GERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARR 175
Cdd:PRK10261 422 DSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1426272298 176 LLRLLL-ELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK10261 502 IINLLLdLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-213 |
6.81e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.66 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIfgkDRSKITRTELPLLRRNIGVVFQD-------- 87
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI---DDHPLHFGDYSYRSQRIRMIFQDpstslnpr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 88 ---FRLLDhlttyenvaLPLRVRGRDESTYRSD-VIELLKWVGL-GERMHVLPPILSGGEKQRAAIARALIEQPRILLAD 162
Cdd:PRK15112 104 qriSQILD---------FPLRLNTDLEPEQREKqIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 163 EPTGNVD-PQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGG 213
Cdd:PRK15112 175 EALASLDmSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQG 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-215 |
8.27e-14 |
|
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: 66.69 E-value: 8.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELplLRRNIGVVFQDFR---LLDHL 94
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--IRAGIAYVPEDRKregLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 95 TTYENVALPLrvrgrdestyrsdviellkwvglgermhvlppILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLAR 174
Cdd:cd03215 94 SVAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1426272298 175 RLLRLLLELNRLGTAVVIATHDL----GLMDQVdarrMVLSGGRL 215
Cdd:cd03215 142 EIYRLIRELADAGKAVLLISSELdellGLCDRI----LVMYEGRI 182
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-203 |
9.72e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.50 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGP----EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLlfmslkpTRGLI------TIFG--KDRSKI 69
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQL-------TNGLIisetgqTIVGdyAIPANL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 70 TR-TELPLLRRNIGVVFQ--DFRLLDHlTTYENVAL-PLRVRGRDESTYRSdVIELLKWVGLGERMHVLPPI-LSGGEKQ 144
Cdd:PRK13645 80 KKiKEVKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVNLGENKQEAYKK-VPELLKLVQLPEDYVKRSPFeLSGGQKR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 145 RAAIARALIEQPRILLADEPTGNVDPQ-LARRLLRLLLELNRLGTAVVIATHDlglMDQV 203
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKgEEDFINLFERLNKEYKKRIIMVTHN---MDQV 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-215 |
1.33e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.08 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPE-ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElplLRRN 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHlTTYENVALPLRvRGRDEStyrsdVIELLKWVGLGERMHVLPPI----------LSGGEKQRAAIAR 150
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLAAP-NASDEA-----LIEVLQQVGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIAR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 151 ALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIaTHDLGLMDQVDaRRMVLSGGRL 215
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMI-THRLTGLEQFD-RICVMDNGQI 551
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-199 |
1.51e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKitrtELPLLRRNIGVVFQDFRLLDHLTT 96
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK----DLCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 97 YENVALPLRVrgrdeSTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRL 176
Cdd:PRK13540 92 RENCLYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|....
gi 1426272298 177 LRLLLELNRLGTAVVIATH-DLGL 199
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-215 |
2.57e-13 |
|
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: 66.01 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FMSLKPTRGLITIFGKDRSKITRTELPllRRNIGVVFQDfrlldh 93
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEERA--RLGIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 94 lttyenvalPLRVRGrdestyrSDVIELLKWVGLGermhvlppiLSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLA 173
Cdd:cd03217 86 ---------PPEIPG-------VKNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDAL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1426272298 174 RRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRM-VLSGGRL 215
Cdd:cd03217 141 RLVAEVINKLREEGKSVLIITHYQRLLDYIKPDRVhVLYDGRI 183
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-171 |
3.42e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLP--ERSFqfLSGPSGAGKTTLLR--------------------LLFMSLKPTrglitifgkdrskitrteL 74
Cdd:COG4178 378 LLEDLSLSLKpgERLL--ITGPSGSGKSTLLRaiaglwpygsgriarpagarVLFLPQRPY------------------L 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 75 PL--LRrnigvvfqdfrlldhlttyENVALPLRVRGRDEStyrsDVIELLKWVGLG---ERMHVLPP---ILSGGEKQRA 146
Cdd:COG4178 438 PLgtLR-------------------EALLYPATAEAFSDA----ELREALEAVGLGhlaERLDEEADwdqVLSLGEQQRL 494
|
170 180
....*....|....*....|....*
gi 1426272298 147 AIARALIEQPRILLADEPTGNVDPQ 171
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEE 519
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-171 |
4.69e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLF--MSLKPTRGLITI----FGKDRSkitrtelpllrrnigvvfqdfrL 90
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAgaLKGTPVAGCVDVpdnqFGREAS----------------------L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 LDHLttyenvalplrvrGRDESTyrSDVIELLKWVGLGERMHVL--PPILSGGEKQRAAIARALIEQPRILLADEPTGNV 168
Cdd:COG2401 103 IDAI-------------GRKGDF--KDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
...
gi 1426272298 169 DPQ 171
Cdd:COG2401 168 DRQ 170
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-204 |
6.96e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.97 E-value: 6.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRY-GMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLfmslkpTR------GLITIFGKDrskITRTEL 74
Cdd:PRK11176 342 IEFRNVTFTYpGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLL------TRfydideGEILLDGHD---LRDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 75 PLLRRNIGVVFQDFRLLDHlTTYENVALPlrvrgRDESTYRSDVIELLKW---VGLGERM-HVLPPI-------LSGGEK 143
Cdd:PRK11176 413 ASLRNQVALVSQNVHLFND-TIANNIAYA-----RTEQYSREQIEEAARMayaMDFINKMdNGLDTVigengvlLSGGQR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 144 QRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVD 204
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTIEKAD 546
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-169 |
7.25e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 7.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEIlRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSkiTRTELPLLRRNIGVVFQDFR---L 90
Cdd:PRK10762 265 GPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV--TRSPQDGLANGIVYISEDRKrdgL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 LDHLTTYENVALP---------LRVRGRDESTYRSDVIELL--------KWVGLgermhvlppiLSGGEKQRAAIARALI 153
Cdd:PRK10762 342 VLGMSVKENMSLTalryfsragGSLKHADEQQAVSDFIRLFniktpsmeQAIGL----------LSGGNQQKVAIARGLM 411
|
170
....*....|....*.
gi 1426272298 154 EQPRILLADEPTGNVD 169
Cdd:PRK10762 412 TRPKVLILDEPTRGVD 427
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
11-198 |
1.08e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 11 YGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQDFRL 90
Cdd:PRK15056 16 WRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 91 LDH----LTTYENVALPLRVRGRDestyRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTG 166
Cdd:PRK15056 96 LVEdvvmMGRYGHMGWLRRAKKRD----RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|..
gi 1426272298 167 NVDPQLARRLLRLLLELNRLGTAVVIATHDLG 198
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-214 |
1.12e-12 |
|
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: 62.85 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrtelpllrrnI 81
Cdd:cd03221 1 IELENLSKTYG-GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK--------------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQdfrlldhlttyenvalplrvrgrdestyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03221 66 GYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1426272298 162 DEPTGNVDPQlaRRLLRLLLELNRLGTaVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:cd03221 95 DEPTNHLDLE--SIEALEEALKEYPGT-VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-169 |
1.13e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPllrRNI 81
Cdd:PRK10253 8 LRGEQLTLGYG-KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHLTTYENVAL------PLRVRGRDEStyRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQ 155
Cdd:PRK10253 84 GLLAQNATTPGDITVQELVARgryphqPLFTRWRKED--EEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170
....*....|....
gi 1426272298 156 PRILLADEPTGNVD 169
Cdd:PRK10253 162 TAIMLLDEPTTWLD 175
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-214 |
3.01e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 21 VSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLIT-----IFGKDRSKITRtelpllrrnIGVV--FQDFRLLDH 93
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILlrgqhIEGLPGHQIAR---------MGVVrtFQHVRLFRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 94 LTTYEN--VALPLRVRG-------------RDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRI 158
Cdd:PRK11300 95 MTVIENllVAQHQQLKTglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 159 LLADEPTGNVDPQLARRLLRLLLELNRL-GTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-171 |
3.13e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.99 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQ--------------FLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrsKITRTELPLLRRNIGV 83
Cdd:PRK10522 325 LRNVTFAYQDNGFSvgpinltikrgellFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 84 VFQDFRLLDHLTTYEN-VALPLRVRgrdestyrsdviELLKWVGLGERMH-----VLPPILSGGEKQRAAIARALIEQPR 157
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGkPANPALVE------------KWLERLKMAHKLEledgrISNLKLSKGQKKRLALLLALAEERD 469
|
170
....*....|....
gi 1426272298 158 ILLADEPTGNVDPQ 171
Cdd:PRK10522 470 ILLLDEWAADQDPH 483
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-170 |
3.95e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEI--LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIfgkDRSKITRTELPLLR 78
Cdd:PRK13642 4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI---DGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQ--DFRLLDhLTTYENVALPLRVRG--RDESTYRSDviELLKWVGLGERMHVLPPILSGGEKQRAAIARALIE 154
Cdd:PRK13642 81 RKIGMVFQnpDNQFVG-ATVEDDVAFGMENQGipREEMIKRVD--EALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170
....*....|....*.
gi 1426272298 155 QPRILLADEPTGNVDP 170
Cdd:PRK13642 158 RPEIIILDESTSMLDP 173
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-212 |
3.96e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQDfrlldhLTT 96
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKAD------LST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 97 YENVALPLRVRGRDESTYRSDVIELlkwVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRL 176
Cdd:PRK13543 100 LENLHFLCGLHGRRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLV 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1426272298 177 LRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSG 212
Cdd:PRK13543 177 NRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLEA 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-197 |
6.07e-12 |
|
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: 64.26 E-value: 6.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 26 PERSFQFLsGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskiTRTELPLLRRNIGVVFQDFRLLDHLTTYENVALPLR 105
Cdd:TIGR01257 1964 PGECFGLL-GVNGAGKTTTFKMLTGDTTVTSGDATVAGKS----ILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 106 VRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNR 185
Cdd:TIGR01257 2039 LRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR 2118
|
170
....*....|..
gi 1426272298 186 LGTAVVIATHDL 197
Cdd:TIGR01257 2119 EGRAVVLTSHSM 2130
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-170 |
6.96e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.99 E-value: 6.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLpERS--FQFLsGPSGAGKTTLLRLLFMSLKPTRGLITIFGK--DRSKITrtelplLRRNIGVVFQDFRLLDHLT 95
Cdd:NF033858 284 HVSFRI-RRGeiFGFL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIA------TRRRVGYMSQAFSLYGELT 355
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 96 TYENVALPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDP 170
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP 430
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-170 |
1.05e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.61 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKD-RSKITRTEL------ 74
Cdd:NF033858 2 ARLEGVSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDmADARHRRAVcpriay 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 75 -PL-LRRNigvvfqdfrLLDHLTTYENVALPLRVRGRDESTYRSDVIELLKWVGLG---ERmhvlpPI--LSGGEKQRAA 147
Cdd:NF033858 81 mPQgLGKN---------LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLApfaDR-----PAgkLSGGMKQKLG 146
|
170 180
....*....|....*....|...
gi 1426272298 148 IARALIEQPRILLADEPTGNVDP 170
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDP 169
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-169 |
1.82e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPE--ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLL--FMSLKPTRGLI------------------ 59
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrFYDLKNDHHIVfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 60 -------------------------TIF---GK---DRSKITRTELPLLRRNIGVVFQDfRLLDHLTTYENVALplrvrG 108
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedsTVFknsGKillDGVDICDYNLKDLRNLFSIVSQE-PMLFNMSIYENIKF-----G 1319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 109 RDESTyRSDVIELLKWVGLGERMHVLP-----------PILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PTZ00265 1320 KEDAT-REDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-165 |
2.12e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.24 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 3 RFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELplLRRNIG 82
Cdd:PRK11288 6 SFDGIGKTFP-GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAA--LAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 83 VVFQDFRLLDHLTTYENV---ALPLRVRGRDESTYRSDVIELLKwvGLGERMHVLPPI--LSGGEKQRAAIARALIEQPR 157
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLE--HLGVDIDPDTPLkyLSIGQRQMVEIAKALARNAR 160
|
....*...
gi 1426272298 158 ILLADEPT 165
Cdd:PRK11288 161 VIAFDEPT 168
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
17-169 |
3.74e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.96 E-value: 3.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPER------SFQF-------LSGPSGAGKTTLLRLLFMSLKPTRGLITIfgkDRSKITRTELPLLRRNIGV 83
Cdd:PRK10575 13 ALRNVSFRVPGRtllhplSLTFpagkvtgLIGHNGSGKSTLLKMLGRHQPPSEGEILL---DAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 84 VFQDFRLLDHLTTYENVAL---PLR-VRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRIL 159
Cdd:PRK10575 90 LPQQLPAAEGMTVRELVAIgryPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCL 169
|
170
....*....|
gi 1426272298 160 LADEPTGNVD 169
Cdd:PRK10575 170 LLDEPTSALD 179
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-219 |
4.99e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMG-PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElplLRR 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 NIGVVFQDFRL--------LDHLTTYENVALPLRVrgrdESTYRSDVIELLKWvGLGERMHVLPPILSGGEKQRAAIARA 151
Cdd:PLN03232 1311 VLSIIPQSPVLfsgtvrfnIDPFSEHNDADLWEAL----ERAHIKDVIDRNPF-GLDAEVSEGGENFSVGQRQLLSLARA 1385
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 152 LIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVDaRRMVLSGGRLEIYD 219
Cdd:PLN03232 1386 LLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIA-HRLNTIIDCD-KILVLSSGQVLEYD 1451
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
35-214 |
1.12e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 60.12 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKT-TLLRLlfMSLKPTRGLIT---IF-GKDRSKITRTELPLLR-RNIGVVFQDfrLLDHLTTYENVA------L 102
Cdd:PRK09473 49 GESGSGKSqTAFAL--MGLLAANGRIGgsaTFnGREILNLPEKELNKLRaEQISMIFQD--PMTSLNPYMRVGeqlmevL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 103 PLRvRGRDESTYRSDVIELLKWVGLGE---RMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRL 179
Cdd:PRK09473 125 MLH-KGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTL 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 1426272298 180 LLELNRL-GTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:PRK09473 204 LNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
19-164 |
1.36e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.66 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 19 RDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDrskitrtelplLRRNIGVVFQDFRLLDH----- 93
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEP-----------IRRQRDEYHQDLLYLGHqpgik 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 94 --LTTYENV--ALPLRVRGRDEstyrsDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:PRK13538 87 teLTALENLrfYQRLHGPGDDE-----ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
33-169 |
1.76e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 59.72 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKT----TLLRLLfmslkPT------RGLITIFGKDRSKITRTELPLLRRN-IGVVFQDFRL-LDHLTT---- 96
Cdd:PRK15134 40 LVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASEQTLRGVRGNkIAMIFQEPMVsLNPLHTlekq 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 97 -YENVALPlrvRGRDESTYRSDVIELLKWVGL---GERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK15134 115 lYEVLSLH---RGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALD 188
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-171 |
2.01e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.73 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrsKITRTELPLLRRNIGVVFQD-FRLLDhlT 95
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI---PLTKLQLDSWRSRLAVVSQTpFLFSD--T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 96 TYENVALplrvrGRDESTyRSDVIELLKWVGLGERMHVLPP-----------ILSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:PRK10789 405 VANNIAL-----GRPDAT-QQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILILDDA 478
|
....*..
gi 1426272298 165 TGNVDPQ 171
Cdd:PRK10789 479 LSAVDGR 485
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-219 |
5.37e-10 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 57.40 E-value: 5.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPE---------------------ILRDVSFHLPE-RSFQFLsGPSGAGKTTLLRLLFMSLKPTRGL 58
Cdd:COG1134 4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreefwALKDVSFEVERgESVGII-GRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 59 ITIfgkdRSKITrtelPLLrrNIGVVFQdfrllDHLTTYENVALPLRVRGRDestyRSDVIELLKWV----GLGERMHVl 134
Cdd:COG1134 83 VEV----NGRVS----ALL--ELGAGFH-----PELTGRENIYLNGRLLGLS----RKEIDEKFDEIvefaELGDFIDQ- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 135 pPI--LSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSG 212
Cdd:COG1134 143 -PVktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEK 221
|
....*..
gi 1426272298 213 GRLEIYD 219
Cdd:COG1134 222 GRLVMDG 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
35-214 |
9.10e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRsKITRtelPLLRRnIGVVFQDFRLLDHLTTYENVA------LPLRVRG 108
Cdd:PLN03211 101 GPSGSGKSTLLNALAGRIQGNNFTGTILANNR-KPTK---QILKR-TGFVTQDDILYPHLTVRETLVfcsllrLPKSLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 109 RDESTYRSDVIELLKWVGLGERM--HVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRL 186
Cdd:PLN03211 176 QEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK 255
|
170 180 190
....*....|....*....|....*....|...
gi 1426272298 187 GTAVVIATHD-----LGLMDQVdarrMVLSGGR 214
Cdd:PLN03211 256 GKTIVTSMHQpssrvYQMFDSV----LVLSEGR 284
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-170 |
1.54e-09 |
|
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: 57.23 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLlFMSLKPTRGLITIFGKDRSKITrteLPLLRRNIGVVFQD------ 87
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSA-LLRLLSTEGEIQIDGVSWNSVT---LQTWRKAFGVIPQKvfifsg 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 88 -FRLldHLTTYEnvalplrvRGRDESTYRsdvieLLKWVGLGERMHVLPP-----------ILSGGEKQRAAIARALIEQ 155
Cdd:TIGR01271 1307 tFRK--NLDPYE--------QWSDEEIWK-----VAEEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSK 1371
|
170
....*....|....*
gi 1426272298 156 PRILLADEPTGNVDP 170
Cdd:TIGR01271 1372 AKILLLDEPSAHLDP 1386
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-213 |
2.02e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITrtelPLLRRNIGV--VFQDFRLL 91
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT----PAKAHQLGIylVPQEPLLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 92 DHLTTYENVALPLRVRGRDESTyrsdVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQ 171
Cdd:PRK15439 99 PNLSVKENILFGLPKRQASMQK----MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1426272298 172 LARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGG 213
Cdd:PRK15439 175 ETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
56-215 |
2.14e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 56.29 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 56 RGLITIFGKDRSKITRTElpllrrnIGVVFQD------------FRLLDHLTTYEnvalplrvrGRDESTYRSDVIELLK 123
Cdd:PRK11022 73 QDLQRISEKERRNLVGAE-------VAMIFQDpmtslnpcytvgFQIMEAIKVHQ---------GGNKKTRRQRAIDLLN 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 124 WVGL---GERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQ-LARRLLRLLLELNRLGTAVVIATHDLGL 199
Cdd:PRK11022 137 QVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTiQAQIIELLLELQQKENMALVLITHDLAL 216
|
170
....*....|....*.
gi 1426272298 200 MDQVDARRMVLSGGRL 215
Cdd:PRK11022 217 VAEAAHKIIVMYAGQV 232
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-212 |
3.21e-09 |
|
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: 55.11 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRS--------KITRTELPLLRRNIGvvfqdfrllDHLTtyenvalplrv 106
Cdd:cd03237 32 GPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGTVRDLLSSITK---------DFYT----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 107 rgrdESTYRSDVIELLKWVGLGERmhvLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRL--LLELN 184
Cdd:cd03237 92 ----HPYFKTEIAKPLQIEQILDR---EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVirRFAEN 164
|
170 180
....*....|....*....|....*...
gi 1426272298 185 RLGTAVVIaTHDLGLMDQVDARRMVLSG 212
Cdd:cd03237 165 NEKTAFVV-EHDIIMIDYLADRLIVFEG 191
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-169 |
3.52e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 55.79 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLpeRSFQFL--SGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSkiTRTELPLLRRNIGVVFQDfR-- 89
Cdd:COG1129 264 VGGVVRDVSFSV--RAGEILgiAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDAIRAGIAYVPED-Rkg 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 90 --LLDHLTTYENVALP-LRVRGR----DESTYRSDVIELLKwvglgeRMHVLPP-----I--LSGGEKQRAAIARALIEQ 155
Cdd:COG1129 339 egLVLDLSIRENITLAsLDRLSRggllDRRRERALAEEYIK------RLRIKTPspeqpVgnLSGGNQQKVVLAKWLATD 412
|
170
....*....|....
gi 1426272298 156 PRILLADEPTGNVD 169
Cdd:COG1129 413 PKVLILDEPTRGID 426
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-216 |
3.81e-09 |
|
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: 55.99 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILR--DVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLkPTRGLITIFGKDRSKITRTELPLLR 78
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKFEGNVFINGKPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 79 RNIGVVFQDFR---LLDHLTTYENVALPlrVRGRDESTYRSDVIELLKWVGLG-ERMHVLP-----PI--LSGGEKQRAA 147
Cdd:TIGR02633 336 AGIAMVPEDRKrhgIVPILGVGKNITLS--VLKSFCFKMRIDAAAELQIIGSAiQRLKVKTaspflPIgrLSGGNQQKAV 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 148 IARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRLE 216
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-219 |
6.64e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMG-PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElplLRRN 80
Cdd:PLN03130 1238 IKFEDVVLRYRPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD---LRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRL--------LDHLTTYENVALPlrvrgrdESTYRSDVIELLKWVGLGERMHVLP--PILSGGEKQRAAIAR 150
Cdd:PLN03130 1315 LGIIPQAPVLfsgtvrfnLDPFNEHNDADLW-------ESLERAHLKDVIRRNSLGLDAEVSEagENFSVGQRQLLSLAR 1387
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1426272298 151 ALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIAtHDLGLMDQVDaRRMVLSGGRLEIYD 219
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIA-HRLNTIIDCD-RILVLDAGRVVEFD 1454
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
119-214 |
1.61e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 119 IELLKWVGLGER---MHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRL-LRLLLELNRLGTAVVIAT 194
Cdd:PRK15093 137 IELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIfRLLTRLNQNNNTTILLIS 216
|
90 100
....*....|....*....|
gi 1426272298 195 HDLGLMDQVDARRMVLSGGR 214
Cdd:PRK15093 217 HDLQMLSQWADKINVLYCGQ 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-170 |
2.39e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.63 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 4 FENVGHRYGMG-PEILRDVSFHLPERSFQFLSGPSGAGKTTLLrLLFMSLKPT-RGLITIFGKDrskITRTELPLLRRNI 81
Cdd:PTZ00243 1311 FEGVQMRYREGlPLVLRGVSFRIAPREKVGIVGRTGSGKSTLL-LTFMRMVEVcGGEIRVNGRE---IGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 82 GVVFQDFRLLDHlTTYENVALPLrvrgrdESTyRSDVIELLKWVGLGERMH-----VLPPILSG------GEKQRAAIAR 150
Cdd:PTZ00243 1387 SMIPQDPVLFDG-TVRQNVDPFL------EAS-SAEVWAALELVGLRERVAsesegIDSRVLEGgsnysvGQRQLMCMAR 1458
|
170 180
....*....|....*....|.
gi 1426272298 151 ALIEQPR-ILLADEPTGNVDP 170
Cdd:PTZ00243 1459 ALLKKGSgFILMDEATANIDP 1479
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
137-171 |
4.22e-08 |
|
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: 51.00 E-value: 4.22e-08
10 20 30
....*....|....*....|....*....|....*
gi 1426272298 137 ILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQ 171
Cdd:cd03223 91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-169 |
1.18e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGliTIFgkdRSKITRTELPLLRRN 80
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG--TVF---RSAKVRMAVFSQHHV 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRLLDHLTTYENVAlplrvrgrdESTYRSDvielLKWVGLGERMHVLPP-ILSGGEKQRAAIARALIEQPRIL 159
Cdd:PLN03073 583 DGLDLSSNPLLYMMRCFPGVP---------EQKLRAH----LGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHIL 649
|
170
....*....|
gi 1426272298 160 LADEPTGNVD 169
Cdd:PLN03073 650 LLDEPSNHLD 659
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-201 |
1.43e-07 |
|
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: 50.44 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 9 HRYGMGPEILrdvsFHLP-ERSFQFLS--GPSGAGKTTLLRLLFMSLKPTrglitiFGKDRSKITRTELplLRRNIGVVF 85
Cdd:cd03236 8 HRYGPNSFKL----HRLPvPREGQVLGlvGPNGIGKSTALKILAGKLKPN------LGKFDDPPDWDEI--LDEFRGSEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 86 QDF--RLLD------HLTTYENVaLPLRVRGR--------DESTYRSDVIELLKWVGLGERmHVlpPILSGGEKQRAAIA 149
Cdd:cd03236 76 QNYftKLLEgdvkviVKPQYVDL-IPKAVKGKvgellkkkDERGKLDELVDQLELRHVLDR-NI--DQLSGGELQRVAIA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 150 RALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMD 201
Cdd:cd03236 152 AALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-169 |
1.51e-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: 51.09 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 6 NVGHRYGMGPEILRDVSFhlpersfQFLS-------GPSGAGKTTLLRLLfmslkptRGLITIF-GKDRskitrtelPLL 77
Cdd:TIGR03719 9 RVSKVVPPKKEILKDISL-------SFFPgakigvlGLNGAGKSTLLRIM-------AGVDKDFnGEAR--------PQP 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNIGVVFQDFRLLDHLTTYENVALPLRVRGR-----------------------DESTYRSDVIELLKWVGLGERMHV- 133
Cdd:TIGR03719 67 GIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDaldrfneisakyaepdadfdklaAEQAELQEIIDAADAWDLDSQLEIa 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1426272298 134 -----LPP------ILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:TIGR03719 147 mdalrCPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-170 |
1.66e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 50.67 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 21 VSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPT------------RGLITIFGKDRSKITRtelpllrRNIGVVFQD- 87
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtadrfrwngIDLLKLSPRERRKIIG-------REIAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 88 FRLLDHLTTYE---NVALPLRV-------RGRDESTYrsdVIELLKWVGLGERMHVL---PPILSGGEKQRAAIARALIE 154
Cdd:COG4170 99 SSCLDPSAKIGdqlIEAIPSWTfkgkwwqRFKWRKKR---AIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIAN 175
|
170
....*....|....*.
gi 1426272298 155 QPRILLADEPTGNVDP 170
Cdd:COG4170 176 QPRLLIADEPTNAMES 191
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
5-169 |
4.65e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 4.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGMGPeILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGlitifgkdrsKITRTElpllRRNIGVV 84
Cdd:PRK15064 323 ENLTKGFDNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSE----NANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 85 FQD--------FRLLDHLTTYenvalplRVRGRDESTYRSDVIELL-------KWVGlgermhvlppILSGGEKQRAAIA 149
Cdd:PRK15064 388 AQDhaydfendLTLFDWMSQW-------RQEGDDEQAVRGTLGRLLfsqddikKSVK----------VLSGGEKGRMLFG 450
|
170 180
....*....|....*....|
gi 1426272298 150 RALIEQPRILLADEPTGNVD 169
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD 470
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-170 |
4.82e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.08 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLlFMSLKPTRGLITIFGKDRSKITrteLPLLRRNIGVVFQD------ 87
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSA-FLRLLNTEGDIQIDGVSWNSVP---LQKWRKAFGVIPQKvfifsg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 88 -FRLldHLTTYEnvalplrvRGRDESTYRsdvieLLKWVGLGERMHVLPP-----------ILSGGEKQRAAIARALIEQ 155
Cdd:cd03289 92 tFRK--NLDPYG--------KWSDEEIWK-----VAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSK 156
|
170
....*....|....*
gi 1426272298 156 PRILLADEPTGNVDP 170
Cdd:cd03289 157 AKILLLDEPSAHLDP 171
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
134-169 |
5.26e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 5.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1426272298 134 LPP------ILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK11819 154 CPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-170 |
6.88e-07 |
|
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: 49.36 E-value: 6.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLfmslkptRGLITIFGKDRSKITRTELPLLRRN 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-------GELWPVYGGRLTKPAKGKLFYVPQR 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 IGVVFQDFRlldhlttyENVALPLRVRGRDESTYR-SDVIELLKWVGLGermHVLP------------PILSGGEKQRAA 147
Cdd:TIGR00954 524 PYMTLGTLR--------DQIIYPDSSEDMKRRGLSdKDLEQILDNVQLT---HILEreggwsavqdwmDVLSGGEKQRIA 592
|
170 180
....*....|....*....|...
gi 1426272298 148 IARALIEQPRILLADEPTGNVDP 170
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSV 615
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-215 |
7.48e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 49.17 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 15 PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGkdrskitrtelpllrrNIGVVFQDfRLLDHL 94
Cdd:TIGR00957 651 PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG----------------SVAYVPQQ-AWIQND 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 95 TTYENValpLRVRGRDESTYRSdvieLLKWVGLGERMHVLPP-----------ILSGGEKQRAAIARALIEQPRILLADE 163
Cdd:TIGR00957 714 SLRENI---LFGKALNEKYYQQ----VLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 164 PTGNVDPQLARRLLRLLL--ELNRLGTAVVIATHDLGLMDQVDArRMVLSGGRL 215
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDV-IIVMSGGKI 839
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-171 |
9.05e-07 |
|
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: 47.85 E-value: 9.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENV----GHRYGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKdrskitrtelpll 77
Cdd:cd03250 1 ISVEDAsftwDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 rrnIGVVFQDFRLLdHLTTYENV--ALPLrvrgrDESTYRsDVIEL------LKWVGLGERMHvlppI------LSGGEK 143
Cdd:cd03250 68 ---IAYVSQEPWIQ-NGTIRENIlfGKPF-----DEERYE-KVIKAcalepdLEILPDGDLTE----IgekginLSGGQK 133
|
170 180
....*....|....*....|....*...
gi 1426272298 144 QRAAIARALIEQPRILLADEPTGNVDPQ 171
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAH 161
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-165 |
1.09e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLfMSLKPT---RGLITIFGKDR--SKITRTElpllRRNIGVVFQDFRLLDHLTTYENVAL---PL 104
Cdd:PRK13549 36 LCGENGAGKSTLMKVL-SGVYPHgtyEGEIIFEGEELqaSNIRDTE----RAGIAIIHQELALVKELSVLENIFLgneIT 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 105 RvRGR---DESTYRSDviELLKWVGLGerMHVLPPI--LSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:PRK13549 111 P-GGImdyDAMYLRAQ--KLLAQLKLD--INPATPVgnLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-165 |
1.83e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.69 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRS----KITRTElpllrrNIGVVFQDFRLLDHLTTYENVALplrvrG 108
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEA------GIGIIHQELNLIPQLTIAENIFL-----G 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 109 RdESTYRSDVIE----------LLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:PRK10762 104 R-EFVNRFGRIDwkkmyaeadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-164 |
1.90e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 46.98 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLfM---SLKPTRGLITIFGKDrskITrtELPL---LRRNIGVVFQD-- 87
Cdd:COG0396 14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL-MghpKYEVTSGSILLDGED---IL--ELSPderARAGIFLAFQYpv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 88 ----FRLLDHLTTYENvalplRVRGRDEST--YRSDVIELLKWVGLGERMhvlppI-------LSGGEKQRAAIARALIE 154
Cdd:COG0396 88 eipgVSVSNFLRTALN-----ARRGEELSAreFLKLLKEKMKELGLDEDF-----LdryvnegFSGGEKKRNEILQMLLL 157
|
170
....*....|
gi 1426272298 155 QPRILLADEP 164
Cdd:COG0396 158 EPKLAILDET 167
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-171 |
1.92e-06 |
|
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: 46.47 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLfmSLKPTRGLIT----IFGKDRSKItrtelplLRRNIGVVFQDFRLL 91
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVL--AGRKTAGVITgeilINGRPLDKN-------FQRSTGYVEQQDVHS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 92 DHLTTYENVALPLRVRGrdestyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIEQPRILLADEPTGNVDPQ 171
Cdd:cd03232 92 PNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-212 |
2.15e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 47.47 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKTTLLRLLFMSLKPTRGliTIFGKDR---------SKITRTELPLLRRNIGVVFqdfrlldhlttyenvalplr 105
Cdd:COG1245 373 GPNGIGKTTFAKILAGVLKPDEG--EVDEDLKisykpqyisPDYDGTVEEFLRSANTDDF-------------------- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 106 vrgrDESTYRSDVIELLkwvGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVD-PQLARRLLRLLLELN 184
Cdd:COG1245 431 ----GSSYYKTEIIKPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDvEQRLAVAKAIRRFAE 503
|
170 180
....*....|....*....|....*...
gi 1426272298 185 RLGTAVVIATHDLGLMDQVDARRMVLSG 212
Cdd:COG1245 504 NRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-204 |
3.10e-06 |
|
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: 45.78 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRllfmslkptrgliTIFGKDRSKITRTELPLLRRNIGVVfqdfrlLDHLTTY 97
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNKLIF------IDQLQFL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 98 ENVALPLRVRGRDESTyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIEQPR--ILLADEPTGNVDPQLARR 175
Cdd:cd03238 72 IDVGLGYLTLGQKLST------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQ 127
|
170 180
....*....|....*....|....*....
gi 1426272298 176 LLRLLLELNRLGTAVVIATHDLGLMDQVD 204
Cdd:cd03238 128 LLEVIKGLIDLGNTVILIEHNLDVLSSAD 156
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-169 |
3.13e-06 |
|
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: 47.24 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITI--------FGKDRSKITRTE 73
Cdd:TIGR03719 323 IEAENLTKAFG-DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayVDQSRDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 74 lpllrrnigVVFQDFRL-LDHLTTyENVALPLRV-------RGRDEStyrsdviellKWVGlgermhvlppILSGGEKQR 145
Cdd:TIGR03719 402 ---------TVWEEISGgLDIIKL-GKREIPSRAyvgrfnfKGSDQQ----------KKVG----------QLSGGERNR 451
|
170 180
....*....|....*....|....
gi 1426272298 146 AAIARALIEQPRILLADEPTGNVD 169
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-215 |
3.25e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 46.62 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 15 PEILRDVSFHLPERSFQFLSGPSGAGKT----TLLRLLFMSLKPTRGLITIFGKdrskitRTELPLLR-RNIGVVFQDFR 89
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK------PVAPCALRgRKIATIMQNPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 90 -LLDHLTTYENVAL-PLRVRGRDEStyRSDVIELLKWVGLGERMHVL---PPILSGGEKQRAAIARALIEQPRILLADEP 164
Cdd:PRK10418 90 sAFNPLHTMHTHAReTCLALGKPAD--DATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1426272298 165 TGNVDP-QLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK10418 168 TTDLDVvAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-169 |
3.53e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 5 ENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIfGkdrskiTRTELpllrrnigVV 84
Cdd:PRK11147 323 ENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-G------TKLEV--------AY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 85 FQDFR-LLD-HLTTYENVAlplrvRGRDESTyrsdviellkwVGlGERMHVL--------PP--------ILSGGEKQRA 146
Cdd:PRK11147 387 FDQHRaELDpEKTVMDNLA-----EGKQEVM-----------VN-GRPRHVLgylqdflfHPkramtpvkALSGGERNRL 449
|
170 180
....*....|....*....|...
gi 1426272298 147 AIARALIEQPRILLADEPTGNVD 169
Cdd:PRK11147 450 LLARLFLKPSNLLILDEPTNDLD 472
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
14-165 |
4.53e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.56 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLpeRSFQFL--SGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELplLRRNIGVVFQDfRLL 91
Cdd:COG3845 270 GVPALKDVSLEV--RAGEILgiAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER--RRLGVAYIPED-RLG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 92 D----HLTTYENVAL------PLRVRGR-DESTYRSDVIELLkwvglgERMHVLPP-------ILSGGEKQRAAIARALI 153
Cdd:COG3845 345 RglvpDMSVAENLILgryrrpPFSRGGFlDRKAIRAFAEELI------EEFDVRTPgpdtparSLSGGNQQKVILARELS 418
|
170
....*....|..
gi 1426272298 154 EQPRILLADEPT 165
Cdd:COG3845 419 RDPKLLIAAQPT 430
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
138-169 |
4.61e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 4.61e-06
10 20 30
....*....|....*....|....*....|..
gi 1426272298 138 LSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
17-169 |
4.83e-06 |
|
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: 46.83 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGK-DRSKITRTELP-LLRRNI--GVVFQDFRlld 92
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTSWIMPgTIKDNIifGLSYDEYR--- 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 93 hlttyenvalplrvrgrdestYRSdvieLLKWVGLGERMHVLPP-----------ILSGGEKQRAAIARALIEQPRILLA 161
Cdd:TIGR01271 518 ---------------------YTS----VIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLL 572
|
....*...
gi 1426272298 162 DEPTGNVD 169
Cdd:TIGR01271 573 DSPFTHLD 580
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-205 |
4.97e-06 |
|
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: 46.36 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLfMSLKPT---RGLITIFGKD--RSKITRTElpllRRNIGVVFQDFRLLDHLTTYENV------A 101
Cdd:TIGR02633 32 LCGENGAGKSTLMKIL-SGVYPHgtwDGEIYWSGSPlkASNIRDTE----RAGIVIIHQELTLVPELSVAENIflgneiT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 102 LPLRVRGRDESTYRSDviELLKWVGLgERMHVLPPI--LSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRL 179
Cdd:TIGR02633 107 LPGGRMAYNAMYLRAK--NLLRELQL-DADNVTRPVgdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDI 183
|
170 180
....*....|....*....|....*.
gi 1426272298 180 LLELNRLGTAVVIATHDLglmDQVDA 205
Cdd:TIGR02633 184 IRDLKAHGVACVYISHKL---NEVKA 206
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-212 |
5.43e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.34 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKTTLLRLLFMSLKPTRGLITifgkdrSKITRTELP-LLRRNIGVVFQDFrLLDHLTTYenvalplrvrgrDEST 113
Cdd:PRK13409 372 GPNGIGKTTFAKLLAGVLKPDEGEVD------PELKISYKPqYIKPDYDGTVEDL-LRSITDDL------------GSSY 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 114 YRSDVIELLKwvglgermhvLPPI-------LSGGEKQRAAIARALIEQPRILLADEPTGNVD-PQLARRLLRLLLELNR 185
Cdd:PRK13409 433 YKSEIIKPLQ----------LERLldknvkdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDvEQRLAVAKAIRRIAEE 502
|
170 180
....*....|....*....|....*..
gi 1426272298 186 LGTAVVIATHDLGLMDQVDARRMVLSG 212
Cdd:PRK13409 503 REATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-169 |
5.52e-06 |
|
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: 46.00 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGK-DRSKITRTELP-LLRRNI--GVVFQDFR 89
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFSWIMPgTIKENIifGVSYDEYR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 90 lldhlttYENVALPLRVRgRDESTYRSDVIELLKWVGLgermhvlppILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:cd03291 129 -------YKSVVKACQLE-EDITKFPEKDNTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-171 |
7.83e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLfmSLKPTRGLITifGKDRSKITRTELPLLRRNIGVVFQDFRLLDHLTTYENVALPLRVRGRDES 112
Cdd:TIGR00956 794 LMGASGAGKTTLLNVL--AERVTTGVIT--GGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLRQPKSV 869
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 113 T------YRSDVIELLKWVGLGERMHVLPPI-LSGGEKQRAAIARALIEQPRILL-ADEPTGNVDPQ 171
Cdd:TIGR00956 870 SksekmeYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQ 936
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-169 |
8.00e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.69 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 20 DVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLkPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQDFR------LLD- 92
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDRKrdgivpVMGv 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 93 ----HLTTYENVALPLRVRGRDESTYRSDVIELLKWvglgERMHVLPPI--LSGGEKQRAAIARALIEQPRILLADEPTG 166
Cdd:PRK13549 359 gkniTLAALDRFTGGSRIDDAAELKTILESIQRLKV----KTASPELAIarLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
...
gi 1426272298 167 NVD 169
Cdd:PRK13549 435 GID 437
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-197 |
9.79e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 44.92 E-value: 9.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLfMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGV---------VFQdfrlldhlttYENVALP 103
Cdd:PRK03695 27 LVGPNGAGKSTLLARM-AGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQqqtppfampVFQ----------YLTLHQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 104 LRVRGRDESTYRSDVIELLKwvgLGERMHVLPPILSGGEKQR---AA----IARALIEQPRILLADEPTGNVDPQLARRL 176
Cdd:PRK03695 96 DKTRTEAVASALNEVAEALG---LDDKLGRSVNQLSGGEWQRvrlAAvvlqVWPDINPAGQLLLLDEPMNSLDVAQQAAL 172
|
170 180
....*....|....*....|.
gi 1426272298 177 LRLLLELNRLGTAVVIATHDL 197
Cdd:PRK03695 173 DRLLSELCQQGIAVVMSSHDL 193
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-165 |
2.08e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKTTLLRLLFMSLKPTrglitiFGKDRSKITRTELplLRRNIGVVFQD-FRLLdhlttYEN---VA--------L 102
Cdd:PRK13409 106 GPNGIGKTTAVKILSGELIPN------LGDYEEEPSWDEV--LKRFRGTELQNyFKKL-----YNGeikVVhkpqyvdlI 172
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1426272298 103 PLRVRGR--------DESTYRSDVIELLkwvGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:PRK13409 173 PKVFKGKvrellkkvDERGKLDEVVERL---GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
33-215 |
2.36e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 44.06 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 33 LSGPSGAGKTTLLRLLfMSLKPTRGLITIFGKDRSKITRTELPLLRrniGVVFQDFRLLDHLTTYENVALPLRvRGRDES 112
Cdd:COG4138 27 LIGPNGAGKSTLLARM-AGLLPGQGEILLNGRPLSDWSAAELARHR---AYLSQQQSPPFAMPVFQYLALHQP-AGASSE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 113 TYRSDVIELLKWVGLGERMHvlPPI--LSGGEKQRAAIARALIE-------QPRILLADEPTGNVDPQLARRLLRLLLEL 183
Cdd:COG4138 102 AVEQLLAQLAEALGLEDKLS--RPLtqLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLREL 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 1426272298 184 NRLGTAVVIATHDLGLM----DQVdarrMVLSGGRL 215
Cdd:COG4138 180 CQQGITVVMSSHDLNHTlrhaDRV----WLLKQGKL 211
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-169 |
2.44e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.39 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 19 RDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSkiTRTELPLLRRNIGVVFQDFR---LLDHLT 95
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYITESRRdngFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 96 TYENVALP--LRVRG----------RDESTYRSDVIELL--KWVGLGERMHVLppilSGGEKQRAAIARALIEQPRILLA 161
Cdd:PRK09700 358 IAQNMAISrsLKDGGykgamglfheVDEQRTAENQRELLalKCHSVNQNITEL----SGGNQQKVLISKWLCCCPEVIIF 433
|
....*...
gi 1426272298 162 DEPTGNVD 169
Cdd:PRK09700 434 DEPTRGID 441
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
15-169 |
2.80e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 15 PEIlRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTE-----LPLL---RRNIGVVFQ 86
Cdd:PRK10982 262 PSI-RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgFALVteeRRSTGIYAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 87 ---DFR-LLDHLTTYENvalplRVRGRDESTYRSDViellKWVGlgERMHVLPP-------ILSGGEKQRAAIARALIEQ 155
Cdd:PRK10982 341 ldiGFNsLISNIRNYKN-----KVGLLDNSRMKSDT----QWVI--DSMRVKTPghrtqigSLSGGNQQKVIIGRWLLTQ 409
|
170
....*....|....
gi 1426272298 156 PRILLADEPTGNVD 169
Cdd:PRK10982 410 PEILMLDEPTRGID 423
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-214 |
3.99e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKT----TLLRLLFMSLKPTR-GLITIFGKDRSKITRTELP--LLRR----NIGVVFQ 86
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQcDKMLLRRRSRQVIELSEQSaaQMRHvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 87 D--FRLLDHLTTYENVALPLRVR---GRDESTYRSDviELLKWVGLGERMHVL---PPILSGGEKQRAAIARALIEQPRI 158
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHqgaSREEAMVEAK--RMLDQVRIPEAQTILsryPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 159 LLADEPTGNVDPQ-LARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGR 214
Cdd:PRK10261 190 LIADEPTTALDVTiQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
109-215 |
6.28e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 109 RDESTYRSDviELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGT 188
Cdd:NF000106 118 RKDARARAD--ELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100
....*....|....*....|....*..
gi 1426272298 189 AVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-169 |
9.27e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 4 FENV------GHRYGmgpeilrdvsfhlpersfqfLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRskitrteLPLL 77
Cdd:PRK15064 17 FENIsvkfggGNRYG--------------------LIGANGCGKSTFMKILGGDLEPSAGNVSLDPNER-------LGKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 78 RRNiGVVFQDFRLLD-----HLTTYENV-------ALP-------LRVrGRDESTY--------RSDVIELLKWVGLGER 130
Cdd:PRK15064 70 RQD-QFAFEEFTVLDtvimgHTELWEVKqerdriyALPemseedgMKV-ADLEVKFaemdgytaEARAGELLLGVGIPEE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1426272298 131 MH------VLPpilsgGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK15064 148 QHyglmseVAP-----GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
4-169 |
1.12e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 4 FENVGHRYGMGPE------------ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLfmSLKPTRGLI------TIFGKD 65
Cdd:PLN03140 870 FDDVNYFVDMPAEmkeqgvtedrlqLLREVTGAFRPGVLTALMGVSGAGKTTLMDVL--AGRKTGGYIegdiriSGFPKK 947
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 66 RSKITRTElpllrrniGVVFQDFRLLDHLTTYENVA------LPLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPI-- 137
Cdd:PLN03140 948 QETFARIS--------GYCEQNDIHSPQVTVRESLIysaflrLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPGVtg 1019
|
170 180 190
....*....|....*....|....*....|..
gi 1426272298 138 LSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-170 |
1.28e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVGHRYGMGPeILRDVSFH-LPERSFQFLsGPSGAGKTTLLRLLfmslkpT----RGL---ITIFGKDR-SKITRT 72
Cdd:PRK10938 261 IVLNNGVVSYNDRP-ILHNLSWQvNPGEHWQIV-GPNGAGKSTLLSLI------TgdhpQGYsndLTLFGRRRgSGETIW 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 73 ELpllRRNIGVV----FQDFRLLdhlTTYENVALplrvRGRDES--TYR--SDVIELL--KW---VGLGERMHVLP-PIL 138
Cdd:PRK10938 333 DI---KKHIGYVssslHLDYRVS---TSVRNVIL----SGFFDSigIYQavSDRQQKLaqQWldiLGIDKRTADAPfHSL 402
|
170 180 190
....*....|....*....|....*....|..
gi 1426272298 139 SGGEKQRAAIARALIEQPRILLADEPTGNVDP 170
Cdd:PRK10938 403 SWGQQRLALIVRALVKHPTLLILDEPLQGLDP 434
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-169 |
2.42e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 1 MIRFENVGHRYGmGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIF-GKDRSKITRTELPLLRr 79
Cdd:PRK10636 312 LLKMEKVSAGYG-DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLR- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 80 nigvvfQDFRLLDHLTTYENVALPLRVRgrdestyrsdviELLKWVGL-GERMHVLPPILSGGEKQRAAIARALIEQPRI 158
Cdd:PRK10636 390 ------ADESPLQHLARLAPQELEQKLR------------DYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNL 451
|
170
....*....|.
gi 1426272298 159 LLADEPTGNVD 169
Cdd:PRK10636 452 LLLDEPTNHLD 462
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
14-165 |
2.93e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.25 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 14 GPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTElpLLRRNIGVVFQDFRLLDH 93
Cdd:PRK10982 10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGISMVHQELNLVLQ 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1426272298 94 LTTYENVAL---PLRVRGRDESTYRSDVIELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:PRK10982 88 RSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-201 |
3.44e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.92 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 35 GPSGAGKTTLLRLLFMSLKPTrglitiFGKDRSKITRTElpllrrnigvVFQDFR---LLDHLTT-YEN---VA------ 101
Cdd:COG1245 106 GPNGIGKSTALKILSGELKPN------LGDYDEEPSWDE----------VLKRFRgteLQDYFKKlANGeikVAhkpqyv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 102 --LPLRVRGR--------DESTYRSDVIELLKWVGLGERmhvlpPI--LSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:COG1245 170 dlIPKVFKGTvrellekvDERGKLDELAEKLGLENILDR-----DIseLSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|..
gi 1426272298 170 PQLARRLLRLLLELNRLGTAVVIATHDLGLMD 201
Cdd:COG1245 245 IYQRLNVARLIRELAEEGKYVLVVEHDLAILD 276
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
18-165 |
3.93e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLfMSLKPT---RGLITIFGKDR--SKITRTElpllRRNIGVVFQDFRLLD 92
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVL-SGVYPHgsyEGEILFDGEVCrfKDIRDSE----ALGIVIIHQELALIP 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 93 HLTTYENVAL--PLRVRG---RDESTYRSDviELLKWVGLGERMHVLPPILSGGEKQRAAIARALIEQPRILLADEPT 165
Cdd:NF040905 92 YLSIAENIFLgnERAKRGvidWNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-169 |
4.72e-04 |
|
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: 39.94 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 16 EILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPT---RGLITIFGKDRSKITRTelplLRRNIGVVFQDFRLLD 92
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK----YPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1426272298 93 HLTTYENVALPLRVRGrdestyrSDVIEllkwvglgermhvlppILSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:cd03233 97 TLTVRETLDFALRCKG-------NEFVR----------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
18-195 |
5.04e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 18 LRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRRNIGVVFQdfrlldhLTTY 97
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLE-------MTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 98 ENVALPLRVRGRDESTYRSdvIELLKWVG-LGERMHVlppiLSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRL 176
Cdd:PRK13541 89 ENLKFWSEIYNSAETLYAA--IHYFKLHDlLDEKCYS----LSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170
....*....|....*....
gi 1426272298 177 LRLLLELNRLGTAVVIATH 195
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSH 181
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-169 |
6.75e-04 |
|
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: 39.62 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 11 YGMGPEILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTELPLLRR-NIGVVFQDFR 89
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 90 LLDhLTTYENVAL--PL---RVRGRDESTYRSDVIELLKW---VGLGERmhvlPPILSGGEKQRAAIARALIEQPRILLA 161
Cdd:cd03290 90 LLN-ATVEENITFgsPFnkqRYKAVTDACSLQPDIDLLPFgdqTEIGER----GINLSGGQRQRICVARALYQNTNIVFL 164
|
....*...
gi 1426272298 162 DEPTGNVD 169
Cdd:cd03290 165 DDPFSALD 172
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
139-169 |
7.63e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 7.63e-04
10 20 30
....*....|....*....|....*....|.
gi 1426272298 139 SGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
138-215 |
7.79e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.03 E-value: 7.79e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1426272298 138 LSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSGGRL 215
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-171 |
7.87e-04 |
|
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: 39.13 E-value: 7.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 22 SFHLPERsFQF------LSGPSGAGKTTLLRLLFMSLKPTRGLITIFGKDRSKITRTelpllRRNIGVVfqdfrlldHLT 95
Cdd:cd03240 11 SFHERSE-IEFfspltlIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIRE-----GEVRAQV--------KLA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 96 TYENVALPLRVRgRDESTYRSDVI---ELLKWvgLGERMhvlPPILSGGEKQ------RAAIARALIEQPRILLADEPTG 166
Cdd:cd03240 77 FENANGKKYTIT-RSLAILENVIFchqGESNW--PLLDM---RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
....*
gi 1426272298 167 NVDPQ 171
Cdd:cd03240 151 NLDEE 155
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
33-49 |
1.28e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 37.90 E-value: 1.28e-03
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
138-212 |
1.72e-03 |
|
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: 37.94 E-value: 1.72e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1426272298 138 LSGGEKQRAAIARALIEQPRILLADEPTGNVD-PQLARRLLRLLLELNRLGTAVVIATHDLGLMDQVDARRMVLSG 212
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDiEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
15-201 |
1.80e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.72 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 15 PEILRDVSFHLPERSFQFLSGPSGAGKTTLLRllfmslkptrGLITIFGKDRSKITRTELPLLRRNIGVVFQDFRLLDHL 94
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILD----------AIGLALGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 95 ttyenvalplrvrgrdestyrsdviellkwvglgermhvlppiLSGGEKQRAAIARALIE---QPRILLA-DEPTGNVDP 170
Cdd:cd03227 78 -------------------------------------------LSGGEKELSALALILALaslKPRPLYIlDEIDRGLDP 114
|
170 180 190
....*....|....*....|....*....|.
gi 1426272298 171 QLARRLLRLLLELNRLGTAVVIATHDLGLMD 201
Cdd:cd03227 115 RDGQALAEAILEHLVKGAQVIVITHLPELAE 145
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-169 |
2.31e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.27 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 17 ILRDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPT--------RGLITIFGKDRSKITRTELPLLRrniGVVFQDF 88
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLR---AVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 89 RLLDHLTTYENVAL---PLRVRGRDESTYRSDVIellkWVGLgERMHVLP------PILSGGEKQRAAIARAL------- 152
Cdd:PRK13547 93 QPAFAFSAREIVLLgryPHARRAGALTHRDGEIA----WQAL-ALAGATAlvgrdvTTLSGGELARVQFARVLaqlwpph 167
|
170
....*....|....*....
gi 1426272298 153 --IEQPRILLADEPTGNVD 169
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALD 186
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
33-49 |
2.52e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 37.76 E-value: 2.52e-03
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
33-49 |
3.42e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 36.97 E-value: 3.42e-03
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-169 |
4.14e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.79 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 2 IRFENVghRYGMGPEIL-RDVSFHLPERSFQFLSGPSGAGKTTLLRLLFMSLKPTRGLITIfGkDRSKItrtelpllrrn 80
Cdd:PRK11819 325 IEAENL--SKSFGDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G-ETVKL----------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 81 iGVVFQdFRllDHL----TTYENVA------------LPLRV-------RGRDEStyrsdviellKWVGLgermhvlppi 137
Cdd:PRK11819 390 -AYVDQ-SR--DALdpnkTVWEEISggldiikvgnreIPSRAyvgrfnfKGGDQQ----------KKVGV---------- 445
|
170 180 190
....*....|....*....|....*....|..
gi 1426272298 138 LSGGEKQRAAIARALIEQPRILLADEPTGNVD 169
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
138-215 |
6.20e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 37.20 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 138 LSGGEKQRAAIARALIEQPRILLADEPTGNVDPQLARRLLRLLLELNRLGTAVVIATHDL----GLMDqvdaRRMVLSGG 213
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLpevlGVAD----RIVVMREG 472
|
..
gi 1426272298 214 RL 215
Cdd:PRK11288 473 RI 474
|
|
| AAA_25 |
pfam13481 |
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins. |
24-154 |
7.18e-03 |
|
AAA domain; This AAA domain is found in a wide variety of presumed DNA repair proteins.
Pssm-ID: 463892 [Multi-domain] Cd Length: 193 Bit Score: 36.20 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1426272298 24 HLPERSFQFLSGPSGAGKTTLlrLLFMSLKPTRGLiTIFGKDRSKITR------TELP--LLRRNIGVVFQDFRLLDHLT 95
Cdd:pfam13481 29 LLPAGGLGLLAGAPGTGKTTL--ALDLAAAVATGK-PWLGGPRVPEQGkvlyvsAEGPadELRRRLRAAGADLDLPARLL 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1426272298 96 -TYENVALPLRVRGRDESTYRSDVIELLKWVGLGE--RMHVLPPI--LSGGEKQRAAIARALIE 154
Cdd:pfam13481 106 fLSLVESLPLFFLDRGGPLLDADVDALEAALEEVEdpDLVVIDPLarALGGDENSNSDVGRLVK 169
|
|
| |
