|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-220 |
6.10e-138 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 385.17 E-value: 6.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ 80
Cdd:COG2884 1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-216 |
5.23e-117 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 332.22 E-value: 5.23e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMY 216
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-214 |
6.76e-106 |
|
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: 303.79 E-value: 6.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
1.45e-95 |
|
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: 277.75 E-value: 1.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQI 81
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
1.54e-88 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 260.36 E-value: 1.54e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGG---HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYV 77
Cdd:COG1136 4 LLELRNLTKSYGTGegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQ-IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKP 156
Cdd:COG1136 84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRyRTLTLKAGRMYS 217
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHDPELAARAD-RVIRLRDGRIVS 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-214 |
8.37e-84 |
|
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: 248.17 E-value: 8.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG---HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQ-IPYV 77
Cdd:cd03255 1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLgLIARMRYRTLTLKAGR 214
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDP-ELAEYADRIIELRDGK 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-220 |
1.50e-74 |
|
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: 225.15 E-value: 1.50e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQ---ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYV 77
Cdd:cd03258 1 MIELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINReLGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-196 |
2.72e-74 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 228.04 E-value: 2.72e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQ---ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYV 77
Cdd:COG1135 1 MIELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHD 196
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINReLGLTIVLITHE 200
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-219 |
8.75e-69 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 214.28 E-value: 8.75e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGG---HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYV 77
Cdd:PRK11153 1 MIELKNISKVFPQGgrtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK11153 81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINReLGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-215 |
4.50e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 206.45 E-value: 4.50e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ 80
Cdd:COG3638 2 MLELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNV---------ALPLVIDGYSHGDINkRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARA 151
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVlagrlgrtsTWRSLLGLFPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLiARmRY--RTLTLKAGRM 215
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDL-AR-RYadRIIGLRDGRV 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-219 |
8.07e-65 |
|
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: 200.25 E-value: 8.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqRSQIPYVRRQI 81
Cdd:COG1122 1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQ--DHRLLMDrTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG1122 78 GLVFQnpDDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADG 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-214 |
3.13e-64 |
|
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: 199.33 E-value: 3.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQI 81
Cdd:cd03256 1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVidGYSH---------GDINKRVA-AALDKVGLLGKERYQPRMLSGGEQQRVGIARA 151
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRL--GRRStwrslfglfPKEEKQRAlAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINReEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-197 |
7.57e-64 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 198.78 E-value: 7.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVY---SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqrsqipyV 77
Cdd:COG1116 7 ALELRGVSKRFptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--------P 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 158 LLLADEPTGNLDPQ----LSMDIMRLFEEFNRfgvSVLIATHDL 197
Cdd:COG1116 159 VLLMDEPFGALDALtrerLQDELLRLWQETGK---TVLFVTHDV 199
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-196 |
3.23e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 199.94 E-value: 3.23e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqIPYvRRQ 80
Cdd:COG3842 5 ALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL----PPE-KRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG3842 79 VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498358447 161 ADEPTGNLDPQL--SM--DIMRLFEEfnrFGVSVLIATHD 196
Cdd:COG3842 159 LDEPLSALDAKLreEMreELRRLQRE---LGITFIYVTHD 195
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-214 |
2.90e-60 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 189.05 E-value: 2.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLV--------IDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAI 152
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHGRLgykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKeDGITVIINLHQVDLAKKYADRIVGLKAGE 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-214 |
4.19e-60 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 187.73 E-value: 4.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqiPYVRRQI 81
Cdd:cd03259 1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-----PPERRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEE-FNRFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:cd03259 155 DEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-214 |
7.60e-60 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 195.89 E-value: 7.60e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVY----SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPY 76
Cdd:COG1123 260 LLEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 VRRQIGMIFQDHRLLMD--RTVFDNVALPLVIDG-YSHGDINKRVAAALDKVGLLGK--ERYqPRMLSGGEQQRVGIARA 151
Cdd:COG1123 340 LRRRVQMVFQDPYSSLNprMTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLPPDlaDRY-PHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-214 |
2.04e-59 |
|
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: 185.75 E-value: 2.04e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 3 RFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQI 81
Cdd:cd03225 1 ELKNLSFSYPDGARpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQ--DHRLLMDrTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03225 78 GLVFQnpDDQFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-215 |
2.06e-57 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 181.92 E-value: 2.06e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVY---SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyv 77
Cdd:COG1124 1 MLEVRNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMD--RTVFDNVALPLVIDGysHGDINKRVAAALDKVGLLGKERYQ-PRMLSGGEQQRVGIARAIVN 154
Cdd:COG1124 78 RRRVQMVFQDPYASLHprHTVDRILAEPLRIHG--LPDREERIAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358447 155 KPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-197 |
2.36e-57 |
|
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: 181.72 E-value: 2.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ 80
Cdd:COG1127 5 MIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVI-DGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDL 197
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDeLGLTSVVVTHDL 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-197 |
2.40e-57 |
|
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: 180.75 E-value: 2.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG---HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDdvshiqrsQIPYVR 78
Cdd:cd03293 1 LEVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--------PVTGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 79 RQIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:cd03293 73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEE-FNRFGVSVLIATHDL 197
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDiWRETGKTVLLVTHDI 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-215 |
4.77e-57 |
|
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: 180.39 E-value: 4.77e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGG---HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYV 77
Cdd:cd03257 1 LLEVKNLSVSFPTGggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMD--RTVFDNVALPLVI--DGYSHGDINKRVAAALDKVGLLGK--ERYqPRMLSGGEQQRVGIARA 151
Cdd:cd03257 81 RKEIQMVFQDPMSSLNprMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEvlNRY-PHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-215 |
6.86e-57 |
|
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: 179.94 E-value: 6.86e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQA---LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYV 77
Cdd:COG4181 8 IIELRGLTKTVGTGAGEltiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQ-IGMIFQDHRLLMDRTVFDNVALPLVIDGysHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKP 156
Cdd:COG4181 88 RARhVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRyRTLTLKAGRM 215
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCD-RVLRLRAGRL 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-202 |
1.48e-55 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 176.72 E-value: 1.48e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVsHIQRSQIPYVRRQ 80
Cdd:COG1126 1 MIEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVAL-PLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498358447 160 LADEPTGNLDPQLS---MDIMR-LFEEfnrfGVSVLIATHDLGLiAR 202
Cdd:COG1126 159 LFDEPTSALDPELVgevLDVMRdLAKE----GMTMVVVTHEMGF-AR 200
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-196 |
1.29e-54 |
|
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: 174.35 E-value: 1.29e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqiPYVRRQI 81
Cdd:cd03300 1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 498358447 162 DEPTGNLDPQL----SMDIMRLFEEfnrFGVSVLIATHD 196
Cdd:cd03300 155 DEPLGALDLKLrkdmQLELKRLQKE---LGITFVFVTHD 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-197 |
6.99e-54 |
|
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: 172.69 E-value: 6.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQI 81
Cdd:cd03261 1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLvidgYSHGD-----INKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKP 156
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPL----REHTRlseeeIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDL 197
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDL 197
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-203 |
1.45e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 171.79 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEM-AFLtGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVshiqRSQIPYVRRQ 80
Cdd:COG1131 1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIfGLL-GPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARM 203
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERL 197
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
1.86e-53 |
|
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: 169.68 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShIQRSQIPYVRRQI 81
Cdd:cd03229 1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLT-DLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLvidgyshgdinkrvaaaldkvgllgkeryqprmlSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-210 |
1.91e-53 |
|
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: 170.49 E-value: 1.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQI-PYVRRQIGMIF 85
Cdd:TIGR03608 4 ISKKF-GDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAsKFRREKLGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 86 QDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498358447 166 GNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLgLIARMRYRTLTL 210
Cdd:TIGR03608 163 GSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP-EVAKQADRVIEL 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-196 |
3.88e-53 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 174.11 E-value: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqiPYVRRQ 80
Cdd:COG3839 3 SLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL-----PPKDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLG-KERYqPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDlLDRK-PKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498358447 160 LADEPTGNLDPQL--SM--DIMRLFEefnRFGVSVLIATHD 196
Cdd:COG3839 156 LLDEPLSNLDAKLrvEMraEIKRLHR---RLGTTTIYVTHD 193
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-220 |
4.28e-53 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 170.44 E-value: 4.28e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSkVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVM-----ERPTDGRVFFHGDDVSHIQRSQIpY 76
Cdd:cd03260 1 IELRDLN-VYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDVL-E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 VRRQIGMIFQdHRLLMDRTVFDNVALPLVIDGY-SHGDINKRVAAALDKVGLLG--KERYQPRMLSGGEQQRVGIARAIV 153
Cdd:cd03260 79 LRRRVGMVFQ-KPNPFPGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 154 NKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-196 |
8.20e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 171.81 E-value: 8.20e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQ 80
Cdd:COG1125 1 MIEFENVTKRYPDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVE---LRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKE---RYqPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEyrdRY-PHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498358447 158 LLLADEPTGNLDP----QLSMDIMRLFEEFNRfgvSVLIATHD 196
Cdd:COG1125 157 ILLMDEPFGALDPitreQLQDELLRLQRELGK---TIVFVTHD 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-215 |
1.55e-52 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 169.23 E-value: 1.55e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYSGGH---QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVR-RQ 80
Cdd:PRK11629 9 DNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRyRTLTLKAGRM 215
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-165 |
1.00e-50 |
|
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: 161.66 E-value: 1.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRsqiPYVRRQIGMIFQDHRLLMDRTVF 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER---KSLRKEIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358447 98 DNVALPLVIDGYSHGDINKRVAAALDKVGLLGKE----RYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-220 |
5.15e-50 |
|
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: 163.29 E-value: 5.15e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:COG1120 1 MLEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL---ARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVAL---PLV--IDGYSHGDInKRVAAALDKVGLLG-KERYQPRmLSGGEQQRVGIARAIVN 154
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDR-EAVEEALERTGLEHlADRPVDE-LSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 155 KPPLLLADEPTGNLDPQLSMDIMRLFEEFNRF-GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-198 |
9.06e-50 |
|
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: 161.16 E-value: 9.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiQRSQIPYVRRQI 81
Cdd:cd03262 1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLV-IDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLG 198
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMG 196
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-215 |
5.51e-49 |
|
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: 160.16 E-value: 5.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQI 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---RRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKE---RYqPRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfadRY-PHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 159 LLADEPTGNLDP----QLSMDIMRLFEEFNRfgvSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03295 157 LLMDEPFGALDPitrdQLQEEFKRLQQELGK---TIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
13-219 |
4.13e-48 |
|
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: 157.60 E-value: 4.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyVRRQIGMIFQDHRLLM 92
Cdd:cd03219 11 GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLGIGRTFQIPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 DRTVFDNVALPLVIDG----------YSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:cd03219 89 ELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 163 EPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03219 169 EPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
5.66e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.51 E-value: 5.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDvshIQRSQIPYVRRQI 81
Cdd:COG4619 1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKP---LSAMPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDrTVFDNVALPLVIDGYSHGDinKRVAAALDKVGL----LGKERYQprmLSGGEQQRVGIARAIVNKPP 157
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFDR--ERALELLERLGLppdiLDKPVER---LSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-220 |
1.49e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.07 E-value: 1.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsgGHQALQkVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQrsqiPYvRRQ 80
Cdd:COG3840 1 MLRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----PA-ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLvidgysHGDIN------KRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVN 154
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLGL------RPGLKltaeqrAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 155 KPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:COG3840 147 KRPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-219 |
2.51e-46 |
|
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: 160.07 E-value: 2.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGG-HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPT---DGRVFFHGDDVSHIQRSQIpy 76
Cdd:COG1123 4 LLEVRDLSVRYPGGdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 vRRQIGMIFQDHRL-LMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNK 155
Cdd:COG1123 82 -GRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 156 PPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDG 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-219 |
6.85e-46 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.17 E-value: 6.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiQRSQIPYV--R 78
Cdd:COG1121 6 AIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-ARRRIGYVpqR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 79 RQIgmifqdhrllmDR----TVFDNVALPLV-----IDGYSHGDiNKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIA 149
Cdd:COG1121 84 AEV-----------DWdfpiTVRDVVLMGRYgrrglFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 150 RAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLkAGRMYSSG 219
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHG 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
17-219 |
7.27e-46 |
|
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: 153.18 E-value: 7.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ-IGMIFQDHRLLMDRT 95
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP----Q 171
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirrE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498358447 172 LSMDIMRLFEEFNRfgvSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03294 199 MQDELLRLQAELQK---TIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-219 |
1.05e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 151.78 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiQRSQIPYVRRQ 80
Cdd:PRK09493 1 MIEFKNVSKHF-GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVAL-PLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDG 218
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-197 |
7.08e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.61 E-value: 7.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqrSQIPYVRRQI 81
Cdd:COG1118 3 IEVRNISKRF-GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLG-KERYqPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGlADRY-PSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 498358447 161 ADEPTGNLDPQLSMDIMR-LFEEFNRFGVSVLIATHDL 197
Cdd:COG1118 157 LDEPFGALDAKVRKELRRwLRRLHDELGGTTVFVTHDQ 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
9-215 |
1.17e-44 |
|
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: 151.36 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 9 KVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERP---TDGRVFFHGDDVSHIQRSQIPYVR-RQIGMI 84
Cdd:COG0444 12 PTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRgREIQMI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 85 FQDHrllMD-----RTVFDNVALPLVI-DGYSHGDINKRVAAALDKVGLLGKE----RYqPRMLSGGEQQRVGIARAIVN 154
Cdd:COG0444 92 FQDP---MTslnpvMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPErrldRY-PHELSGGMRQRVMIARALAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358447 155 KPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:COG0444 168 EPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-196 |
1.83e-44 |
|
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: 148.64 E-value: 1.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqrsqIPYVRRQI 81
Cdd:cd03296 3 IEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-----VPVQERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVI----DGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHD 196
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHD 196
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-214 |
2.39e-44 |
|
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: 147.24 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVshiqRSQIPYVRRQ 80
Cdd:COG4133 2 MLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDInkRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIArmRYRTLTLKAGR 214
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
2.96e-44 |
|
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: 145.60 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG-HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipYVRRQ 80
Cdd:cd03228 1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE---SLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHrLLMDRTVFDNValplvidgyshgdinkrvaaaldkvgllgkeryqprmLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03228 78 IAYVPQDP-FLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRyRTLTLKAGR 214
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDAD-RIIVLDDGR 171
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-196 |
5.22e-44 |
|
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: 146.63 E-value: 5.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQrsqiPYvRRQI 81
Cdd:cd03301 1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP----PK-DRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRV---AAALDKVGLLgkERYqPRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVrevAELLQIEHLL--DRK-PKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498358447 159 LLADEPTGNLDPQLSMDiMRlfEEFNRF----GVSVLIATHD 196
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQ-MR--AELKRLqqrlGTTTIYVTHD 190
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-198 |
1.65e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 148.73 E-value: 1.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQDH------R 89
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQDPyaslnpR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 90 LlmdrTVFDNVALPLVIDG-YSHGDINKRVAAALDKVGLLGK--ERYqPRMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:COG4608 112 M----TVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEhaDRY-PHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180 190
....*....|....*....|....*....|...
gi 498358447 167 NLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLG 198
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLqDELGLTYLFISHDLS 219
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
11-222 |
2.54e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 146.76 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 11 YSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPyVRRQIGMIFQ--DH 88
Cdd:PRK13639 11 YPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLE-VRKTVGIVFQnpDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLMDrTVFDNVAL-PLVIdGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:PRK13639 90 QLFAP-TVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 168 LDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK13639 168 LDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPK 222
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-220 |
2.69e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 146.83 E-value: 2.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG----HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYV 77
Cdd:TIGR04521 1 IKLKNVSYIYQPGtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQ--DHRLLMDrTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlgKERYQ---PRMLSGGEQQRVGIARAI 152
Cdd:TIGR04521 81 RKKVGLVFQfpEHQLFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGL--DEEYLersPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
1.05e-42 |
|
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: 141.23 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 3 RFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQIG 82
Cdd:cd00267 1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE---LRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQdhrllmdrtvfdnvalplvidgyshgdinkrvaaaldkvgllgkeryqprmLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498358447 163 EPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-197 |
2.09e-42 |
|
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: 144.11 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGH-QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqRSQIPYVRRQ 80
Cdd:TIGR04520 1 IEVENVSFSYPESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQ--DHRLLmDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:TIGR04520 79 VGMVFQnpDNQFV-GATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDL 197
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDM 197
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-219 |
6.63e-42 |
|
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: 150.37 E-value: 6.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQ 80
Cdd:COG2274 474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAS---LRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLlMDRTVFDNVALplvidgySHGDIN-KRVAAALDKVGLLGKERYQP-----------RMLSGGEQQRVGI 148
Cdd:COG2274 551 IGVVLQDVFL-FSGTIRENITL-------GDPDATdEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 149 ARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRyRTLTLKAGRMYSSG 219
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLAD-RIIVLDKGRIVEDG 691
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-202 |
1.54e-41 |
|
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: 141.33 E-value: 1.54e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyVRRQ 80
Cdd:COG0411 4 LLEVRGLTKRF-GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--ARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVA---------------LPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQR 145
Cdd:COG0411 81 IARTFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 146 VGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIAR 202
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMG 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
4.19e-41 |
|
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: 137.91 E-value: 4.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVshiqRSQIPYVRRQI 81
Cdd:cd03230 1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNValplvidgyshgdinkrvaaaldkvgllgkeryqprMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03230 76 GYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-214 |
4.40e-41 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 146.83 E-value: 4.40e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQI 81
Cdd:COG4988 337 IELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---RRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDrTVFDNVALplvidgYSHGDINKRVAAALDKVGLLGKERYQP-----------RMLSGGEQQRVGIAR 150
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRL------GRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 151 AIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRyRTLTLKAGR 214
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALLAQAD-RILVLDDGR 548
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
5-196 |
5.17e-41 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 142.87 E-value: 5.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqiPYVRRQIGMI 84
Cdd:TIGR03265 8 DNIRKRF-GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRL-----PPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 85 FQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEP 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 498358447 165 TGNLDPQ----LSMDIMRLFEefnRFGVSVLIATHD 196
Cdd:TIGR03265 162 LSALDARvrehLRTEIRQLQR---RLGVTTIMVTHD 194
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-219 |
8.24e-41 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 139.38 E-value: 8.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHG---DDVSHIQRSQIPYVR 78
Cdd:COG4161 3 IQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfDFSQKPSEKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 79 RQIGMIFQDHRLLMDRTVFDN-VALPLVIDGYSHGDINKRVAAALDKVGLLGK-ERYqPRMLSGGEQQRVGIARAIVNKP 156
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKaDRF-PLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-215 |
1.04e-40 |
|
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: 138.84 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVshiqRSQIPYVRRQ 80
Cdd:COG4555 1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV----RKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-220 |
2.16e-40 |
|
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: 137.85 E-value: 2.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqrsQIPYVRRQIGMIFQDHRLLMDRTVF 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-----NLPPEKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 98 DNVALPLVIDGYSHGDINKRV---AAALDKVGLLGKeryQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSM 174
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERKVleiAEMLGIDHLLNR---KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498358447 175 DIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:cd03299 167 KLREELKKIRKeFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGK 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-213 |
2.86e-40 |
|
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: 136.62 E-value: 2.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 3 RFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRsqipyvRRQIG 82
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER------RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQD--HRLLMDrTVFDNVALPLviDGYShgDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03226 75 YVMQDvdYQLFTD-SVREELLLGL--KELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 161 ADEPTGNLDPQlSMD-IMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAG 213
Cdd:cd03226 150 FDEPTSGLDYK-NMErVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-219 |
3.19e-40 |
|
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: 135.64 E-value: 3.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQIGMIFQdhrllm 92
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---ARKIAYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 drtvfdnvalplvidgyshgdinkrvaaALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQL 172
Cdd:cd03214 81 ----------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498358447 173 SMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03214 133 QIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-219 |
3.33e-40 |
|
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: 136.85 E-value: 3.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsgGHQALQkVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqiPYVRRQI 81
Cdd:cd03298 1 VRLDKIRFSY--GEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA-----PPADRPV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03298 73 SMLFQENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-219 |
6.85e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 137.07 E-value: 6.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGD--DVS-HIQRSQIPYVR 78
Cdd:PRK11124 3 IQLNGINCFY-GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSkTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 79 RQIGMIFQDHRLLMDRTVFDN-VALPLVIDGYSHGDINKRVAAALDKVGLLGK-ERYqPRMLSGGEQQRVGIARAIVNKP 156
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYaDRF-PLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-200 |
1.27e-39 |
|
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: 135.35 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqrsqipYVRRQIGMIFQdhRLLM 92
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGYVPQ--RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 DR----TVFDNVALPLV-----IDGYSHGDInKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:cd03235 80 DRdfpiSVRDVVLMGLYghkglFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 498358447 164 PTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLI 200
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLV 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-172 |
1.77e-39 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 139.31 E-value: 1.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEmaFLT--GHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqiPYVRR 79
Cdd:PRK09452 15 VELRGISKSF-DGKEVISNLDLTINNGE--FLTllGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV-----PAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVL 166
|
170
....*....|...
gi 498358447 160 LADEPTGNLDPQL 172
Cdd:PRK09452 167 LLDESLSALDYKL 179
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
33-222 |
4.74e-39 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 136.85 E-value: 4.74e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 33 LTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqiPYVRRQIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHG 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV-----PPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 113 DINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD----PQLSMDIMRLFEefnRFGV 188
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQE---QLGI 152
|
170 180 190
....*....|....*....|....*....|....
gi 498358447 189 SVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPE 186
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-196 |
4.76e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 137.52 E-value: 4.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyvrRQI 81
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD-----RKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVI----DGYSHGDINKRVAAALDKVGL--LGkERYqPRMLSGGEQQRVGIARAIVNK 155
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLahLA-DRY-PAQLSGGQKQRVALARALAVE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498358447 156 PPLLLADEPTGNLDPQLSMDIMR----LFEEFNRFGVSVliaTHD 196
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRwlrqLHEELKFTSVFV---THD 196
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-222 |
6.79e-39 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 134.49 E-value: 6.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGgHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVF---FHGDDVSHI--QRSQIP 75
Cdd:PRK11264 3 AIEVKNLVKKFHG-QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgdITIDTARSLsqQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 76 YVRRQIGMIFQDHRLLMDRTVFDNVAL-PLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVN 154
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 155 KPPLLLADEPTGNLDPQLSMDIM---RLFEEFNRfgvSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLntiRQLAQEKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-214 |
1.17e-38 |
|
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: 140.29 E-value: 1.17e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQ 80
Cdd:COG4987 334 LELEDVSFRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDrTVFDN--VALPLVIDGyshgdinkRVAAALDKVGLLGKERYQP-----------RMLSGGEQQRVG 147
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENlrLARPDATDE--------ELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRyRTLTLKAGR 214
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERMD-RILVLEDGR 546
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-221 |
1.25e-38 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 134.22 E-value: 1.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGG---HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqrsqiPYV 77
Cdd:COG4525 3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG------PGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRqiGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:COG4525 77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 158 LLLADEPTGNLDpQLSMDIMR--LFEEFNRFGVSVLIATHDL-----------------GLIArmryRTLTLKAGRMYSS 218
Cdd:COG4525 155 FLLMDEPFGALD-ALTREQMQelLLDVWQRTGKGVFLITHSVeealflatrlvvmspgpGRIV----ERLELDFSRRFLA 229
|
...
gi 498358447 219 GED 221
Cdd:COG4525 230 GED 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-203 |
1.84e-38 |
|
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: 139.34 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQdHRLLMDRTVFDNVALplvidgYSHGDINKRVAAALDKVGLLGKERYQP-----------RMLSGGEQQRVGIAR 150
Cdd:TIGR02857 399 AWVPQ-HPFLFAGTIAENIRL------ARPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 151 AIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARM 203
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALA 523
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-220 |
3.20e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 136.12 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYSGGHqALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQrsqiPYvRRQIGMIFQ 86
Cdd:PRK11607 25 LTKSFDGQH-AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP----PY-QRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 87 DHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 167 NLDPQLSmDIMRL--FEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK11607 179 ALDKKLR-DRMQLevVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-200 |
3.41e-38 |
|
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: 131.01 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 11 YSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiQRSQIPYVRRQIGMIFQD-HR 89
Cdd:TIGR01166 1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDY-SRKGLLERRQRVGLVFQDpDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 90 LLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 498358447 170 PQLSMDIMRLFEEFNRFGVSVLIATHDLGLI 200
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
13-202 |
8.50e-38 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 131.85 E-value: 8.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQ----------RSQIPYVRRQIG 82
Cdd:COG4598 19 GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvpadRRQLQRIRTRLG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQDHRLLMDRTVFDNVAL-PLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:COG4598 99 MVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498358447 162 DEPTGNLDPQLSMD---IMR-LFEEfnrfGVSVLIATHDLGLiAR 202
Cdd:COG4598 179 DEPTSALDPELVGEvlkVMRdLAEE----GRTMLVVTHEMGF-AR 218
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
12-219 |
1.44e-37 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 134.21 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 12 SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRR-QIGMIFQDHRL 90
Cdd:TIGR01186 3 TGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRRkKIGMVFQQFAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 LMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:TIGR01186 83 FPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 171 QLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:TIGR01186 163 LIRDSMQDELKKLQAtLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVG 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
13-196 |
1.88e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 133.31 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSH--IQRsqipyvrRQIGMIFQDHRL 90
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsIQQ-------RDICMVFQSYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 LMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLG-KERYQPRmLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGfEDRYVDQ-ISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190
....*....|....*....|....*....|
gi 498358447 170 PQL--SM-DIMRLFEEfnRFGVSVLIATHD 196
Cdd:PRK11432 169 ANLrrSMrEKIRELQQ--QFNITSLYVTHD 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-219 |
3.26e-37 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 130.28 E-value: 3.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSkVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPyvrRQ 80
Cdd:PRK13548 2 MLEARNLS-VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLvidgYSHGDINKR----VAAALDKVGLLG-KERYQPRmLSGGEQQRVGIARAIV-- 153
Cdd:PRK13548 78 RAVLPQHSSLSFPFTVEEVVAMGR----APHGLSRAEddalVAAALAQVDLAHlAGRDYPQ-LSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 154 ----NKPPLLLADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-219 |
3.49e-37 |
|
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: 129.16 E-value: 3.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG-HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVshiqRSQIPYVRRQ 80
Cdd:cd03263 1 LQIRNLTKTYKKGtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI----RTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFnRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-215 |
5.74e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 129.93 E-value: 5.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGG--------HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRS 72
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 73 QIPYVRRQIGMIFQDHRLLMD--RTVFDNVALPLV-IDGYSHGDINKRVAAALDKVGLLGKE-RYQPRMLSGGEQQRVGI 148
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNprMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDaDKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 149 ARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
10-219 |
6.98e-37 |
|
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: 128.32 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 10 VYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyVRRQIGMIFQDHR 89
Cdd:cd03224 8 AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 90 LLMDRTVFDNvaLPLVIDGYSHGDINKRVAAALDKVGLLGKERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNL 168
Cdd:cd03224 86 IFPELTVEEN--LLLGAYARRRAKRKARLERVYELFPRLKERRKQLaGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498358447 169 DPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03224 164 APKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-215 |
8.38e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 129.81 E-value: 8.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 12 SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQDHRLL 91
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 92 MD--RTVFDNVALPLV-IDGYSHGDINKRVAAALDKVGL-LGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:PRK10419 102 VNprKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498358447 168 LDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-217 |
8.70e-37 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 135.62 E-value: 8.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYSGGHQA---LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ-IG 82
Cdd:PRK10535 10 IRRSYPSGEEQvevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:PRK10535 90 FIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 163 EPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDlGLIARMRYRTLTLKAGRMYS 217
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVR 223
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-203 |
1.84e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 134.14 E-value: 1.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQI 81
Cdd:COG1132 340 IEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LRRQI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHrLLMDRTVFDNVALplvidgyshGDIN---KRVAAALDKVGLLG-----KERYQ----PR--MLSGGEQQRVG 147
Cdd:COG1132 417 GVVPQDT-FLFSGTIRENIRY---------GRPDatdEEVEEAAKAAQAHEfiealPDGYDtvvgERgvNLSGGQRQRIA 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARM 203
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTIRNA 541
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-197 |
3.12e-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: 3.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipyVRRQI 81
Cdd:cd03265 1 IEVENLVKKY-GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE----VRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDL 197
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYM 192
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
13-219 |
3.69e-36 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 127.78 E-value: 3.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQ----------RSQIPYVRRQIG 82
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkvadKNQLRLLRTRLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQDHRLLMDRTVFDNV-ALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQ-PRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK10619 96 MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
10-215 |
4.58e-36 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 126.82 E-value: 4.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 10 VYSGGHQ--ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVR-RQIGMIFQ 86
Cdd:PRK10584 16 VGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 87 DHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:PRK10584 96 SFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 167 NLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRyRTLTLKAGRM 215
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNReHGTTLILVTHDLQLAARCD-RRLRLVNGQL 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-215 |
6.84e-36 |
|
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: 125.41 E-value: 6.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRsqipyVRRQIGMIFQ 86
Cdd:cd03268 6 LTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----ALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 87 DHRLLMDRTVFDNvalpLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:cd03268 80 APGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498358447 167 NLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-220 |
7.84e-36 |
|
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: 132.12 E-value: 7.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTL----LKLIsvmerPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQD- 87
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 88 -----HRLlmdrTVFDNVALPLVI--DGYSHGDINKRVAAALDKVGLLG--KERYqPRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:COG4172 372 fgslsPRM----TVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLDPaaRHRY-PHEFSGGQRQRIAIARALILEPKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:COG4172 447 LVLDEPTSALDVSVQAQILDLLRDLQrEHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGP 509
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-214 |
2.31e-35 |
|
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: 124.85 E-value: 2.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYS----GGHQ--ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGD----DVSHIQ 70
Cdd:COG4778 4 LLEVENLSKTFTlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 71 RSQIPYVRRQ-IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlgKER----YqPRMLSGGEQQR 145
Cdd:COG4778 84 PREILALRRRtIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL--PERlwdlP-PATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 146 VGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
13-220 |
3.47e-35 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 130.19 E-value: 3.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKS----TLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVR-RQIGMIFQD 87
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 88 --------HrllmdrTVFDNVALPLVI-DGYSHGDINKRVAAALDKVGLLGKER----YqPRMLSGGEQQRVGIARAIVN 154
Cdd:COG4172 101 pmtslnplH------TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERrldaY-PHQLSGGQRQRVMIAMALAN 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 155 KPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:COG4172 174 EPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
18-222 |
3.59e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 125.61 E-value: 3.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqRSQIPYVRRQIGMIFQ--DHRLLmDRT 95
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDIRHKIGMVFQnpDNQFV-GAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMD 175
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498358447 176 IMRLFEEF-NRFGVSVLIATHDLGLIArMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK13650 179 LIKTIKGIrDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPR 225
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-219 |
8.06e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 124.07 E-value: 8.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSkVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPyvrRQ 80
Cdd:COG4559 1 MLEAENLS-VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA---RR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLG-KER-YQprMLSGGEQQRVGIARAIV----- 153
Cdd:COG4559 77 RAVLPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRsYQ--TLSGGEQQRVQLARVLAqlwep 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 154 --NKPPLLLADEPTGNLDP--QLSmdIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:COG4559 155 vdGGPRWLFLDEPTSALDLahQHA--VLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
1.93e-34 |
|
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: 121.92 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHqALQKVSFHLRKGeMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVshiqRSQIPYVRRQI 81
Cdd:cd03264 1 LQLENLTKRYGKKR-ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 162 DEPTGNLDPqlsmdimrlfEEFNRF---------GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03264 155 DEPTAGLDP----------EERIRFrnllselgeDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
11-222 |
2.17e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 123.69 E-value: 2.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 11 YSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqRSQIPYVRRQIGMIFQD-HR 89
Cdd:PRK13647 14 YKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKWVRSKVGLVFQDpDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 90 LLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK13647 91 QVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 170 PQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK13647 171 PRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-197 |
2.81e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.84 E-value: 2.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 10 VYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLK-------LISVMErpTDGRVFFHGDDVSHIQRSQIpYVRRQIG 82
Cdd:COG1117 19 VYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDIYDPDVDVV-ELRRRVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQdhrllmdR------TVFDNVALPLVIDGY-SHGDINKRVAAALDKVGLLG--KER-YQPRM-LSGGEQQRVGIARA 151
Cdd:COG1117 96 MVFQ-------KpnpfpkSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALWDevKDRlKKSALgLSGGQQQRLCIARA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEF-NRFgvSVLIATHDL 197
Cdd:COG1117 169 LAVEPEVLLMDEPTSALDPISTAKIEELILELkKDY--TIVIVTHNM 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-219 |
3.31e-34 |
|
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: 124.83 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 21 VSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQ-IPYVRRQIGMIFQDHRLLMDRTVFDN 99
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIfLPPHRRRIGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 100 VAlplviDGYSHGDINKRVAAALDKVGLLGKE----RYqPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMD 175
Cdd:COG4148 98 LL-----YGRKRAPRAERRISFDEVVELLGIGhlldRR-PATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498358447 176 IM----RLFEEFNrfgVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:COG4148 172 ILpyleRLRDELD---IPILYVSHSLDEVARLADHVVLLEQGRVVASG 216
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-196 |
3.89e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 121.05 E-value: 3.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSkVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERP---TDGRVFFHGDDVSHIqrsqiPYV 77
Cdd:COG4136 1 MLSLENLT-ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTAL-----PAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRTVFDNV--ALPlviDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNK 155
Cdd:COG4136 75 QRRIGILFQDDLLFPHLSVGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498358447 156 PPLLLADEPTGNLDPQLSMDIMRL-FEEFNRFGVSVLIATHD 196
Cdd:COG4136 152 PRALLLDEPFSKLDAALRAQFREFvFEQIRQRGIPALLVTHD 193
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
9-207 |
7.46e-34 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 121.25 E-value: 7.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 9 KVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTD-----GRVFFHGDDVSHiQRSQIPYVRRQIGM 83
Cdd:TIGR00972 8 NLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVPgvrieGKVLFDGQDIYD-KKIDVVELRRRVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 84 IFQdHRLLMDRTVFDNVALPLVIDGY-SHGDINKRVAAALDKVGLLG--KERYQ--PRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:TIGR00972 87 VFQ-KPNPFPMSIYDNIAYGPRLHGIkDKKELDEIVEESLKKAALWDevKDRLHdsALGLSGGQQQRLCIARALAVEPEV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFnRFGVSVLIATHDLGLIARMRYRT 207
Cdd:TIGR00972 166 LLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISDRT 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-192 |
1.98e-33 |
|
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: 120.09 E-value: 1.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSkVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyVRRQ 80
Cdd:COG0410 3 MLEVENLH-AGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNvalpLVIDGYSHGDiNKRVAAALDKV-GL---LGKERYQP-RMLSGGEQQRVGIARAIVNK 155
Cdd:COG0410 80 IGYVPEGRRIFPSLTVEEN----LLLGAYARRD-RAEVRADLERVyELfprLKERRRQRaGTLSGGEQQMLAIGRALMSR 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 498358447 156 PPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLI 192
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILL 191
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-219 |
2.40e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.89 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVffhgdDVSHIQRSQ--IPYVR 78
Cdd:PRK13635 6 IRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI-----TVGGMVLSEetVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 79 RQIGMIFQ--DHRLLmDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKP 156
Cdd:PRK13635 81 RQVGMVFQnpDNQFV-GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRyRTLTLKAGRMYSSG 219
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEAAQAD-RVIVMNKGEILEEG 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-219 |
3.69e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 120.61 E-value: 3.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSG----GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFhGDDV--SHIQRSQI 74
Cdd:PRK13643 1 MIKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVvsSTSKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 75 PYVRRQIGMIFQ-DHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlGKERYQ--PRMLSGGEQQRVGIARA 151
Cdd:PRK13643 80 KPVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGL-ADEFWEksPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-214 |
4.04e-33 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 119.78 E-value: 4.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqipyvRRQIGMI 84
Cdd:PRK11247 16 NAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA--------REDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 85 FQDHRLLMDRTVFDNVALPLvidgysHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498358447 165 TGNLDPQLSMDIMRLFEE-FNRFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:PRK11247 161 LGALDALTRIEMQDLIESlWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
7.18e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.47 E-value: 7.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRR 79
Cdd:PRK13648 7 IIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQD-HRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK13648 84 HIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYrTLTLKAGRMYSSG 219
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSeHNITIISITHDLSEAMEADH-VIVMNKGTVYKEG 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-197 |
1.31e-32 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 119.42 E-value: 1.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 9 KVYsGGHQALQKVSFHLRKGE-MAFLtGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqrSQIPYVRRQIGMIFQD 87
Cdd:TIGR01188 1 KVY-GDFKAVDGVNFKVREGEvFGFL-GPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV----REPRKVRRSIGIVPQY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 88 HRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:TIGR01188 75 ASVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTG 154
|
170 180 190
....*....|....*....|....*....|
gi 498358447 168 LDPQLSMDIMRLFEEFNRFGVSVLIATHDL 197
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHYM 184
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-196 |
1.79e-32 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 120.33 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyvrRQ 80
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAAldkVGLLGKERY---QPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEA---ARILELEPLldrKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498358447 158 LLLADEPTGNLDPQL--SM--DIMRLFEefnRFGVSVLIATHD 196
Cdd:PRK11650 155 VFLFDEPLSNLDAKLrvQMrlEIQRLHR---RLKTTSLYVTHD 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-195 |
2.51e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.27 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQ-----ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrSQIP 75
Cdd:PRK13633 4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 76 YVRRQIGMIFQ--DHRLLMDrTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIV 153
Cdd:PRK13633 82 DIRNKAGMVFQnpDNQIVAT-IVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498358447 154 NKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATH 195
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKkYGITIILITH 203
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-201 |
4.96e-32 |
|
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: 116.18 E-value: 4.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsQIPYVRRQI 81
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV---TLDSLRRAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDrTVFDNVAlplvidgYSHGD------INKRVAAALDKVGLLGKERYQPR------MLSGGEQQRVGIA 149
Cdd:cd03253 78 GVVPQDTVLFND-TIGYNIR-------YGRPDatdeevIEAAKAAQIHDKIMRFPDGYDTIvgerglKLSGGEKQRVAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498358447 150 RAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIAtHDLGLIA 201
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIV 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-220 |
8.13e-32 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 116.34 E-value: 8.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqrsqiPYVRRq 80
Cdd:PRK11248 1 MLQISHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG------PGAER- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 iGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 161 ADEPTGNLDP----QLSMDIMRLFEEfnrFGVSVLIATHD----------LGLIA----RMRYRtLTLKAGRMYSSGE 220
Cdd:PRK11248 152 LDEPFGALDAftreQMQTLLLKLWQE---TGKQVLLITHDieeavfmateLVLLSpgpgRVVER-LPLNFARRFVAGE 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-222 |
8.77e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 117.89 E-value: 8.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQD--HRLLMD 93
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 94 RTVFDNVALPLVIdgY----SHGDINKRVAAALDKVGLLGK--ERYqPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:PRK15079 115 MTIGEIIAEPLRT--YhpklSRQEVKDRVKAMMLKVGLLPNliNRY-PHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 168 LDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQReMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-222 |
9.31e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 117.07 E-value: 9.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG----HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiQRSQIPYV 77
Cdd:PRK13637 3 IKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQ--DHRLLmDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlGKERYQ---PRMLSGGEQQRVGIARAI 152
Cdd:PRK13637 82 RKKVGLVFQypEYQLF-EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGL-DYEDYKdksPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHkEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-219 |
1.18e-31 |
|
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: 114.70 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 20 KVSFHLrKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHG---DDVShiQRSQIPYVRRQIGMIFQDHRLLMDRTV 96
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSR--KKINLPPQQRKIGLVFQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 FDNVALPLviDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDI 176
Cdd:cd03297 93 RENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 177 MRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03297 171 LPELKQIkKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-197 |
1.41e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.24 E-value: 1.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqRSQIPYVRR 79
Cdd:PRK13632 7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQ--DHRLLmDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK13632 84 KIGIIFQnpDNQFI-GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIA-THDL 197
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDM 203
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-220 |
3.48e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 115.08 E-value: 3.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrSQIPYVRRQ 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDF--SKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQD-HRLLMDRTV-----F--DNVALPLVidgyshgDINKRVAAALDKVGlLGKERYQ-PRMLSGGEQQRVGIARA 151
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVeedlaFgpENLCLPPI-------EIRKRVDRALAEIG-LEKYRHRsPKTLSGGQGQCVALAGI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIaRMRYRTLTLKAGRMYSSGE 220
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGE 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-197 |
3.64e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.97 E-value: 3.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGE-MAfLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDV--SHIQRSQipyv 77
Cdd:COG1129 4 LLEMRGISKSF-GGVKALDGVSLELRPGEvHA-LLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfRSPRDAQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRTVFDNVAL------PLVIDgysHGDINKRVAAALDKVGLlgkeRYQPRM----LSGGEQQRVG 147
Cdd:COG1129 78 AAGIAIIHQELNLVPNLSVAENIFLgreprrGGLID---WRAMRRRARELLARLGL----DIDPDTpvgdLSVAQQQLVE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQlsmDIMRLFEEFNRF---GVSVLIATHDL 197
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTER---EVERLFRIIRRLkaqGVAIIYISHRL 200
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-200 |
3.74e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 116.22 E-value: 3.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQD--HRLLMD 93
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpyGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 94 RTVFDNVALPLVIdgysHGDINK-----RVAAALDKVGlLGKERYQ--PRMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:PRK11308 109 KKVGQILEEPLLI----NTSLSAaerreKALAMMAKVG-LRPEHYDryPHMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190
....*....|....*....|....*....|....*
gi 498358447 167 NLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLI 200
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQeLGLSYVFISHDLSVV 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-219 |
4.62e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 116.75 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 20 KVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDV-SHIQRSQIPYVRRQIGMIFQDHRLLMDRTVFD 98
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 99 NVALplvidGYSHGDINKRVAAALDKVGLLGKE---RYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMD 175
Cdd:TIGR02142 95 NLRY-----GMKRARPSERRISFERVIELLGIGhllGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498358447 176 IMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:TIGR02142 170 ILPYLERLHAeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAG 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-219 |
5.79e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 114.94 E-value: 5.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 11 YSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiQRSQIPYVRRQIGMIFQ--DH 88
Cdd:PRK13636 15 YSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDY-SRKGLMKLRESVGMVFQdpDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLmDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNL 168
Cdd:PRK13636 94 QLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498358447 169 DPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13636 173 DPMGVSEIMKLLVEMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQG 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-197 |
1.16e-30 |
|
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: 112.56 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqrsqiPYVRRQIgmIFQDHRLLMDRTVF 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE------PGPDRMV--VFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 98 DNVALPL--VIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP----Q 171
Cdd:TIGR01184 73 ENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgN 152
|
170 180
....*....|....*....|....*.
gi 498358447 172 LSMDIMRLFEEfnrFGVSVLIATHDL 197
Cdd:TIGR01184 153 LQEELMQIWEE---HRVTVLMVTHDV 175
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-220 |
1.90e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.98 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSggHQALQkVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIqrsqiPYVRRQ 80
Cdd:PRK10771 1 MLKLTDITWLYH--HLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT-----PPSRRP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVAL---P-LVIDGYSHgdinKRVAAALDKVGLlgkERYQPRM---LSGGEQQRVGIARAIV 153
Cdd:PRK10771 73 VSMLFQENNLFSHLTVAQNIGLglnPgLKLNAAQR----EKLHAIARQMGI---EDLLARLpgqLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 154 NKPPLLLADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-219 |
2.31e-30 |
|
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: 111.53 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG-HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:cd03245 3 IEFRNVSFSYPNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDrTVFDNVALplvidGYSHGDiNKRVAAALDKVGLLGKERYQP-----------RMLSGGEQQRVGIA 149
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNITL-----GAPLAD-DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498358447 150 RAIVNKPPLLLADEPTGNLDPQLSmdiMRLFEEFNRF--GVSVLIATHDLGLIArMRYRTLTLKAGRMYSSG 219
Cdd:cd03245 153 RALLNDPPILLLDEPTSAMDMNSE---ERLKERLRQLlgDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-202 |
4.46e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 110.02 E-value: 4.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDD-VSHI-QRSQIP-----YVRRQIGMIF 85
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArVAYVpQRSEVPdslplTVRDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 86 QDHRLLMDRtvfdnvalplvidgYSHGDiNKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:NF040873 83 WARRGLWRR--------------LTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 498358447 166 GNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIAR 202
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR 184
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
13-197 |
6.20e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 111.78 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQDHRLLM 92
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 DRTVFDNVALPLvidgYSHGD-----INKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:PRK11831 98 DMNVFDNVAYPL----REHTQlpaplLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190
....*....|....*....|....*....|..
gi 498358447 168 LDPqLSMDIM-RLFEEFNR-FGVSVLIATHDL 197
Cdd:PRK11831 174 QDP-ITMGVLvKLISELNSaLGVTCVVVSHDV 204
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
16-220 |
6.36e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 111.47 E-value: 6.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDdvsHIQRSQIPYVRRQIGMIFQDhrllmdrt 95
Cdd:COG4167 27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGDYKYRCKHIRMIFQD-------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 vfDNVAL------------PLVID-GYSHGDINKRVAAALDKVGLLGKER-YQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:COG4167 96 --PNTSLnprlnigqileePLRLNtDLTAEEREERIFATLRLVGLLPEHAnFYPHMLSSGQKQRVALARALILQPKIIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:COG4167 174 DEALAALDMSVRSQIINLMLELQeKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-215 |
1.08e-29 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 109.68 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqrsqiPYVRRQI 81
Cdd:cd03269 1 LEVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-------IAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 162 DEPTGNLDP---QLSMDIMRlfeEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03269 153 DEPFSGLDPvnvELLKDVIR---ELARAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-169 |
1.38e-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: 110.01 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSG-GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:cd03251 1 VEFKNVTFRYPGdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL---RRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDhRLLMDRTVFDNVALPLviDGYSHGDINK--RVAAALDKVGLLgKERYQPRM------LSGGEQQRVGIARAI 152
Cdd:cd03251 78 IGLVSQD-VFLFNDTVAENIAYGR--PGATREEVEEaaRAANAHEFIMEL-PEGYDTVIgergvkLSGGQRQRIAIARAL 153
|
170
....*....|....*..
gi 498358447 153 VNKPPLLLADEPTGNLD 169
Cdd:cd03251 154 LKDPPILILDEATSALD 170
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-195 |
1.46e-29 |
|
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: 109.94 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQrsqiPYVRRQI 81
Cdd:cd03218 1 LRAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLP----MHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIF--QDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlGKERYQPRM-LSGGEQQRVGIARAIVNKPPL 158
Cdd:cd03218 76 GIGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASsLSGGERRRVEIARALATNPKF 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATH 195
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH 191
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-215 |
1.47e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 1.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG----HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDV-SHIQRSQIPY 76
Cdd:PRK13641 3 IKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 VRRQIGMIFQ-DHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlgKER---YQPRMLSGGEQQRVGIARAI 152
Cdd:PRK13641 83 LRKKVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGL--SEDlisKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
2.24e-29 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 107.69 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQA-LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:cd03246 1 LEVENVSFRYPGAEPPvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---GDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLmDRTVFDNValplvidgyshgdinkrvaaaldkvgllgkeryqprmLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03246 78 VGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRyRTLTLKAGRM 215
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASAD-RILVLEDGRV 173
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-219 |
3.43e-29 |
|
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: 109.11 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSG-GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipYVRRQ 80
Cdd:cd03252 1 ITFEHVRFRYKPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA---WLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHrLLMDRTVFDNVALplvidGYSHGDINKRVAAAldkvGLLGKERYQPRM--------------LSGGEQQRV 146
Cdd:cd03252 78 VGVVLQEN-VLFNRSIRDNIAL-----ADPGMSMERVIEAA----KLAGAHDFISELpegydtivgeqgagLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 147 GIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIaRMRYRTLTLKAGRMYSSG 219
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQG 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-202 |
4.02e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 109.49 E-value: 4.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 10 VYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMER--PT---DGRVFFHGDDV--SHIQRSQipyVRRQIG 82
Cdd:PRK14243 18 VYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVE---VRRRIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQDHRLLmDRTVFDNVALPLVIDGYShGDINKRVAAALDKVGLLGKERYQPRM----LSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK14243 95 MVFQKPNPF-PKSIYDNIAYGARINGYK-GDMDELVERSLRQAALWDEVKDKLKQsglsLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIAR 202
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAAR 215
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
28-219 |
8.94e-29 |
|
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: 108.36 E-value: 8.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 28 GEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipyVR-RQIGMIFQDHRLLMDRTVFDNVALPLV- 105
Cdd:TIGR03873 27 GSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRR----ARaRRVALVEQDSDTAVPLTVRDVVALGRIp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 106 IDGYSHGDINKRVAAALDKVGLLGKERYQPR---MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEE 182
Cdd:TIGR03873 103 HRSLWAGDSPHDAAVVDRALARTELSHLADRdmsTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRE 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 498358447 183 FNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:TIGR03873 183 LAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAG 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-222 |
1.00e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.49 E-value: 1.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQIGMIFQDHRLLM 92
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 DrTVFDNVALPLVIDGySHGDiNKRVAAALDKVGlLGKERYQPRM--LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:PRK10247 95 D-TVYDNLIFPWQIRN-QQPD-PAIFLDDLERFA-LPDTILTKNIaeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 171 QLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARM-RYRTLTLKAGRMYSSGEDR 222
Cdd:PRK10247 171 SNKHNVNEIIHRYVReQNIAVLWVTHDKDEINHAdKVITLQPHAGEMQEARYEL 224
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-219 |
1.17e-28 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 107.99 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ 80
Cdd:TIGR02323 3 LLQVSGLSKSY-GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 I------GMIFQDHR--LLMDRTVFDNVALPLVIDGYSH-GDINKRVAAALDKVGL-LGKERYQPRMLSGGEQQRVGIAR 150
Cdd:TIGR02323 82 RlmrtewGFVHQNPRdgLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 151 AIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRdLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
1.61e-28 |
|
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: 105.20 E-value: 1.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqRSQIPYVRRQI 81
Cdd:cd03216 1 LELRGITKRF-GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF--ASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQdhrllmdrtvfdnvalplvidgyshgdinkrvaaaldkvgllgkeryqprmLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03216 78 AMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 162 DEPTGNLDPQlsmDIMRLFEEFNRF---GVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03216 107 DEPTAALTPA---EVERLFKVIRRLraqGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
2.08e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.79 E-value: 2.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGgHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVM---ERPTDGRVFFHGDDVSHIQR--SQIP 75
Cdd:PRK09984 4 IIRVEKLAKTFNQ-HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaRDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 76 YVRRQIGMIFQDHRLLMDRTVFDNVAL------PL--VIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVG 147
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLENVLIgalgstPFwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRF-GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-220 |
4.93e-28 |
|
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: 106.32 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSkVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDG---RVF---FHGDDVSHIqrsqi 74
Cdd:COG1119 3 LLELRNVT-VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWEL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 75 pyvRRQIGMI--FQDHRLLMDRTVFDnvalpLVIDG----------YSHGDInKRVAAALDKVGL--LGKERYqpRMLSG 140
Cdd:COG1119 77 ---RKRIGLVspALQLRFPRDETVLD-----VVLSGffdsiglyrePTDEQR-ERARELLELLGLahLADRPF--GTLSQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 141 GEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLI-ATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
.
gi 498358447 220 E 220
Cdd:COG1119 226 P 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-222 |
6.46e-28 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 110.72 E-value: 6.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEMAFLTGHSGAGKST----LLKLISVMErptdGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQDHRLLM 92
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVESQG----GEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPYASL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 D--RTVFDNVALPLVIDGYSHGD-INKRVAAALDKVGLLGKE--RYqPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:PRK10261 415 DprQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLPEHawRY-PHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 168 LDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRdFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
7-219 |
6.58e-28 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.16 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQI----- 81
Cdd:PRK11701 12 LTKLY-GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRllrte 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 -GMIFQDHR--LLMDRTVFDNVALPLVIDGYSH-GDINKRVAAALDKVGLlGKERY--QPRMLSGGEQQRVGIARAIVNK 155
Cdd:PRK11701 91 wGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEI-DAARIddLPTTFSGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 156 PPLLLADEPTGNLDPQLS---MDIMR-LFEEfnrFGVSVLIATHDLGlIARM-RYRTLTLKAGRMYSSG 219
Cdd:PRK11701 170 PRLVFMDEPTGGLDVSVQarlLDLLRgLVRE---LGLAVVIVTHDLA-VARLlAHRLLVMKQGRVVESG 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-222 |
8.34e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 8.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 9 KVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLK----LISVMERP-TDGRVFFHGDDVSHIQRSQIpyvRRQIGM 83
Cdd:PRK14247 10 KVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDVIEL---RRRVQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 84 IFQDHRLLMDRTVFDNVALPLVIDGY--SHGDINKRVAAALDKVGLLgkERYQPRM------LSGGEQQRVGIARAIVNK 155
Cdd:PRK14247 87 VFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLW--DEVKDRLdapagkLSGGQQQRLCIARALAFQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 156 PPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK14247 165 PEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTR 230
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-220 |
1.56e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.32 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGH----QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRV-FFHGDDVSH-------- 68
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 69 ------IQRS------QIPYVRRQIGMIFQ-DHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlgKERYQP 135
Cdd:PRK13651 83 vleklvIQKTrfkkikKIKEIRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL--DESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 136 RM---LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKA 212
Cdd:PRK13651 161 RSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*...
gi 498358447 213 GRMYSSGE 220
Cdd:PRK13651 241 GKIIKDGD 248
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
16-220 |
2.03e-27 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 106.53 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERP----TDGRVFFHGDDV---SHIQRSQIpyVRRQIGMIFQDH 88
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlklSPRERRKI--IGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLMD--RTVFDNvaLPLVIDGYS--------HGDINKRVAAALDKVGLLGKERYQ---PRMLSGGEQQRVGIARAIVNK 155
Cdd:COG4170 99 SSCLDpsAKIGDQ--LIEAIPSWTfkgkwwqrFKWRKKRAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 156 PPLLLADEPTGNLDPQLSMDIMRLFEEFNRF-GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTVESGP 242
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
3.00e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.88 E-value: 3.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDvshIQRSQIPYVRRQ 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEP---ITKENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQD-HRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK13652 80 VGLVFQNpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-220 |
3.18e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.83 E-value: 3.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGH----QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDV-SHIQRSQIPY 76
Cdd:PRK13649 3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 VRRQIGMIFQ-DHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVG----LLGKeryQPRMLSGGEQQRVGIARA 151
Cdd:PRK13649 83 IRKKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGisesLFEK---NPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
7-196 |
4.66e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 106.27 E-value: 4.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGddvshiQR-SQIPYVRRQIGMIF 85
Cdd:PRK11000 9 VTKAY-GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE------KRmNDVPPAERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 86 QDHRLLMDRTVFDNVALPLVIDGYSHGDINKRV---AAALDKVGLLgkERyQPRMLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLL--DR-KPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 498358447 163 EPTGNLDP----QLSMDIMRLFEEFNRFGVSVliaTHD 196
Cdd:PRK11000 159 EPLSNLDAalrvQMRIEISRLHKRLGRTMIYV---THD 193
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-215 |
1.23e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 103.25 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVysgghQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDdvsHIQRSQIPYVRRQ 80
Cdd:PRK13642 11 VFKYEKESDV-----NQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQD-HRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRyRTLTLKAGRM 215
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAASSD-RILVMKAGEI 218
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-197 |
1.39e-26 |
|
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: 101.71 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGddvSHIQRSQIpyvrRQIGMIFQ 86
Cdd:TIGR03740 6 LSKRF-GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG---HPWTRKDL----HKIGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 87 DHRLLMDRTVFDNVALPLVIDGYSHGDINKrvaaALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:TIGR03740 78 SPPLYENLTARENLKVHTTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTN 153
|
170 180 190
....*....|....*....|....*....|.
gi 498358447 167 NLDPQLSMDIMRLFEEFNRFGVSVLIATHDL 197
Cdd:TIGR03740 154 GLDPIGIQELRELIRSFPEQGITVILSSHIL 184
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-215 |
1.45e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 102.26 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyVRRQ 80
Cdd:PRK11614 5 MLSFDKVSAHY-GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVALplviDGY--SHGDINKRVAAALDKVGLLGKERYQ-PRMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAM----GGFfaERDQFQERIKWVYELFPRLHERRIQrAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-219 |
1.63e-26 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 101.92 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQI 81
Cdd:cd03254 3 IEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS---LRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDhRLLMDRTVFDNVAlplvidgYSHGDIN-KRVAAALDKVGLLG-----KERYQPRM------LSGGEQQRVGIA 149
Cdd:cd03254 80 GVVLQD-TFLFSGTIMENIR-------LGRPNATdEEVIEAAKEAGAHDfimklPNGYDTVLgenggnLSQGERQLLAIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 150 RAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIAtHDLGLIaRMRYRTLTLKAGRMYSSG 219
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIA-HRLSTI-KNADKILVLDDGKIIEEG 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-169 |
5.28e-26 |
|
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: 104.90 E-value: 5.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHI-QRSqipyVRRQ 80
Cdd:COG5265 358 VRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVtQAS----LRAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDrTVFDNVAlplvidgY-----SHGDINK--RVAAALDKVGLLgKERYQPR------MLSGGEQQRVG 147
Cdd:COG5265 434 IGIVPQDTVLFND-TIAYNIA-------YgrpdaSEEEVEAaaRAAQIHDFIESL-PDGYDTRvgerglKLSGGEKQRVA 504
|
170 180
....*....|....*....|..
gi 498358447 148 IARAIVNKPPLLLADEPTGNLD 169
Cdd:COG5265 505 IARTLLKNPPILIFDEATSALD 526
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-220 |
5.35e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.79 E-value: 5.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKST----LLKLIsvmerPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQD- 87
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 88 HRLLMDR-TVFDNVALPLVID--GYSHGDINKRVAAALDKVGLLGKERYQ-PRMLSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:PRK15134 372 NSSLNPRlNVLQIIEEGLRVHqpTLSAAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 164 PTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGD 509
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-203 |
7.19e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 101.72 E-value: 7.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEM-AFLtGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPY--- 76
Cdd:COG4152 1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIfGLL-GPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYlpe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 ---------VRRQIGMIFQDHrllmdrtvfdnvalplvidGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVG 147
Cdd:COG4152 79 erglypkmkVGEQLVYLARLK-------------------GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDP---QLSMDIMRlfeEFNRFGVSVLIATHDLGLIARM 203
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPvnvELLKDVIR---ELAAKGTTVIFSSHQMELVEEL 195
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-196 |
7.27e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 7.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 4 FDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDdvshiqrsqipyVRrqIGM 83
Cdd:COG0488 1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------------LR--IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 84 IFQDHRLLMDRTVFDNVALPL-----------------------------------VIDGYshgDINKRVAAALDKVGLL 128
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVLDGDaelraleaeleeleaklaepdedlerlaelqeefeALGGW---EAEARAEEILSGLGFP 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 129 GKERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDpqlsMDIMRLFEEF-NRFGVSVLIATHD 196
Cdd:COG0488 143 EEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEFlKNYPGTVLVVSHD 208
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
7.49e-26 |
|
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: 104.50 E-value: 7.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVME--RPTDGRVFFHGDDVSHIQRSQIPY--- 76
Cdd:TIGR03269 1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHVALCEKCGYVERPSkvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 ---------------------------VRRQIGMIFQ-DHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLL 128
Cdd:TIGR03269 80 epcpvcggtlepeevdfwnlsdklrrrIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 129 GKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEE-FNRFGVSVLIATHDLGLIARMRYRT 207
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|...
gi 498358447 208 LTLKAGRMYSSGE 220
Cdd:TIGR03269 240 IWLENGEIKEEGT 252
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-197 |
7.95e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.95 E-value: 7.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEM-AFLtGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVsHIQRSQIPyVRR 79
Cdd:COG3845 5 ALELRGITKRF-GGVVANDDVSLTVRPGEIhALL-GENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRSPRDA-IAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQdHRLLMDR-TVFDNVAL---PLVIDGYSHGDINKRVAAALDKVGLlgkeRYQPRM----LSGGEQQRVGIARA 151
Cdd:COG3845 81 GIGMVHQ-HFMLVPNlTVAENIVLglePTKGGRLDRKAARARIRELSERYGL----DVDPDAkvedLSVGEQQRVEILKA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498358447 152 IVNKPPLLLADEPTGNLDPQlsmDIMRLFEEFNRF---GVSVLIATHDL 197
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQ---EADELFEILRRLaaeGKSIIFITHKL 201
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-222 |
8.04e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 100.69 E-value: 8.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 9 KVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLK----LISVMERP-TDGRVFFHGDDVSHIQRSQIPyVRRQIGM 83
Cdd:PRK14267 11 RVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEArVEGEVRLFGRNIYSPDVDPIE-VRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 84 IFQDHRLLMDRTVFDNVALPLVIDGY--SHGDINKRVAAALDKVGLLG--KERYQ--PRMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK14267 90 VFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDevKDRLNdyPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-169 |
8.13e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 104.27 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQI 81
Cdd:PRK13657 335 VEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---RRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDhRLLMDRTVFDN--VALPlvidGYSHGDINK--RVAAALD-------KVGLLGKERyqPRMLSGGEQQRVGIAR 150
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNirVGRP----DATDEEMRAaaERAQAHDfierkpdGYDTVVGER--GRQLSGGERQRLAIAR 484
|
170
....*....|....*....
gi 498358447 151 AIVNKPPLLLADEPTGNLD 169
Cdd:PRK13657 485 ALLKDPPILILDEATSALD 503
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-203 |
8.69e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.88 E-value: 8.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGgHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVM-----ERPTDGRVFFHGDDVsHIQRSQIPY 76
Cdd:PRK14258 8 IKVNNLSFYYDT-QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNI-YERRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 VRRQIGMIFQDHRLLmDRTVFDNVALPLVIDGYSHG-DINKRVAAALDKVGLLGKERYQPRM----LSGGEQQRVGIARA 151
Cdd:PRK14258 86 LRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARM 203
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRL 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-219 |
1.22e-25 |
|
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: 99.36 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVY---SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipyV 77
Cdd:cd03266 1 MITADALTKRFrdvKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGmIFQDHRLLMDR-TVFDNVALplviDGYSHGDINKRVAAALDKV-GLLGKERYQPRM---LSGGEQQRVGIARAI 152
Cdd:cd03266 77 RRRLG-FVSDSTGLYDRlTARENLEY----FAGLYGLKGDELTARLEELaDRLGMEELLDRRvggFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
12-219 |
1.37e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 12 SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQ-IGMIFQDHRL 90
Cdd:PRK10070 38 TGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFAL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 LMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:PRK10070 118 MPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 171 ----QLSMDIMRLFEEFNRfgvSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK10070 198 lirtEMQDELVKLQAKHQR---TIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-219 |
3.45e-25 |
|
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: 102.49 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSG-GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:TIGR02203 331 VEFRNVTFRYPGrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASL---RRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDhRLLMDRTVFDNVALPlVIDGYSHGDINKRVAAA--LDKVGLLGKERYQP-----RMLSGGEQQRVGIARAIV 153
Cdd:TIGR02203 408 VALVSQD-VVLFNDTIANNIAYG-RTEQADRAEIERALAAAyaQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 154 NKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIAtHDLGLIARMRyRTLTLKAGRMYSSG 219
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA-HRLSTIEKAD-RIVVMDDGRIVERG 549
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-169 |
4.54e-25 |
|
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: 98.38 E-value: 4.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSG--GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIsvmER---PTDGRVFFHGDDVSHIqrsQIPY 76
Cdd:cd03249 1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDL---NLRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 VRRQIGMIFQDhRLLMDRTVFDNVALplvidgyshGDIN---------KRVAAALDKVGLLgKERYQPR------MLSGG 141
Cdd:cd03249 75 LRSQIGLVSQE-PVLFDGTIAENIRY---------GKPDatdeeveeaAKKANIHDFIMSL-PDGYDTLvgergsQLSGG 143
|
170 180
....*....|....*....|....*...
gi 498358447 142 EQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-219 |
7.29e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.20 E-value: 7.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVM------ERPTDGRVFFHGDDVSHIQRSQIpyvRRQIGMIFQDHRLL 91
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQIDAIKL---RKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 92 MDRTVFDNVALPLvidgYSHG-----DINKRVAAALDKVGLLgKERYQ-----PRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:PRK14246 103 PHLSIYDNIAYPL----KSHGikekrEIKKIVEECLRKVGLW-KEVYDrlnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVARVADYVAFLYNGELVEWG 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
7.76e-25 |
|
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: 97.54 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSG--GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipYVRR 79
Cdd:cd03248 12 VKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQDhRLLMDRTVFDNVA--LPLVIDG---------YSHGDINKRVAAALDKVGLLGKEryqprmLSGGEQQRVGI 148
Cdd:cd03248 89 KVSLVGQE-PVLFARSLQDNIAygLQSCSFEcvkeaaqkaHAHSFISELASGYDTEVGEKGSQ------LSGGQKQRVAI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 149 ARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMrYRTLTLKAGRM 215
Cdd:cd03248 162 ARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
13-199 |
9.44e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 96.27 E-value: 9.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipyvrRQIGMIFQDHR--L 90
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE------PHENILYLGHLpgL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 LMDRTVFDNVALPLVIdgysHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:TIGR01189 85 KPELSALENLHFWAAI----HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180 190
....*....|....*....|....*....|
gi 498358447 171 QLSMDIMRLFEEFNRFGVSVLIATH-DLGL 199
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHqDLGL 190
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-220 |
9.69e-25 |
|
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: 101.36 E-value: 9.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQA-LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:COG4618 331 LSVENLTVVPPGSKRPiLRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL---GRH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLmDRTVFDNVA-LPLVidgyshgDINKRVAAAlDKVGL--------LGkerYQPR------MLSGGEQQR 145
Cdd:COG4618 408 IGYLPQDVELF-DGTIAENIArFGDA-------DPEKVVAAA-KLAGVhemilrlpDG---YDTRigeggaRLSGGQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 146 VGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRyRTLTLKAGRMYSSGE 220
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVD-KLLVLRDGRVQAFGP 549
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-195 |
1.00e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 97.41 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHI---QRSqipyv 77
Cdd:COG1137 3 TLEAENLVKSY-GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhKRA----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlGKERYQPRM-LSGGEQQRVGIARAIVNKP 156
Cdd:COG1137 77 RLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI-THLRKSKAYsLSGGERRRVEIARALATNP 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATH 195
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDH 194
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-219 |
1.55e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 95.46 E-value: 1.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSG-GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipyVRRQ 80
Cdd:cd03247 1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQD-HrlLMDRTVFDNVALPLvidgyshgdinkrvaaaldkvgllgkeryqprmlSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03247 77 ISVLNQRpY--LFDTTLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARMRyRTLTLKAGRMYSSG 219
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHMD-KILFLENGKIIMQG 178
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
17-221 |
1.76e-24 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 98.64 E-value: 1.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEMAFLTGHSGAGKS-TLLKLISVMERP--TDGRVFFHGDDVSHIQRSQIPYVR-RQIGMIFQDHRLLM 92
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRaEQISMIFQDPMTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 D--RTVFDNVALPLVI-DGYSHGDINKRVAAALDKVGL---LGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:PRK09473 111 NpyMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 167 NLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRM--YSSGED 221
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKReFNTAIIMITHDLGVVAGICDKVLVMYAGRTmeYGNARD 248
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
3.13e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.31 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPyvrRQ 80
Cdd:COG4604 1 MIEIKNVSKRY-GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA---KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVAL---PlvidgYSHGDINKR----VAAALDKVGLLG-KERY--QprmLSGGEQQRVGIAR 150
Cdd:COG4604 77 LAILRQENHINSRLTVRELVAFgrfP-----YSKGRLTAEdreiIDEAIAYLDLEDlADRYldE---LSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 151 AIVNKPPLLLADEPTGNLDPQLSMDIM----RLFEEFNRfgvSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMkllrRLADELGK---TVVIVLHDINFASCYADHIVAMKDGRVVAQG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-215 |
3.33e-24 |
|
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: 95.86 E-value: 3.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGddvshiqrsQIPYVRR-----QIGMIF-QDHRL 90
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---------LVPWKRRkkflrRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 LMDRTVFDNVALPLVIDGYSHGDINKRV---AAALDkvglLGKERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDLPPARFKKRLdelSELLD----LEELLDTPvRQLSLGQRMRAEIAAALLHEPEILFLDEPTI 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 167 NLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03267 183 GLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-219 |
3.89e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.79 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIsvmerptDGRVFFHGDDVSHIQRSQIPY---- 76
Cdd:PRK13640 6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLI-------NGLLLPDDNPNSKITVDGITLtakt 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 ---VRRQIGMIFQD-HRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAI 152
Cdd:PRK13640 79 vwdIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDLGLiARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAQG 225
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-219 |
4.05e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.02 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 35 GHSGAGKSTLLKLISVMERPTDGRVFFHGDD-VSHIQRSQIPYVRRQIGMIFQDHRLLMDRTVFDNValplvidgySHGD 113
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNL---------RYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 114 INKRVAAALDKVGLLGKE----RYqPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD--------PQLSmdimRLFE 181
Cdd:PRK11144 102 AKSMVAQFDKIVALLGIEplldRY-PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlprkrellPYLE----RLAR 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 498358447 182 EFNrfgVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK11144 177 EIN---IPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
6.21e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 96.24 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG----HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFhGDDV--SHIQRSQIP 75
Cdd:PRK13634 3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 76 YVRRQIGMIFQ--DHRLLmDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGL----LGKeryQPRMLSGGEQQRVGIA 149
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLF-EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpeelLAR---SPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 150 RAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
8.68e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 96.41 E-value: 8.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqrSQIPYVRRQI 81
Cdd:PRK13537 8 IDFRNVEKRY-GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP----SRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-203 |
1.03e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---RQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDrTVFDN--VALPLVIDgyshgdinKRVAAALDKVGLlGK--ERYQP---------RMLSGGEQQRVG 147
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNllLAAPNASD--------EALIEVLQQVGL-EKllEDDKGlnawlgeggRQLSGGEQRRLG 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDLGLIARM 203
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF 540
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-215 |
1.23e-23 |
|
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: 92.88 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 14 GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqRSQIPYVRRQIGMIFQDHR---L 90
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR--RSPRDAIRAGIAYVPEDRKregL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 LMDRTVFDNVALPlvidgyshgdinkrvaaaldkvgllgkeryqpRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:cd03215 90 VLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498358447 171 QLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:cd03215 138 GAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-210 |
1.48e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 93.33 E-value: 1.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 22 SFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiQR----SQIPYVRRQIGMifqdHRLLmdrTVF 97
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR-QRdeyhQDLLYLGHQPGI----KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 98 DNVALPLVIDGYSHGDinkRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIM 177
Cdd:PRK13538 93 ENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLE 169
|
170 180 190
....*....|....*....|....*....|....
gi 498358447 178 RLFEEFNRFGVSVLIATH-DLGLIArMRYRTLTL 210
Cdd:PRK13538 170 ALLAQHAEQGGMVILTTHqDLPVAS-DKVRKLRL 202
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-197 |
1.76e-23 |
|
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: 97.82 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQI 81
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQD-HrlLMDRTVFDNVAL--PLVIDgyshgdinKRVAAALDKVGLLGKERYQP-----------RMLSGGEQQRVG 147
Cdd:TIGR02868 412 SVCAQDaH--LFDTTVRENLRLarPDATD--------EELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDL 197
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-202 |
1.78e-23 |
|
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: 93.88 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHI---QRSqipyvRRQI 81
Cdd:TIGR04406 5 ENLIKSY-KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLpmhERA-----RLGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNVALPL-VIDGYSHGDINKRVAAALDKVGLlGKERYQPRM-LSGGEQQRVGIARAIVNKPPLL 159
Cdd:TIGR04406 79 GYLPQEASIFRKLTVEENIMAVLeIRKDLDRAEREERLEALLEEFQI-SHLRDNKAMsLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHD----LGLIAR 202
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNvretLDICDR 204
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-220 |
2.63e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPyVRRQIGMIFQDHrllmDRT 95
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLA-LRQQVATVFQDP----EQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VF-----DNVALPLVIDGYSHGDINKRVAAALDKVGLLGKeRYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK13638 90 IFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHF-RHQPiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498358447 170 PQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
13-199 |
2.84e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQ-RSQIPYVRRQIGMifqdHRLL 91
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEACHYLGHRNAM----KPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 92 mdrTVFDNVALPLVIdgysHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQ 171
Cdd:PRK13539 89 ---TVAENLEFWAAF----LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*....
gi 498358447 172 LSMDIMRLFEEFNRFGVSVLIATH-DLGL 199
Cdd:PRK13539 162 AVALFAELIRAHLAQGGIVIAATHiPLGL 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-195 |
3.06e-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: 92.23 E-value: 3.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIS--VMERPTDGRVFFHGddvshIQRSQIPYvRR 79
Cdd:cd03213 9 LTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING-----RPLDKRSF-RK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQDHRLLMDRTVFDNValplvidgyshgdinkRVAAALdkvgllgkeryqpRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETL----------------MFAAKL-------------RGLSGGERKRVSIALELVSNPSLL 133
|
170 180 190
....*....|....*....|....*....|....*.
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATH 195
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIH 169
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-222 |
4.26e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.08 E-value: 4.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG----HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQ-IPY 76
Cdd:PRK13646 3 IRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 VRRQIGMIFQdhrlLMDRTVF-DNVALPLVIDGYSHG-DINKRVAAALDKVGLLGKER----YQPRMLSGGEQQRVGIAR 150
Cdd:PRK13646 83 VRKRIGMVFQ----FPESQLFeDTVEREIIFGPKNFKmNLDEVKNYAHRLLMDLGFSRdvmsQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 151 AIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPK 231
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
18-220 |
4.87e-23 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 92.98 E-value: 4.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMErPTDGRVFFHGDDVSHIQRSQIpyvRRQIGMIFQDHRLLMDRTVF 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAEL---ARHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 98 DNVALplvidGYSHGDINKRVAAALDKV-GLLGKERYQPRM---LSGGEQQRVGIARAI------VNKPP-LLLADEPTG 166
Cdd:COG4138 88 QYLAL-----HQPAGASSEAVEQLLAQLaEALGLEDKLSRPltqLSGGEWQRVRLAAVLlqvwptINPEGqLLLLDEPMN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 167 NLD--PQLSMDimRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:COG4138 163 SLDvaQQAALD--RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-219 |
5.47e-23 |
|
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: 92.21 E-value: 5.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVY---------------------SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVF 60
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 61 FHGDDVSHIqrsqipyvrrQIGMIFQdhrllMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGlLGKERYQP-RMLS 139
Cdd:cd03220 81 VRGRVSSLL----------GLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSE-LGDFIDLPvKTYS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 140 GGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-214 |
5.61e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.13 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyVRRQIGMIFQDHRLLM 92
Cdd:PRK11300 16 GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARMGVVRTFQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 DRTVFDN--VALPL-VIDGYSHGDIN------------KRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK11300 94 EMTVIENllVAQHQqLKTGLFSGLLKtpafrraesealDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNeHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
13-219 |
9.53e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 9.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPyvrRQIGMIFQDHRLLM 92
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS---RRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 DRTVFDNVAL---PLVIDGYSHGDINKR-VAAALDKVGLlgkERYQPR---MLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:PRK09536 91 EFDVRQVVEMgrtPHRSRFDTWTETDRAaVERAMERTGV---AQFADRpvtSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 498358447 166 GNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK09536 168 ASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-214 |
2.41e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFfHGDDVshiqrsqipyvrrQ 80
Cdd:COG0488 315 VLELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVK-LGETV-------------K 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLL-MDRTVFDNVAlplvidGYSHGDINKRVAAALDKVGLLGKERYQP-RMLSGGEQQRVGIARAIVNKPPL 158
Cdd:COG0488 380 IGYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 159 LLADEPTGNLDpqlsMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:COG0488 454 LLLDEPTNHLD----IETLEALEEAlDDFPGTVLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-220 |
2.49e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.77 E-value: 2.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipYVRRQIGMIFQDHRLLMD-- 93
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS---YRSQRIRMIFQDPSTSLNpr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 94 RTVFDNVALPLVID-GYSHGDINKRVAAALDKVGLLGKE-RYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQ 171
Cdd:PRK15112 104 QRISQILDFPLRLNtDLEPEQREKQIIETLRQVGLLPDHaSYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 172 LSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK15112 184 MRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-219 |
2.75e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG----HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFhGD-----DVSHIQrs 72
Cdd:PRK13645 7 IILDNVSYTYAKKtpfeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDyaipaNLKKIK-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 73 QIPYVRRQIGMIFQ--DHRLLMDrTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlgKERY---QPRMLSGGEQQRVG 147
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQL--PEDYvkrSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-182 |
3.19e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.10 E-value: 3.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIS--------VMERPTDGRVFFhgddVShiQRs 72
Cdd:COG4178 362 ALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAglwpygsgRIARPAGARVLF----LP--QR- 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 73 qiPYVrrQIGmifqdhrllmdrTVFDNVALPLVIDGYShgdiNKRVAAALDKVGL------LGKERYQPRMLSGGEQQRV 146
Cdd:COG4178 435 --PYL--PLG------------TLREALLYPATAEAFS----DAELREALEAVGLghlaerLDEEADWDQVLSLGEQQRL 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 498358447 147 GIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEE 182
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-220 |
4.45e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.53 E-value: 4.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVY---------------------SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRV 59
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 60 FFHGDDVSHIqrsqipyvrrQIGMIFQdhrllMDRTVFDNVALPLVIDGYSHGDINKRVAAALDKVGlLGKERYQP-RML 138
Cdd:COG1134 84 EVNGRVSALL----------ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAE-LGDFIDQPvKTY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 139 SGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSS 218
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMD 227
|
..
gi 498358447 219 GE 220
Cdd:COG1134 228 GD 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-220 |
5.74e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 93.33 E-value: 5.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVY----SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFH-GD---DVSHIQRS 72
Cdd:TIGR03269 279 IIKVRNVSKRYisvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 73 QIPYVRRQIGMIFQDHRLLMDRTVFDNVA------LP-----------LVIDGYShgdiNKRVAAALDKVgllgkeryqP 135
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTeaigleLPdelarmkavitLKMVGFD----EEKAEEILDKY---------P 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 136 RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP----QLSMDIMRLFEEFNRfgvSVLIATHDLGLIARMRYRTLTLK 211
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEMEQ---TFIIVSHDMDFVLDVCDRAALMR 502
|
....*....
gi 498358447 212 AGRMYSSGE 220
Cdd:TIGR03269 503 DGKIVKIGD 511
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
10-207 |
5.87e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 90.22 E-value: 5.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 10 VYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVM-----ERPTDGRVFFHGDDVsHIQRSQIPYVRRQIGMI 84
Cdd:PRK14239 13 VYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNI-YSPRTDTVDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 85 FQD-HRLLMdrTVFDNVALPLVIDGYSHGDI-------NKRVAAALDKVgllgKERYQPRM--LSGGEQQRVGIARAIVN 154
Cdd:PRK14239 92 FQQpNPFPM--SIYENVVYGLRLKGIKDKQVldeavekSLKGASIWDEV----KDRLHDSAlgLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 155 KPPLLLADEPTGNLDP----QLSMDIMRLFEEFnrfgvSVLIATHDLGLIARMRYRT 207
Cdd:PRK14239 166 SPKIILLDEPTSALDPisagKIEETLLGLKDDY-----TMLLVTRSMQQASRISDRT 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
13-210 |
1.27e-21 |
|
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: 88.32 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHG---DDVSHIQRSQIPYVRRQIGMifqDHR 89
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGgplDFQRDSIARGLLYLGHAPGI---KTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 90 LlmdrTVFDNVALPLVIdgysHGDinKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:cd03231 88 L----SVLENLRFWHAD----HSD--EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498358447 170 PQLSMDIMRLFEEFNRFGVSVLIATH-DLGlIARMRYRTLTL 210
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHqDLG-LSEAGARELDL 198
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-219 |
1.52e-21 |
|
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: 92.38 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 14 GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVshiqRSQIPYVRRQIGMIFQDHRLLMD 93
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 94 RTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLS 173
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 498358447 174 MDIMRLFEEFnRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:TIGR01257 1098 RSIWDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-219 |
2.01e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 89.28 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDdvsHIQRSQIPYVRRQI 81
Cdd:PRK10253 8 LRGEQLTLGY-GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE---HIQHYASKEVARRI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDnvalpLVIDG-YSHGDINKR--------VAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAI 152
Cdd:PRK10253 84 GLLAQNATTPGDITVQE-----LVARGrYPHQPLFTRwrkedeeaVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRF-GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK10253 159 AQETAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
2.24e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.99 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGG----HQALQKVSFHLRKGEmaFLT--GHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHI---QR 71
Cdd:COG1101 1 MLELKNLSKTFNPGtvneKRALDGLNLTIEEGD--FVTviGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeyKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 72 SqipyvrRQIGMIFQDHrlLM----DRTVFDNVAL--------PLVIdGYSHGDInKRVAAALDKVGlLGKE-RYQPRM- 137
Cdd:COG1101 79 A------KYIGRVFQDP--MMgtapSMTIEENLALayrrgkrrGLRR-GLTKKRR-ELFRELLATLG-LGLEnRLDTKVg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 138 -LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEF-NRFGVSVLIATHDlgliarMRY------RTLT 209
Cdd:COG1101 148 lLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHN------MEQaldygnRLIM 221
|
....*
gi 498358447 210 LKAGR 214
Cdd:COG1101 222 MHEGR 226
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-219 |
2.62e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 90.28 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiqrSQIPYVRRQI 81
Cdd:PRK13536 42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP----ARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDRTVFDNValpLVIDGY---SHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENL---LVFGRYfgmSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-214 |
4.84e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 4.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 15 HQALQKVSFHLRKGEMAFLTGHSGAGKS-TLLKLISVMERP----TDGRVFFHGDDVSHIQRSQIPYVR-RQIGMIFQD- 87
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 88 -------HRLlmDRTVFDNVALplvidgysHGDINKRVAAA-----LDKVGL---LGKERYQPRMLSGGEQQRVGIARAI 152
Cdd:PRK15134 102 mvslnplHTL--EKQLYEVLSL--------HRGMRREAARGeilncLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQeLNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-214 |
8.06e-21 |
|
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: 86.39 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTL-LKLISVMErPTDGRVFFHGDDVSHIQRSQIpyvRR 79
Cdd:cd03244 3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLlLALFRLVE-LSSGSILIDGVDISKIGLHDL---RS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQDhRLLMDRTVFDNVAlPLviDGYSHGDINKrvaaALDKVGLLGKERYQPRML-----------SGGEQQRVGI 148
Cdd:cd03244 79 RISIIPQD-PVLFSGTIRSNLD-PF--GEYSDEELWQ----ALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 149 ARAIVNKPPLLLADEPTGNLDPQLSMDIMR-LFEEFnrFGVSVLIATHDLGLIarMRY-RTLTLKAGR 214
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKtIREAF--KDCTVLTIAHRLDTI--IDSdRILVLDKGR 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
10-219 |
1.28e-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: 86.04 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 10 VYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQrsqiPY--VRRQIGMIFQD 87
Cdd:TIGR03410 8 VYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP----PHerARAGIAYVPQG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 88 HRLLMDRTVFDNVALPLVIDGYSHGDINKRVAA---ALDKVgllgkeryQPRM---LSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:TIGR03410 84 REIFPRLTVEENLLTGLAALPRRSRKIPDEIYElfpVLKEM--------LGRRggdLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 162 DEPTGNLDPQLSMDIMRLFEEFN-RFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRaEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-219 |
1.83e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.22 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPyvrRQ 80
Cdd:PRK11231 2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA---RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVFDNVA------LPLVidGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVN 154
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVAygrspwLSLW--GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 155 KPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-200 |
3.06e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.54 E-value: 3.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG-HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDvshIQRSQIPYVRRQ 80
Cdd:PRK11176 342 IEFRNVTFTYPGKeVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDrTVFDNVALPlVIDGYSHGDINK--RVAAALD-----KVGL---LGKERYqprMLSGGEQQRVGIAR 150
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYA-RTEQYSREQIEEaaRMAYAMDfinkmDNGLdtvIGENGV---LLSGGQRQRIAIAR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 151 AIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIAtHDLGLI 200
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIA-HRLSTI 542
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-219 |
3.75e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRV----FFHGDDVSHIQRSQIPY---------VRRQIGM 83
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNPYskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 84 IFQ--DHRLLMDrTVFDNVALPLVIDGYSHGDINKRVAAALDKVGLlgKERY---QPRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK13631 121 VFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGL--DDSYlerSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-215 |
3.00e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 21 VSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVS--HIQRSqipyVRRQIGMIFQDHR---LLMDRT 95
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirSPRDA----IRAGIAYVPEDRKgegLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNVALPlVIDGYSHG---DINKRVAAALDKVGLLG---KERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNL 168
Cdd:COG1129 347 IRENITLA-SLDRLSRGgllDRRRERALAEEYIKRLRiktPSPEQPvGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498358447 169 DPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:COG1129 426 DVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-200 |
3.03e-19 |
|
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: 80.57 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGrvffhgdDVSHIQRSQIPYVRRqi 81
Cdd:cd03221 1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-------IVTWGSTVKIGYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 gmifqdhrllmdrtvfdnvalplvidgyshgdinkrvaaaldkvgllgkeryqprmLSGGEQQRVGIARAIVNKPPLLLA 161
Cdd:cd03221 71 --------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....*....
gi 498358447 162 DEPTGNLDPQlsmDIMRLFEEFNRFGVSVLIATHDLGLI 200
Cdd:cd03221 95 DEPTNHLDLE---SIEALEEALKEYPGTVILVSHDRYFL 130
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
16-220 |
3.16e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 84.02 E-value: 3.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKS----TLLKLISVMERPTDGRVFFHGDDVSHI---QRSQIpyVRRQIGMIFQDH 88
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRIsekERRNL--VGAEVAMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLMD--RTV-FDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKER---YQPRMLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:PRK11022 99 MTSLNpcYTVgFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASrldVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 163 EPTGNLDPQLSMDIMRLFEEFNRF-GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
21-220 |
5.84e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.44 E-value: 5.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 21 VSFHLRKGEMAFLTGHSGAGKS-TLLKLISVME---RPTDGRVFFHGDDVSHIQrsqipyVR-RQIGMIFQDHRLLMD-- 93
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAPCA------LRgRKIATIMQNPRSAFNpl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 94 RTVFDNVALPLVIDGySHGDiNKRVAAALDKVGLLGKERY---QPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:PRK10418 96 HTMHTHARETCLALG-KPAD-DATLTAALEAVGLENAARVlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498358447 171 QLSMDIMRLFEEFNRF-GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK10418 174 VAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-202 |
6.35e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.77 E-value: 6.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipYVRRQIGMIFQDhRLLMDRT 95
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH---YLHRQVALVGQE-PVLFSGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNVALPLviDGYSHGDINK--RVAAALDKVGLLGKERY-----QPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNL 168
Cdd:TIGR00958 571 VRENIAYGL--TDTPDEEIMAaaKAANAHDFIMEFPNGYDtevgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190
....*....|....*....|....*....|....*
gi 498358447 169 DPQlsmdIMRLFEEFNRF-GVSVLIATHDLGLIAR 202
Cdd:TIGR00958 649 DAE----CEQLLQESRSRaSRTVLLIAHRLSTVER 679
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
16-195 |
1.33e-18 |
|
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: 80.78 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERP---TDGRVFFHGDDVS-HIQRSQIPYVRrqigmifQDHRLL 91
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKpDQFQKCVAYVR-------QDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 92 MDRTVFDNVALPLVIDGYSHGD---INKRVA-AALDKVGL--LGKERYqpRMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:cd03234 94 PGLTVRETLTYTAILRLPRKSSdaiRKKRVEdVLLRDLALtrIGGNLV--KGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190
....*....|....*....|....*....|
gi 498358447 166 GNLDPQLSMDIMRLFEEFNRFGVSVLIATH 195
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
23-197 |
1.87e-18 |
|
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: 80.28 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 23 FHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVffhgddvsHIQRSQIPYVRRQIGMIFQDHRLLMD------RTV 96
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTV--------KVAGASPGKGWRHIGYVPQRHEFAWDfpisvaHTV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 FDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDI 176
Cdd:TIGR03771 73 MSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELL 152
|
170 180
....*....|....*....|.
gi 498358447 177 MRLFEEFNRFGVSVLIATHDL 197
Cdd:TIGR03771 153 TELFIELAGAGTAILMTTHDL 173
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-197 |
2.03e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 80.71 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYSGgHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipYVRRQIGMI 84
Cdd:PRK10895 7 KNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 85 FQDHRLLMDRTVFDNVALPLVI-DGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190
....*....|....*....|....*....|....
gi 498358447 164 PTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDL 197
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNV 197
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-219 |
4.28e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSH-IQRSQIPYVRRQ 80
Cdd:PRK15056 7 IVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDrtvfdnvalpLVIDG-YSHGDINKR--------VAAALDKVGLLGKERYQPRMLSGGEQQRVGIARA 151
Cdd:PRK15056 87 EEVDWSFPVLVED----------VVMMGrYGHMGWLRRakkrdrqiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 152 IVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKaGRMYSSG 219
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASG 223
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
18-220 |
5.04e-18 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 79.59 E-value: 5.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMeRPTDGRVFFHGDDVSHIQRSQIPYVRrqiGMIFQDHRLLMDRTVF 97
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 98 DNVALPLViDGYSHGDINKRVAAALDKVGLLGKeryQPRM---LSGGEQQRVGIARAIVNKPP-------LLLADEPTGN 167
Cdd:PRK03695 88 QYLTLHQP-DKTRTEAVASALNEVAEALGLDDK---LGRSvnqLSGGEWQRVRLAAVVLQVWPdinpagqLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 168 LD--PQLSMDimRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK03695 164 LDvaQQAALD--RLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-217 |
6.55e-18 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.54 E-value: 6.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGD-DVSHIQrsqipyvrrqigmifQDHRLL 91
Cdd:PRK11147 14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDlIVARLQ---------------QDPPRN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 92 MDRTVFDNVA----------------LPLVIDGYSHGDINK--RVAAALDKVGL----------LGKERYQPRM----LS 139
Cdd:PRK11147 79 VEGTVYDFVAegieeqaeylkryhdiSHLVETDPSEKNLNElaKLQEQLDHHNLwqlenrinevLAQLGLDPDAalssLS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 140 GGEQQRVGIARAIVNKPPLLLADEPTGNLDpqlsMDIMRLFEEF-NRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYS 217
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLD----IETIEWLEGFlKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVS 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-199 |
2.51e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.91 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDvshIQRSQIPYvrrQIGMIFQDHRLLMDR--T 95
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS---IKKDLCTY---QKQLCFVGHRSGINPylT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNVALPLvidGYSHGDINKRVAAALDKVGLLGKerYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMD 175
Cdd:PRK13540 91 LRENCLYDI---HFSPGAVGITELCRLFSLEHLID--YPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*
gi 498358447 176 IMRLFEEFNRFGVSVLIATH-DLGL 199
Cdd:PRK13540 166 IITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-220 |
2.61e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 79.70 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGG-HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPyvrRQ 80
Cdd:TIGR01842 317 LSVENVTIVPPGGkKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG---KH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLlMDRTVFDNVA--------------------------LPlviDGYShGDINKRVAAaldkvgllgkeryq 134
Cdd:TIGR01842 394 IGYLPQDVEL-FPGTVAENIArfgenadpekiieaaklagvhelilrLP---DGYD-TVIGPGGAT-------------- 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 135 prmLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYrTLTLKAGR 214
Cdd:TIGR01842 455 ---LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDK-ILVLQDGR 530
|
....*.
gi 498358447 215 MYSSGE 220
Cdd:TIGR01842 531 IARFGE 536
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-219 |
2.78e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 78.69 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVME----RPTDGRVFFhgDDVSHIQ---RSQIPYVRRQIGMIFQDH 88
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRF--DDIDLLRlspRERRKLVGHNVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLMDRTvfDNVALPLV--IDGYSH--------GDINKRVAAALDKVGLLGKE---RYQPRMLSGGEQQRVGIARAIVNK 155
Cdd:PRK15093 99 QSCLDPS--ERVGRQLMqnIPGWTYkgrwwqrfGWRKRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 156 PPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-220 |
5.30e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.06 E-value: 5.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQrsqiPYVRRQ 80
Cdd:PRK09700 5 YISMAGIGKSF-GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD----HKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 --IGMIFQDHRLLMDRTVFDNV---ALPL-------VIDgysHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGI 148
Cdd:PRK09700 80 lgIGIIYQELSVIDELTVLENLyigRHLTkkvcgvnIID---WREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 149 ARAIVNKPPLLLADEPTGNLDPQlsmDIMRLFEEFNRF---GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLTNK---EVDYLFLIMNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGM 228
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-200 |
8.58e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 8.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSkVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRvffhgddvshIQRSQipyvRRQ 80
Cdd:PRK09544 4 LVSLENVS-VSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV----------IKRNG----KLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQdhRLLMDRTvfdnvaLPLVID-------GYSHGDIN---KRVAAAldkvGLLGkeryQP-RMLSGGEQQRVGIA 149
Cdd:PRK09544 69 IGYVPQ--KLYLDTT------LPLTVNrflrlrpGTKKEDILpalKRVQAG----HLID----APmQKLSGGETQRVLLA 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 498358447 150 RAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLI 200
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRReLDCAVLMVSHDLHLV 184
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-220 |
9.13e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 76.75 E-value: 9.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 14 GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRS----QIPYVRRQI----GMif 85
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafarKVAYLPQQLpaaeGM-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 86 qdhrllmdrTVFDNVAlplvIDGYS-HGDINK-------RVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPP 157
Cdd:PRK10575 101 ---------TVRELVA----IGRYPwHGALGRfgaadreKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 158 LLLADEPTGNLDPQLSMDIMRLFEEFNRF-GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-219 |
3.05e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.52 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGrvFFHGDDVSHIQRSQIPY-----VRRQIGMIFQD 87
Cdd:PRK14271 32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG--YRYSGDVLLGGRSIFNYrdvleFRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 88 HRLLmDRTVFDNVALPLvidgYSHGDINKR-----VAAALDKVGLLG--KERYQ--PRMLSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK14271 110 PNPF-PMSIMDNVLAGV----RAHKLVPRKefrgvAQARLTEVGLWDavKDRLSdsPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 159 LLADEPTGNLDPQLSMDImrlfEEFNRF---GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKI----EEFIRSladRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-219 |
3.06e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.82 E-value: 3.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKS-TLLKLISVMERpTDGRVFFHG----------DDVSHIQRSQIPYVR-RQIGM 83
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsrqvIELSEQSAAQMRHVRgADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 84 IFQDHRLLMDR--TVFDNVALPLVI-DGYSHGDINKRVAAALDKVGLLGKE----RYqPRMLSGGEQQRVGIARAIVNKP 156
Cdd:PRK10261 109 IFQEPMTSLNPvfTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilsRY-PHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSG 219
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETG 251
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-214 |
3.20e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 3 RFDKVSKVYSGgHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqRSQIPYVRRQIG 82
Cdd:PRK11288 6 SFDGIGKTFPG-VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF--ASTTAALAAGVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQDHRLLMDRTVFDNV---ALPL---VIDgysHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKP 156
Cdd:PRK11288 83 IIYQELHLVPEMTVAENLylgQLPHkggIVN---RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGR 214
Cdd:PRK11288 160 RVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR 217
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-215 |
4.81e-16 |
|
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: 73.60 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRRQIGMIFQDHRLLMDrT 95
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED---LRSSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNValplviDGYSHGDiNKRVAAALdKVGLLGKEryqprmLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMD 175
Cdd:cd03369 98 IRSNL------DPFDEYS-DEEIYGAL-RVSEGGLN------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 498358447 176 IMRLF-EEFNrfGVSVLIATHDLGLIARMRyRTLTLKAGRM 215
Cdd:cd03369 164 IQKTIrEEFT--NSTILTIAHRLRTIIDYD-KILVMDAGEV 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-197 |
1.48e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIS-VMERPT-DGRVFFHGDDV--SHIQRSQipyvRRQIGMIFQDH 88
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSgVYPHGTyEGEIIFEGEELqaSNIRDTE----RAGIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLMDRTVFDNVAL--PLVIDGYSHGD-INKRVAAALDKVGlLGKERYQPRM-LSGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:PRK13549 92 ALVKELSVLENIFLgnEITPGGIMDYDaMYLRAQKLLAQLK-LDINPATPVGnLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190
....*....|....*....|....*....|...
gi 498358447 165 TGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDL 197
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHGIACIYISHKL 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-169 |
1.60e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.68 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 12 SGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyvRRQIGMIF-----Q 86
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE----RRRLGVAYipedrL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 87 DHRLLMDRTVFDNVALPLVID-GYSHG---DINKRVAAALDKVgllgkERYQ---------PRMLSGGEQQRVGIARAIV 153
Cdd:COG3845 344 GRGLVPDMSVAENLILGRYRRpPFSRGgflDRKAIRAFAEELI-----EEFDvrtpgpdtpARSLSGGNQQKVILARELS 418
|
170
....*....|....*.
gi 498358447 154 NKPPLLLADEPTGNLD 169
Cdd:COG3845 419 RDPKLLIAAQPTRGLD 434
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-222 |
1.62e-15 |
|
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: 74.78 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQI 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDhRLLMDRTVFDNVALplvidGYSHGDINKRVAAALDKVGL--------LGkerYQPRM------LSGGEQQRVG 147
Cdd:TIGR01193 551 NYLPQE-PYIFSGSILENLLL-----GAKENVSQDEIWAACEIAEIkddienmpLG---YQTELseegssISGGQKQRIA 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSMDI----MRLFEEfnrfgvSVLIATHDLGlIARMRYRTLTLKAGRMYSSGEDR 222
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIvnnlLNLQDK------TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHD 693
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-182 |
1.95e-15 |
|
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: 71.03 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIS--------VMERPTDGRVFFhgddvshiqRSQ 73
Cdd:cd03223 1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLF---------LPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 74 IPYvrrqigmifqdhrlLMDRTVFDNVALPLvidgyshgdinkrvaaalDKVgllgkeryqprmLSGGEQQRVGIARAIV 153
Cdd:cd03223 72 RPY--------------LPLGTLREQLIYPW------------------DDV------------LSGGEQQRLAFARLLL 107
|
170 180
....*....|....*....|....*....
gi 498358447 154 NKPPLLLADEPTGNLDPQLSMDIMRLFEE 182
Cdd:cd03223 108 HKPKFVFLDEATSALDEESEDRLYQLLKE 136
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
23-211 |
2.13e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 71.80 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 23 FHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSqipyvrRQIGMIFQDHRLLMDRTVFDNVAL 102
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS------RFMAYLGHLPGLKADLSTLENLHF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 103 PLVIdgysHGDINKRV-AAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFE 181
Cdd:PRK13543 106 LCGL----HGRRAKQMpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIS 181
|
170 180 190
....*....|....*....|....*....|
gi 498358447 182 EFNRFGVSVLIATHDLGLIARMRYRTLTLK 211
Cdd:PRK13543 182 AHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
16-202 |
5.22e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.43 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEM-AFLtGHSGAGKSTLLKLISVMERPTDGRVffhgdDVSHIqrsqIPYVRR-----QIGMIF-QDH 88
Cdd:COG4586 36 EAVDDISFTIEPGEIvGFI-GPNGAGKSTTIKMLTGILVPTSGEV-----RVLGY----VPFKRRkefarRIGVVFgQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLMDrtvfdnvaLPlVIDGYS-HGDI----NKRVAAALDK-VGLLGKERY--QP-RMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:COG4586 106 QLWWD--------LP-AIDSFRlLKAIyripDAEYKKRLDElVELLDLGELldTPvRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNR-FGVSVLIATHDLGLIAR 202
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTSHDMDDIEA 220
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-220 |
6.82e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 21 VSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyvRRQIGMIF-----QDHRLLMDRT 95
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNVAlplvidGYSHGDIN-----KRVAAALDK----VGLLGKERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:PRK15439 358 LAWNVC------ALTHNRRGfwikpARENAVLERyrraLNIKFNHAEQAaRTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 166 GNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRmySSGE 220
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGE--ISGA 484
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-197 |
1.62e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 71.67 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 15 HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQ----RSQIPYVRrQIGMIFQDhrl 90
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQldswRSRLAVVS-QTPFLFSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 lmdrTVFDNVAL------PLVIDGYS-----HGDINKRVAAALDKVGLLGKeryqprMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK10789 404 ----TVANNIALgrpdatQQEIEHVArlasvHDDILRLPQGYDTEVGERGV------MLSGGQKQRISIARALLLNAEIL 473
|
170 180 190
....*....|....*....|....*....|....*...
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDL 197
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAHRL 510
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-169 |
3.79e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQI 81
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLLMDrTVFDNVALPLVIDgyshgdiNKRVAAALDKVGL--------------LGKeryQPRMLSGGEQQRVG 147
Cdd:PRK10790 418 AMVQQDPVVLAD-TFLANVTLGRDIS-------EEQVWQALETVQLaelarslpdglytpLGE---QGNNLSVGQKQLLA 486
|
170 180
....*....|....*....|..
gi 498358447 148 IARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-197 |
6.78e-14 |
|
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: 69.85 E-value: 6.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIS-VMERPT-DGRVFFHGDDV--SHIQRSQipyvRRQIGMIFQDH 88
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgVYPHGTwDGEIYWSGSPLkaSNIRDTE----RAGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLMDRTVFDNVAL--PLVIDGY--SHGDINKRVAAALDKVGLLGKERYQPRM-LSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:TIGR02633 88 TLVPELSVAENIFLgnEITLPGGrmAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190
....*....|....*....|....*....|....
gi 498358447 164 PTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDL 197
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAHGVACVYISHKL 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-220 |
7.91e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 21 VSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiQRSQIPYVRRQIGMIFQDHR---LLMDRTVF 97
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV--TRSPQDGLANGIVYISEDRKrdgLVLGMSVK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 98 DNVALPlVIDGYSH--GDINKR--VAAALDKVGLLG---KERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK10762 349 ENMSLT-ALRYFSRagGSLKHAdeQQAVSDFIRLFNiktPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498358447 170 PQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMysSGE 220
Cdd:PRK10762 428 VGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI--SGE 476
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
15-195 |
8.22e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 8.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 15 HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLI--SVMERPTDGRVffhgdDVSHIQRSQipyvrrqigmifqdhrllm 92
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCV-----DVPDNQFGR------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 DRTVFDNValplvidgYSHGDINKrVAAALDKVGL----LGKERYqpRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNL 168
Cdd:COG2401 99 EASLIDAI--------GRKGDFKD-AVELLNAVGLsdavLWLRRF--KELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180
....*....|....*....|....*...
gi 498358447 169 DPQLSMDIMRLFEEFNR-FGVSVLIATH 195
Cdd:COG2401 168 DRQTAKRVARNLQKLARrAGITLVVATH 195
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
9-195 |
1.59e-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: 66.40 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 9 KVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIsvMERP----TDGRVFFHGDDVSHIQRSQIpyVRRQIGMI 84
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTI--MGHPkyevTEGEILFKGEDITDLPPEER--ARLGIFLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 85 FQDhrllmdrtvfdnvalPLVIDGYSHGDinkrvaaaldkvgLLgkeRYQPRMLSGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:cd03217 83 FQY---------------PPEIPGVKNAD-------------FL---RYVNEGFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190
....*....|....*....|....*....|....*
gi 498358447 165 TGNLDpqlsMDIMRL----FEEFNRFGVSVLIATH 195
Cdd:cd03217 132 DSGLD----IDALRLvaevINKLREEGKSVLIITH 162
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
7-220 |
1.61e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 68.92 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYSGgHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQrsqiPYVRRQIG--MI 84
Cdd:PRK15439 17 ISKQYSG-VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT----PAKAHQLGiyLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 85 FQDHRLLMDRTVFDNVALPLVidgySHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 165 TGNLDPqlsMDIMRLFEEFNRF---GVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK15439 168 TASLTP---AETERLFSRIRELlaqGVGIVFISHKLPEIRQLADRISVMRDGTIALSGK 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-202 |
2.59e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.28 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIS-VMERPT-DGRVFFHGDDV--SHIQRSQipyvRRQIGMIFQDH 88
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgVYPHGSyEGEILFDGEVCrfKDIRDSE----ALGIVIIHQEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 89 RLLMDRTVFDNVALPL------VIDgysHGDINKRVAAALDKVGLlgkeRYQPRMLSG----GEQQRVGIARAIVNKPPL 158
Cdd:NF040905 88 ALIPYLSIAENIFLGNerakrgVID---WNETNRRARELLAKVGL----DESPDTLVTdigvGKQQLVEIAKALSKDVKL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 159 LLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIAR 202
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRR 204
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-169 |
7.62e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERP---TDGRVFFHGDDVSHIQRSQI-PYVRRQ---IG-------M 83
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIsAYVQQDdlfIPtltvrehL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 84 IFQDHrLLMDRTVFDNVALplvidgyshgdinKRVAAALDKVGLL-------GKERyQPRMLSGGEQQRVGIARAIVNKP 156
Cdd:TIGR00955 121 MFQAH-LRMPRRVTKKEKR-------------ERVDEVLQALGLRkcantriGVPG-RVKGLSGGERKRLAFASELLTDP 185
|
170
....*....|...
gi 498358447 157 PLLLADEPTGNLD 169
Cdd:TIGR00955 186 PLLFCDEPTSGLD 198
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-169 |
9.66e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 9.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 19 QKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFhgDDVSHIQRSQIPYVRRQIGMIFQDhRLLMDRTVFD 98
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 99 NVALPLVI-------------DGY-SHGDINKR-------------VAAALDKVGLL-GKERYQ---------------- 134
Cdd:PTZ00265 479 NIKYSLYSlkdlealsnyyneDGNdSQENKNKRnscrakcagdlndMSNTTDSNELIeMRKNYQtikdsevvdvskkvli 558
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 135 ------------------PRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PTZ00265 559 hdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-196 |
1.16e-12 |
|
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: 66.11 E-value: 1.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFhGDDVshiqrsQIPYVRRqi 81
Cdd:TIGR03719 323 IEAENLTKAF-GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------KLAYVDQ-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 gmiFQDHrLLMDRTVFDNVAlplviDGYSHGDINKRVAAALDKVGLLG-KERYQPRM---LSGGEQQRVGIARAIVNKPP 157
Cdd:TIGR03719 393 ---SRDA-LDPNKTVWEEIS-----GGLDIIKLGKREIPSRAYVGRFNfKGSDQQKKvgqLSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 498358447 158 LLLADEPTGNLDpqlsMDIMRLFEE-FNRFGVSVLIATHD 196
Cdd:TIGR03719 464 VLLLDEPTNDLD----VETLRALEEaLLNFAGCAVVISHD 499
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-203 |
1.18e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 66.41 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 14 GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMeRPTDGRVFFHGDDVSHIQRSQIpyvRRQIGMIFQDHRLLmD 93
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESW---RKHLSWVGQNPQLP-H 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 94 RTVFDNVALplvidgyshGDIN---KRVAAALDKV-----------GLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK11174 437 GTLRDNVLL---------GNPDasdEQLQQALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 160 LADEPTGNLDPQLSMDIMRLFEEfNRFGVSVLIATHDLGLIARM 203
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW 550
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-201 |
2.38e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 65.65 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFfhgddvshiqRSqiPYVRrq 80
Cdd:PLN03073 508 IISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF----------RS--AKVR-- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQDHRLLMDRTVfdnvaLPLVIDGYSH-GDINKRVAAALDKVGLLGKERYQPR-MLSGGEQQRVGIARAIVNKPPL 158
Cdd:PLN03073 574 MAVFSQHHVDGLDLSS-----NPLLYMMRCFpGVPEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHI 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 159 LLADEPTGNLDpqlsMDIMR-LFEEFNRFGVSVLIATHDLGLIA 201
Cdd:PLN03073 649 LLLDEPSNHLD----LDAVEaLIQGLVLFQGGVLMVSHDEHLIS 688
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-176 |
3.68e-12 |
|
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: 64.93 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVfFHGDDVSHiqRSQIPYVrrqigmifqdhrllMDRTVF 97
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-KHSGRISF--SPQTSWI--------------MPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 98 DNVALPLVIDGYSHGDINKrvAAALDK-VGLLGKERYQPRM-----LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQ 171
Cdd:TIGR01271 505 DNIIFGLSYDEYRYTSVIK--ACQLEEdIALFPEKDKTVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
....*
gi 498358447 172 LSMDI 176
Cdd:TIGR01271 583 TEKEI 587
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-197 |
6.66e-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: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQ-ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVshiqRSQIPYVRR 79
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSSpAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI----LTNISDVHQ 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQdhrllmdrtvFDnvALPLVIDGYSHGDINKRV----AAALDKVG-----LLGKERYQPRM---LSGGEQQRVG 147
Cdd:TIGR01257 2013 NMGYCPQ----------FD--AIDDLLTGREHLYLYARLrgvpAEEIEKVAnwsiqSLGLSLYADRLagtYSGGNKRKLS 2080
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDL 197
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSM 2130
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
21-215 |
7.49e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 7.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 21 VSFHLRKGEMAFLTGHSGAGKSTLLK-LISVMERPTDGRVFFHGDDVShIQRSQiPYVRRQIGMIFQDHR-----LLMDr 94
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVK-IRNPQ-QAIAQGIAMVPEDRKrdgivPVMG- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 95 tVFDNVALPlVIDGYSHG---DINKRVAAALDKVGLLGKERYQPRM----LSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:PRK13549 358 -VGKNITLA-ALDRFTGGsriDDAAELKTILESIQRLKVKTASPELaiarLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498358447 168 LDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:PRK13549 436 IDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-194 |
1.42e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.22 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVF-FHGD--DVSHIQR--SQIPY 76
Cdd:NF033858 2 ARLEGVSHRY-GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDmaDARHRRAvcPRIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 77 VRRQIGmifqdHRLLMDRTVFDNvalplvID------GYSHGDINKRVAAALDKVGLL-------GKeryqprmLSGGEQ 143
Cdd:NF033858 81 MPQGLG-----KNLYPTLSVFEN------LDffgrlfGQDAAERRRRIDELLRATGLApfadrpaGK-------LSGGMK 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 144 QRVGIARAIVNKPPLLLADEPTGNLDPqLSmdiMRLFEEF------NRFGVSVLIAT 194
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPTTGVDP-LS---RRQFWELidriraERPGMSVLVAT 195
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
30-169 |
1.97e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 60.66 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 30 MAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQIGmifqdhrLLMDRTVFDNVALPLVIdgY 109
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLG-------LKLEMTVFENLKFWSEI--Y 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 110 SHGDINKRVAAALDKVGLLGKERYQprmLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK13541 99 NSAETLYAAIHYFKLHDLLDEKCYS---LSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-176 |
2.51e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDV-SHIQRSqipyVRRQIGMIFQDhRLLMDRTV 96
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIgAYGLRE----LRRQFSMIPQD-PVLFDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 FDNValplviDGYSHGDiNKRVAAALDKVGLLGK-----ERYQPRMLSGGEQQRVG------IARAIVNK-PPLLLADEP 164
Cdd:PTZ00243 1401 RQNV------DPFLEAS-SAEVWAALELVGLRERvasesEGIDSRVLEGGSNYSVGqrqlmcMARALLKKgSGFILMDEA 1473
|
170
....*....|..
gi 498358447 165 TGNLDPQLSMDI 176
Cdd:PTZ00243 1474 TANIDPALDRQI 1485
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
21-215 |
2.87e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 62.15 E-value: 2.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 21 VSFHLRKGEMAFLTGHSGAGKSTLLK-LISVMERPTDGRVFFHGDDVShiQRSQIPYVRRQIGMIFQD---HRLLMDRTV 96
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD--IRNPAQAIRAGIAMVPEDrkrHGIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 FDNVALPlVIDGYSH-GDINkrvAAALDKVGLLGKERYQPRM---------LSGGEQQRVGIARAIVNKPPLLLADEPTG 166
Cdd:TIGR02633 357 GKNITLS-VLKSFCFkMRID---AAAELQIIGSAIQRLKVKTaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 498358447 167 NLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-202 |
5.00e-11 |
|
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: 59.79 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIsVME-RPTDGRVFFHGDdVSHIqrSQIPYvrrqigmifqdhrlLMDRT 95
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGS-IAYV--SQEPW--------------IQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNV--ALPLVIDGYshgdinKRV--AAALDK------------VGllgkERyqPRMLSGGEQQRVGIARAIVNKPPLL 159
Cdd:cd03250 82 IRENIlfGKPFDEERY------EKVikACALEPdleilpdgdlteIG----EK--GINLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 160 LADEPTGNLDPQLSMDIM-RLFEEFNRFGVSVLIATHDLGLIAR 202
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH 193
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-214 |
7.86e-11 |
|
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: 60.92 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIS--------VMERPTDGRVFFhgddvshiqRS 72
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY---------VP 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 73 QIPY-----VRRQIgmIFQDHRLLMDRTVFDNVALPLVIDGYSHGDINKRvAAALDKVgllgkeRYQPRMLSGGEQQRVG 147
Cdd:TIGR00954 522 QRPYmtlgtLRDQI--IYPDSSEDMKRRGLSDKDLEQILDNVQLTHILER-EGGWSAV------QDWMDVLSGGEKQRIA 592
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDPQLSmdiMRLFEEFNRFGVSVLIATHDLGLIarmRYRTLTLKAGR 214
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVE---GYMYRLCREFGITLFSVSHRKSLW---KYHEYLLYMDG 653
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-195 |
2.01e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 58.02 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 16 QALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISvmERPTDGRVffHGDdvSHIQRSQIP-YVRRQIGMIFQDHRLLMDR 94
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVI--TGE--ILINGRPLDkNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 95 TVfdNVALplvidgyshgdinkRVAAALdkvgllgkeryqpRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSM 174
Cdd:cd03232 95 TV--REAL--------------RFSALL-------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180
....*....|....*....|.
gi 498358447 175 DIMRLFEEFNRFGVSVLIATH 195
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIH 166
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-196 |
2.22e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.58 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 13 GGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVffhgddvsHI-QRSQIPYvrrqigmiFQDHRLL 91
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCgTKLEVAY--------FDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 92 MD--RTVFDNVAlplviDGYSHGDINKRVAAALdkvGLLGKERYQP-------RMLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:PRK11147 394 LDpeKTVMDNLA-----EGKQEVMVNGRPRHVL---GYLQDFLFHPkramtpvKALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190
....*....|....*....|....*....|....*
gi 498358447 163 EPTGNLDpqlsMDIMRLFEEF-NRFGVSVLIATHD 196
Cdd:PRK11147 466 EPTNDLD----VETLELLEELlDSYQGTVLLVSHD 496
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-168 |
2.90e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.97 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 7 VSKVYSGgHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqRSQIPYVRRQIGMIFQ 86
Cdd:PRK10982 4 ISKSFPG-VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDF--KSSKEALENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 87 DHRLLMDRTVFDNVAL---PLVIDGYSHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADE 163
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
....*
gi 498358447 164 PTGNL 168
Cdd:PRK10982 161 PTSSL 165
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-195 |
2.98e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.15 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIsvMERP----TDGRVFFHGDDVSHI---QRSqipyvRRQIGMIFQD--- 87
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVL--MGHPkyevTSGSILLDGEDILELspdERA-----RAGIFLAFQYpve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 88 ------HRLLmdRTVFDNVALPLVidgySHGDINKRVAAALDKVGLlgKERYQPRML----SGGEQQRVGIARAIVNKPP 157
Cdd:COG0396 89 ipgvsvSNFL--RTALNARRGEEL----SAREFLKLLKEKMKELGL--DEDFLDRYVnegfSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498358447 158 LLLADEPTGNLDpqlsMDIMR-LFEEFNRF---GVSVLIATH 195
Cdd:COG0396 161 LAILDETDSGLD----IDALRiVAEGVNKLrspDRGILIITH 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-196 |
3.03e-10 |
|
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: 59.18 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFH-GDDVSHIQrsQIPY------V 77
Cdd:TIGR03719 8 NRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGYLP--QEPQldptktV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 78 RRQIGMIFQDHRLLMDRtvFDNVALPL-------------------VIDGYSHGDINKRVAAALDKVgllgkeRYQP--- 135
Cdd:TIGR03719 86 RENVEEGVAEIKDALDR--FNEISAKYaepdadfdklaaeqaelqeIIDAADAWDLDSQLEIAMDAL------RCPPwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 136 --RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQlSMDIMRLFeeFNRFGVSVLIATHD 196
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE-SVAWLERH--LQEYPGTVVAVTHD 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
22-205 |
4.96e-10 |
|
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: 56.85 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 22 SFHlRKGEMAF------LTGHSGAGKSTLLKLISVM---ERPTDGRVFFHGDDVSHIQRsqipyVRRQIGMIFQD---HR 89
Cdd:cd03240 11 SFH-ERSEIEFfspltlIVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGE-----VRAQVKLAFENangKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 90 LLMDRT--VFDNVAlplvidgYSH-GDINKRVaaaldkvgLLGKERyqprmLSGGEQQ------RVGIARAIVNKPPLLL 160
Cdd:cd03240 85 YTITRSlaILENVI-------FCHqGESNWPL--------LDMRGR-----CSGGEKVlasliiRLALAETFGSNCGILA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498358447 161 ADEPTGNLDP-QLSMDIMRLFEEFNRFGVS-VLIATHDLGLIARMRY 205
Cdd:cd03240 145 LDEPTTNLDEeNIEESLAEIIEERKSQKNFqLIVITHDEELVDAADH 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-220 |
1.42e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 21 VSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiQRSQIPYVRRQIGMIFQDHR---LLMDRTVF 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID--IRSPRDAIRAGIMLCPEDRKaegIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 98 DNVALP---------LVIDGYSHGDINKRVAAALdKVGLLGKEryQPRM-LSGGEQQRVGIARAIVNKPPLLLADEPTGN 167
Cdd:PRK11288 350 DNINISarrhhlragCLINNRWEAENADRFIRSL-NIKTPSRE--QLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 168 LDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMysSGE 220
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI--AGE 477
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-196 |
1.72e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFhGDDVshiqrsQIPYVRRqi 81
Cdd:PRK11819 325 IEAENLSKSF-GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV------KLAYVDQ-- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 gmiFQDHrLLMDRTVFDNVAlplviDGYSHGDINKR-------VAA----ALD---KVGllgkeryqprMLSGGEQQRVG 147
Cdd:PRK11819 395 ---SRDA-LDPNKTVWEEIS-----GGLDIIKVGNReipsrayVGRfnfkGGDqqkKVG----------VLSGGERNRLH 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 148 IARAIVNKPPLLLADEPTGNLDpqlsMDIMRLFEE-FNRFGVSVLIATHD 196
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD----VETLRALEEaLLEFPGCAVVISHD 501
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-169 |
1.89e-09 |
|
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: 56.40 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVfFHGDDVSHiqRSQIPYVrrqigmifqdhrllMDRTVF 97
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-KHSGRISF--SSQFSWI--------------MPGTIK 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498358447 98 DNVALPLVIDGYSHGDINKrvAAALDK-VGLLGKERYQPR-----MLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:cd03291 116 ENIIFGVSYDEYRYKSVVK--ACQLEEdITKFPEKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-171 |
2.54e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIpyvRRQI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY---RKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIFQDHRLlmdrtvFDNVALPlviDGYSHGDinKRVAAALDKVGLLGK-----ERYQPRMLSGGEQQRVGIARAIVNKP 156
Cdd:PRK10522 400 SAVFTDFHL------FDQLLGP---EGKPANP--ALVEKWLERLKMAHKleledGRISNLKLSKGQKKRLALLLALAEER 468
|
170
....*....|....*
gi 498358447 157 PLLLADEPTGNLDPQ 171
Cdd:PRK10522 469 DILLLDEWAADQDPH 483
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-195 |
3.44e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEM-AFLtGHSGAGKSTLLKLISVMERPTDGRVFFHGDDV--SHIQrsqipyVRRQIGMIFQDHRLLMD 93
Cdd:NF033858 281 AVDHVSFRIRRGEIfGFL-GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIA------TRRRVGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 94 RTVFDNVALplvidgysH--------GDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:NF033858 354 LTVRQNLEL--------HarlfhlpaAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190
....*....|....*....|....*....|....*..
gi 498358447 166 GNLDP-------QLSMDIMRlfeefnRFGVSVLIATH 195
Cdd:NF033858 426 SGVDPvardmfwRLLIELSR------EDGVTIFISTH 456
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
5-200 |
3.49e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.25 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYsggHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKlisvmerptdgrvffhgddvshiqrsqipyvrrQIGMI 84
Cdd:cd03238 1 LTVSGAN---VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------------------------------EGLYA 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 85 FQDHRLLMDRTVFDNVALpLVIDGYShgdinkrvaaALDKVGL----LGKERyqpRMLSGGEQQRVGIARAIVNKPP--L 158
Cdd:cd03238 45 SGKARLISFLPKFSRNKL-IFIDQLQ----------FLIDVGLgyltLGQKL---STLSGGELQRVKLASELFSEPPgtL 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 498358447 159 LLADEPTGNLDPQlsmDIMRLFEEFNRF---GVSVLIATHDLGLI 200
Cdd:cd03238 111 FILDEPSTGLHQQ---DINQLLEVIKGLidlGNTVILIEHNLDVL 152
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-169 |
4.95e-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: 54.72 E-value: 4.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 22 SFHL-------RKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqRSQipYVRRQIGMIFQDhrLLMDR 94
Cdd:cd03237 12 EFTLeveggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY--KPQ--YIKADYEGTVRD--LLSSI 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498358447 95 TVfdnvalplviDGYSHGDINKRVAAALDKVGLLgkERyQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:cd03237 86 TK----------DFYTHPYFKTEIAKPLQIEQIL--DR-EVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
5-178 |
1.08e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLL----KLISvmerpTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:TIGR01271 1222 GLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLS-----TEGEIQIDGVSWNSVTLQTW---RKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQdhRLLMDRTVFDNVALPLviDGYSHGDInKRVAaalDKVGLLGK-ERYQPRM----------LSGGEQQRVGIA 149
Cdd:TIGR01271 1294 FGVIPQ--KVFIFSGTFRKNLDPY--EQWSDEEI-WKVA---EEVGLKSViEQFPDKLdfvlvdggyvLSNGHKQLMCLA 1365
|
170 180
....*....|....*....|....*....
gi 498358447 150 RAIVNKPPLLLADEPTGNLDPqLSMDIMR 178
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDP-VTLQIIR 1393
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-215 |
2.78e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 6 KVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVShiQRSQIPYVRRQIGMIF 85
Cdd:PRK09700 267 EVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS--PRSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 86 QDHR---LLMDRTVFDNVAL-PLVIDG--------YSHGDINKRVAAALDKVGLLGKERYQP-RMLSGGEQQRVGIARAI 152
Cdd:PRK09700 345 ESRRdngFFPNFSIAQNMAIsRSLKDGgykgamglFHEVDEQRTAENQRELLALKCHSVNQNiTELSGGNQQKVLISKWL 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498358447 153 VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-169 |
3.77e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 6 KVSKVYSGGHQALQKVSfhlrkgeMAFLTGH-------SGAGKSTLLKLISVMERPTDGRVFFHgddvshiqrsqiPYVR 78
Cdd:PRK11819 11 RVSKVVPPKKQILKDIS-------LSFFPGAkigvlglNGAGKSTLLRIMAGVDKEFEGEARPA------------PGIK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 79 rqIGMIFQDHRLLMDRTVFDNVALPL-----VIDGYShgDINKRVAAALDKVGLLGKE--RYQPRM-------------- 137
Cdd:PRK11819 72 --VGYLPQEPQLDPEKTVRENVEEGVaevkaALDRFN--EIYAAYAEPDADFDALAAEqgELQEIIdaadawdldsqlei 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498358447 138 ----------------LSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK11819 148 amdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-220 |
5.95e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDdvshiqrsqipyvrrqIGMIFQDHRLLMDRTV 96
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 FDNVALPLVIDGYSHGDInKRVAAALDKVGLLGKERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD---PQL 172
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEI-KAMTPKIIEFSELGEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqtfAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 498358447 173 SMDIMRLFEEFNRfgvSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK13546 182 CLDKIYEFKEQNK---TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-197 |
9.59e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 51.21 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 26 RKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRV-----------FFHG------------DDVSHIQRSQipYVRrQIG 82
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGselqnyftklleGDVKVIVKPQ--YVD-LIP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 83 MIFQDHRLLMDRTVFDNVALPLVIDgyshgdinkrvaaALDKVGLLGKERYQprmLSGGEQQRVGIARAIVNKPPLLLAD 162
Cdd:cd03236 101 KAVKGKVGELLKKKDERGKLDELVD-------------QLELRHVLDRNIDQ---LSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190
....*....|....*....|....*....|....*
gi 498358447 163 EPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDL 197
Cdd:cd03236 165 EPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-168 |
1.30e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.16 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 14 GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHI--QRSQipyvRRQIGMIFQDHRLL 91
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpKSSQ----EAGIGIIHQELNLI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 92 MDRTVFDNVALPLVIDGySHGDIN-KRVAAALDKvgLLGK--ERYQPRMLSG----GEQQRVGIARAIVNKPPLLLADEP 164
Cdd:PRK10762 92 PQLTIAENIFLGREFVN-RFGRIDwKKMYAEADK--LLARlnLRFSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDEP 168
|
....
gi 498358447 165 TGNL 168
Cdd:PRK10762 169 TDAL 172
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
18-170 |
1.48e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISvMERPTD--------GRVFFHGDDVSHIQRsQIPYVRRQIGMifqDHR 89
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT-GDHPQGysndltlfGRRRGSGETIWDIKK-HIGYVSSSLHL---DYR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 90 LLMD-RTV-----FDNVALplvidgYSHGDINKRVAAA--LDKVGLLGKERYQP-RMLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:PRK10938 351 VSTSvRNVilsgfFDSIGI------YQAVSDRQQKLAQqwLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLI 424
|
170
....*....|
gi 498358447 161 ADEPTGNLDP 170
Cdd:PRK10938 425 LDEPLQGLDP 434
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-221 |
1.64e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYSGG-HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQipyVRR 79
Cdd:PLN03232 1234 SIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD---LRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQDHRLLMDRTVFDnvalplvIDGYS-HGDIN--------------KRVAAALDKVGLLGKERYqprmlSGGEQQ 144
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFN-------IDPFSeHNDADlwealerahikdviDRNPFGLDAEVSEGGENF-----SVGQRQ 1378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 145 RVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMR-LFEEFNrfGVSVLIATHDLGLIARMRyRTLTLKAGRM--YSSGED 221
Cdd:PLN03232 1379 LLSLARALLRRSKILVLDEATASVDVRTDSLIQRtIREEFK--SCTMLVIAHRLNTIIDCD-KILVLSSGQVleYDSPQE 1455
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
5-170 |
1.88e-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: 50.24 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 5 DKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTL----LKLISvmerpTDGRVFFHGDDVSHIQRSQIpyvRRQ 80
Cdd:cd03289 7 DLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVPLQKW---RKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 81 IGMIFQ--------------------DHRLLmdrTVFDNVALPLVIDGYShgdinkrvaAALDKVGLLGKeryqpRMLSG 140
Cdd:cd03289 79 FGVIPQkvfifsgtfrknldpygkwsDEEIW---KVAEEVGLKSVIEQFP---------GQLDFVLVDGG-----CVLSH 141
|
170 180 190
....*....|....*....|....*....|
gi 498358447 141 GEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:cd03289 142 GHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
10-219 |
3.43e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 10 VYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLI------SVMER--PTDGRVFFHGDDVSHIQRSQIPYVRRQI 81
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgGGAPRgaRVTGDVTLNGEPLAAIDAPRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMifqdhrllMDRTVFDNVALPLVIDG-YSH-----------GDINKRVAAALDKVGLLGKEryqPRMLSGGEQQRVGIA 149
Cdd:PRK13547 89 PQ--------AAQPAFAFSAREIVLLGrYPHarragalthrdGEIAWQALALAGATALVGRD---VTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 150 RAIVN---------KPPLLLADEPTGNLD----PQLSMDIMRLFEEFNrfgVSVLIATHDLGLIARMRYRTLTLKAGRMY 216
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDlahqHRLLDTVRRLARDWN---LGVLAIVHDPNLAARHADRIAMLADGAIV 234
|
...
gi 498358447 217 SSG 219
Cdd:PRK13547 235 AHG 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
9-195 |
4.22e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 9 KVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISvmERPTDG-------RVFFHGDDVShIQRSqIPYVRRqi 81
Cdd:TIGR00956 770 KIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGvitggdrLVNGRPLDSS-FQRS-IGYVQQ-- 843
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 gmifQD-HrlLMDRTVFDNvalpLVIDGY-------SHGDINKRVAAALDkvgLLGKERYQPRM-------LSGGEQQRV 146
Cdd:TIGR00956 844 ----QDlH--LPTSTVRES----LRFSAYlrqpksvSKSEKMEYVEEVIK---LLEMESYADAVvgvpgegLNVEQRKRL 910
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 498358447 147 GIARAIVNKPPLLL-ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATH 195
Cdd:TIGR00956 911 TIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
14-176 |
4.97e-07 |
|
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: 48.41 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 14 GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPT---DGRVFFHGDDVSHIQRsqipYVRRQIGMIFQDHRL 90
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE----KYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 LMDRTVFDnvalplvidgyshgdinkrvaaALDKVGLLGKERYQpRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP 170
Cdd:cd03233 95 FPTLTVRE----------------------TLDFALRCKGNEFV-RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
....*.
gi 498358447 171 QLSMDI 176
Cdd:cd03233 152 STALEI 157
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
11-197 |
6.13e-07 |
|
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: 48.48 E-value: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 11 YSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQDHRL 90
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 LMDRTVFDNVAL---------PLVIDGYS-HGDINKRVAAALDKVGLLGKEryqprmLSGGEQQRVGIARAIVNKPPLLL 160
Cdd:cd03290 90 LLNATVEENITFgspfnkqryKAVTDACSlQPDIDLLPFGDQTEIGERGIN------LSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498358447 161 ADEPTGNLDPQLS-----MDIMRLFEEFNRfgvSVLIATHDL 197
Cdd:cd03290 164 LDDPFSALDIHLSdhlmqEGILKFLQDDKR---TLVLVTHKL 202
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
15-220 |
7.55e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 15 HQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGddvshiqrsqipyvrrQIGMIFQDHRLLMDR 94
Cdd:PRK13545 37 HYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG----------------SAALIAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 95 TVFDNVALPLVIDGYSHGDInKRVAAALDKVGLLGKERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLS 173
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEKI-KEIIPEIIEFADIGKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 498358447 174 MDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-200 |
9.73e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 9.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 1 MIRFDKVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRV-FFHGDDVSHIQRSQIPYVRR 79
Cdd:PRK10636 312 LLKMEKVSAGY-GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 80 QIGMIFQDHRLLMDRTvfdnvalplvidgyshgdiNKRVAAALDKVGLLGKERYQP-RMLSGGEQQRVGIARAIVNKPPL 158
Cdd:PRK10636 391 DESPLQHLARLAPQEL-------------------EQKLRDYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNL 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 498358447 159 LLADEPTGNLDpqlsMDiMR--LFEEFNRFGVSVLIATHDLGLI 200
Cdd:PRK10636 452 LLLDEPTNHLD----LD-MRqaLTEALIDFEGALVVVSHDRHLL 490
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
24-201 |
1.08e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 48.15 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 24 HLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQRSQIPYVRRQIGMIFQDHRLLMDRTV-FDNVAL 102
Cdd:pfam13304 117 ELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVrGLKLAD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 103 PLVIDGYSHGDINKRVAAALDKVGLLGKERYQ-----PRMLSGGEQQ---RVGIARAIVNKPPLLLADEPTGNLDPQLSM 174
Cdd:pfam13304 197 LNLSDLGEGIEKSLLVDDRLRERGLILLENGGggelpAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLR 276
|
170 180
....*....|....*....|....*..
gi 498358447 175 DIMRLFEEFNRFGVSVLIATHDLGLIA 201
Cdd:pfam13304 277 RLLELLKELSRNGAQLILTTHSPLLLD 303
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-169 |
1.12e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFD-------------KVSKVYsGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIsVMERPTDgrvffHGddvsH 68
Cdd:PRK15064 307 IRFEqdkklhrnaleveNLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-VGELEPD-----SG----T 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 69 IQRSQipyvRRQIGMIFQDH--RLLMDRTVFDNVAL-------PLVIDG------YSHGDINKRVaaaldkvgllgkery 133
Cdd:PRK15064 376 VKWSE----NANIGYYAQDHayDFENDLTLFDWMSQwrqegddEQAVRGtlgrllFSQDDIKKSV--------------- 436
|
170 180 190
....*....|....*....|....*....|....*.
gi 498358447 134 qpRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK15064 437 --KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-220 |
2.26e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLK-LISVMErPTDGRVFfhgddvshIQRSqIPYVRRQIgmifqdhrLLMDRTV 96
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFE-ISEGRVW--------AERS-IAYVPQQA--------WIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 FDNValpLVIDGYSHGDINK--RVAAALDKVGLL--GKERYQPRM---LSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PTZ00243 738 RGNI---LFFDEEDAARLADavRVSQLEADLAQLggGLETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498358447 170 PQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYrTLTLKAGRMYSSGE 220
Cdd:PTZ00243 815 AHVGERVVEECFLGALAGKTRVLATHQVHVVPRADY-VVALGDGRVEFSGS 864
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
110-220 |
2.37e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.42 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 110 SHGDINKRVAAALDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVS 189
Cdd:NF000106 117 SRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGAT 196
|
90 100 110
....*....|....*....|....*....|.
gi 498358447 190 VLIATHDLGLIARMRYRTLTLKAGRMYSSGE 220
Cdd:NF000106 197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGK 227
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
14-165 |
3.08e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 14 GHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLklISVMERP----TDGRVFFHGD--DVSHIQR---SQIPYV---RRQI 81
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELA--MSVFGRSygrnISGTVFKDGKevDVSTVSDaidAGLAYVtedRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 82 GMIfqdhrlLMDrTVFDNVALPlVIDGYS-HGDINK----RVAaaldkvgllgkERYQPRM-------------LSGGEQ 143
Cdd:NF040905 350 GLN------LID-DIKRNITLA-NLGKVSrRGVIDEneeiKVA-----------EEYRKKMniktpsvfqkvgnLSGGNQ 410
|
170 180
....*....|....*....|..
gi 498358447 144 QRVGIARAIVNKPPLLLADEPT 165
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPT 432
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-203 |
3.44e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 45.44 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 27 KGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHIQrsqipyvrrqigmifqdhrllmdrtvfdnvalplvi 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEE------------------------------------ 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 107 dgyshgdinkrvaaaLDKVGLLGKERYQPRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRF 186
Cdd:smart00382 45 ---------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLL 109
|
170 180
....*....|....*....|...
gi 498358447 187 ------GVSVLIATHDLGLIARM 203
Cdd:smart00382 110 llksekNLTVILTTNDEKDLGPA 132
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
116-201 |
3.54e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.45 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 116 KRVAAALDKVGL----LGkeryQP-RMLSGGEQQRVGIARAIVNKPP---LLLADEPTGNLDPQlsmDIMRLFEEFNRF- 186
Cdd:cd03271 147 ARKLQTLCDVGLgyikLG----QPaTTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFH---DVKKLLEVLQRLv 219
|
90
....*....|....*..
gi 498358447 187 --GVSVLIATHDLGLIA 201
Cdd:cd03271 220 dkGNTVVVIEHNLDVIK 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
28-214 |
4.92e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.80 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 28 GEMAFLTGHSGAGKSTLLKLISvmerptdGRVF---FHGDDVSHIQRSQIPYVRRqIGMIFQDHRLLMDRTVFDN---VA 101
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALA-------GRIQgnnFTGTILANNRKPTKQILKR-TGFVTQDDILYPHLTVRETlvfCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 102 LPLVIDGYSHGDINKRVAAALDKVGLLGKERYQP-----RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDI 176
Cdd:PLN03211 166 LLRLPKSLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190
....*....|....*....|....*....|....*....
gi 498358447 177 MRLFEEFNRFGVSVLIATHD-LGLIARMRYRTLTLKAGR 214
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGR 284
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
125-169 |
5.05e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.95 E-value: 5.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 498358447 125 VGLLGKEryqprmLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PTZ00265 1352 VGPYGKS------LSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-213 |
8.98e-06 |
|
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: 46.09 E-value: 8.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTL-LKLISVMErPTDGRVFFHGDDVSHIQRSQIpyvRRQIGMIFQDHRLLmdrtv 96
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINE-SAEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPVLF----- 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 fdNVALPLVIDGYSHGDiNKRVAAALDKVGLLGKERYQP-----------RMLSGGEQQRVGIARAIVNKPPLLLADEPT 165
Cdd:TIGR00957 1373 --SGSLRMNLDPFSQYS-DEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 166 GNLDPQ----LSMDIMRLFEEfnrfgVSVLIATHDLGLIarMRY-RTLTLKAG 213
Cdd:TIGR00957 1450 AAVDLEtdnlIQSTIRTQFED-----CTVLTIAHRLNTI--MDYtRVIVLDKG 1495
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
138-197 |
1.52e-05 |
|
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: 45.16 E-value: 1.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 138 LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDL 197
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-200 |
1.87e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 25 LRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFhGDDVSHiqRSQipYVRRQIGMIFQDhrLLmdRTVFDNVAlpl 104
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISY--KPQ--YIKPDYDGTVED--LL--RSITDDLG--- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 105 viDGYSHGDINKRVAaaLDKvgLLGKERyqpRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDP----QLSMDIMRLF 180
Cdd:PRK13409 430 --SSYYKSEIIKPLQ--LER--LLDKNV---KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVeqrlAVAKAIRRIA 500
|
170 180
....*....|....*....|
gi 498358447 181 EEfnrFGVSVLIATHDLGLI 200
Cdd:PRK13409 501 EE---REATALVVDHDIYMI 517
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
17-215 |
3.77e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 17 ALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGDDVSHiqRSQIPYVRRQIGMIFQDHRllmDRTV 96
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINN--HNANEAINHGFALVTEERR---STGI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 FDNvalpLVIDGYShgdINKRVAAALDKVGLLGKERYQPRM--------------------LSGGEQQRVGIARAIVNKP 156
Cdd:PRK10982 338 YAY----LDIGFNS---LISNIRNYKNKVGLLDNSRMKSDTqwvidsmrvktpghrtqigsLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 157 PLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARMRYRTLTLKAGRM 215
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-195 |
5.04e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.45 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGeMAFLTGHSGAGKSTLLKLISVMERPTDGRV-----FFHGDDVSHIQRSQIPYVRRQIGMIFQDHRLLM 92
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKfdeedFYLGDDPDLPEIEIELTFGSLLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 93 DR------------------------------TVFDNVALPLVIDGYSHGDINKRVaaaldKVGLLGKERYQPRMLSGGE 142
Cdd:COG3593 93 DKeeleealeelneelkealkalnellseylkELLDGLDLELELSLDELEDLLKSL-----SLRIEDGKELPLDRLGSGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 143 QQRVGIA--RAIV-----NKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATH 195
Cdd:COG3593 168 QRLILLAllSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-200 |
6.76e-05 |
|
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: 43.23 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSKVYSGghqalqkvsFHL-------RKGEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFhGDDVSHiqRSQi 74
Cdd:COG1245 342 VEYPDLTKSYGG---------FSLeveggeiREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKISY--KPQ- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 75 pYVRRQIGMIFQDhrlLMDRTVFDNVAlplviDGYSHGDINKRvaaaldkvglLGKER-YQPRM--LSGGEQQRVGIARA 151
Cdd:COG1245 409 -YISPDYDGTVEE---FLRSANTDDFG-----SSYYKTEIIKP----------LGLEKlLDKNVkdLSGGELQRVAIAAC 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 498358447 152 IVNKPPLLLADEPTGNLDP----QLSMDIMRLFEEfnrFGVSVLIATHDLGLI 200
Cdd:COG1245 470 LSRDADLYLLDEPSAHLDVeqrlAVAKAIRRFAEN---RGKTAMVVDHDIYLI 519
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-169 |
9.04e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 28 GEMAFLTGHSGAGKSTLLKLISVMERPTDGRVFFHGD--------DVSHIQRSQIPYV------RRQIgmifqDHRLLMD 93
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawvnqETPALPQPALEYVidgdreYRQL-----EAQLHDA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 94 RTVFDNVALPLV---IDGYSHGDINKRVAAALDKVGLLGKERYQP-RMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PRK10636 102 NERNDGHAIATIhgkLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
133-200 |
1.23e-04 |
|
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: 41.40 E-value: 1.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 133 YQPRM--LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGV-SVLIATHDLGLI 200
Cdd:cd03222 65 YKPQYidLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVL 135
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
138-197 |
1.60e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 1.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 138 LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRfGVSVLIATHDL 197
Cdd:PRK13409 213 LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEHDL 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-169 |
1.93e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 2 IRFDKVSkVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLISVME---RPTDGRVFfH------GDDVSHIQ-- 70
Cdd:PLN03073 178 IHMENFS-ISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQIL-HveqevvGDDTTALQcv 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 71 -RSQIPYVR--RQIGMIFQDHRLLMDRTVFDNVALPLvIDGYSHGDINKRVA-------------AALDKVGLLGKERYQ 134
Cdd:PLN03073 256 lNTDIERTQllEEEAQLVAQQRELEFETETGKGKGAN-KDGVDKDAVSQRLEeiykrlelidaytAEARAASILAGLSFT 334
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 498358447 135 PRM-------LSGGEQQRVGIARAIVNKPPLLLADEPTGNLD 169
Cdd:PLN03073 335 PEMqvkatktFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
138-202 |
3.27e-04 |
|
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: 40.04 E-value: 3.27e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 138 LSGGEQQRVGIARAI----VNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIAR 202
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAEL 146
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
25-203 |
4.75e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.94 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 25 LRKGEMAFLTGHSGAGKSTLLKLISVM---ERPTDGRVFFHGDDVSHI----------QRSQIPY-VRRQIGMIFQDHRl 90
Cdd:cd03279 25 LDNNGLFLICGPTGAGKSTILDAITYAlygKTPRYGRQENLRSVFAPGedtaevsftfQLGGKKYrVERSRGLDYDQFT- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 91 lmdRTVFdnvaLPlvidgysHGDINKrvaaaldkvgLLgkERyQPRMLSGGEQQRVGIARAI--------VNKPPL--LL 160
Cdd:cd03279 104 ---RIVL----LP-------QGEFDR----------FL--AR-PVSTLSGGETFLASLSLALalsevlqnRGGARLeaLF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 498358447 161 ADEPTGNLDPQLSMDIMRLFEEFNRFGVSVLIATHDLGLIARM 203
Cdd:cd03279 157 IDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERI 199
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
18-200 |
5.99e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLL---------------------KLISVMERPtdgrvffhgdDVSHI------- 69
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKP----------DVDSIeglspai 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 70 ---QRSQIPYVRRQIGMIFQDHRLLmdRTVFDNVAlplvidgyshgdINKRVAAALDkVGL--LGKERYQPrMLSGGEQQ 144
Cdd:cd03270 81 aidQKTTSRNPRSTVGTVTEIYDYL--RLLFARVG------------IRERLGFLVD-VGLgyLTLSRSAP-TLSGGEAQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498358447 145 RVGIARAIVNK--PPLLLADEPTGNLDPQlsmDIMRLFEEFNRF---GVSVLIATHDLGLI 200
Cdd:cd03270 145 RIRLATQIGSGltGVLYVLDEPSIGLHPR---DNDRLIETLKRLrdlGNTVLVVEHDEDTI 202
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
136-200 |
7.51e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 39.64 E-value: 7.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498358447 136 RMLSGGEQQRVGIARAIVN---KPPLLLADEPTGNLDPQLSMDIMRLF-EEFNRFGVSVLIATHDLGLI 200
Cdd:COG1106 201 SEESDGTKRLLALAGALLDalaKGGVLLIDEIEASLHPSLLRKLLKLFlDLANKNNAQLIFTTHSTELL 269
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-214 |
1.25e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLLK-LISVMErPTDGRVFFHGDDVSHIQRSQIpyvRRQIGMIFQDhRLLMDRTV 96
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNaLFRIVE-LERGRILIDGCDISKFGLMDL---RKVLGIIPQA-PVLFSGTV 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 97 FDNvalplvIDGYS-HGDINkrVAAALDKVGLLGKERYQPRML-----------SGGEQQRVGIARAIVNKPPLLLADEP 164
Cdd:PLN03130 1330 RFN------LDPFNeHNDAD--LWESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEA 1401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 498358447 165 TGNLDPQLSMDIMR-LFEEFNrfGVSVLIATHDLGLIARMRyRTLTLKAGR 214
Cdd:PLN03130 1402 TAAVDVRTDALIQKtIREEFK--SCTMLIIAHRLNTIIDCD-RILVLDAGR 1449
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-176 |
1.70e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 39.19 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 18 LQKVSFHLRKGEMAFLTGHSGAGKSTLlklISVM--ERPtdgrvffHGDDVSHIQRSQIPYVRrQIGMIFqdhrllmDRT 95
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSL---ISAMlgELS-------HAETSSVVIRGSVAYVP-QVSWIF-------NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 96 VFDNVALPLVIDGYSHGDINKRVAAALDKVGLLGKERYQ----PRMLSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQ 171
Cdd:PLN03232 695 VRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEigerGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAH 774
|
....*
gi 498358447 172 LSMDI 176
Cdd:PLN03232 775 VAHQV 779
|
|
| Twinkle_C |
cd01122 |
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ... |
3-49 |
3.62e-03 |
|
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.
Pssm-ID: 410867 Cd Length: 266 Bit Score: 37.60 E-value: 3.62e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 498358447 3 RFDKVSKVYSGGHQALQKVSFHLRKGEMAFLTGHSGAGKSTLLKLIS 49
Cdd:cd01122 18 NSEQVAGVQWKRFPSLNKLLKGHRRGELTIFTGPTGSGKTTFLSEYS 64
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-196 |
5.25e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.56 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 33 LTGHSGAGKSTLLKLISVMERPTDGRVffhgddvshiqrSQIPYVRrqIGMIFQDHRLLMDRTVFDNV------------ 100
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNV------------SLDPNER--LGKLRQDQFAFEEFTVLDTVimghtelwevkq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498358447 101 ------ALPLVI--DGYSHGDINKRVA-----AALDKVG--LLG----KERYQPRM--LSGGEQQRVGIARAIVNKPPLL 159
Cdd:PRK15064 98 erdriyALPEMSeeDGMKVADLEVKFAemdgyTAEARAGelLLGvgipEEQHYGLMseVAPGWKLRVLLAQALFSNPDIL 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 498358447 160 LADEPTGNLDpqlsMDIMR-LFEEFNRFGVSVLIATHD 196
Cdd:PRK15064 178 LLDEPTNNLD----INTIRwLEDVLNERNSTMIIISHD 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
138-192 |
6.14e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.30 E-value: 6.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 498358447 138 LSGGEQQRVGIARAIVNKPPLLLADEPTGNLDPQLSMDIMRLFEEFNRFGVS-VLI 192
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITlVLV 191
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
7-48 |
6.51e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.61 E-value: 6.51e-03
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....*....|....*....|....*....|....*....|..
gi 498358447 7 VSKVYSGGHQALQKvsfHLrKGEMAFLTGHSGAGKSTLLKLI 48
Cdd:cd01854 68 VSAKTGEGLDELRE---LL-KGKTSVLVGQSGVGKSTLLNAL 105
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