|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-206 |
1.78e-86 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 254.58 E-value: 1.78e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYH 76
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlseRELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHNISLVFQNYNLIDYLTTVENVKL-----GGSGN-----AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASD 146
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALplllaGVSRKerrerARELLERVGLG-DRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-206 |
3.79e-85 |
|
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: 250.87 E-value: 3.79e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHR 77
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlseKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHNISLVFQNYNLIDYLTTVENVKLG----GSGN------AEKLLEEVGIGKEYwQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPlllaGVPKkerrerAEELLERVGLGDRL-NHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-208 |
2.98e-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: 2.98e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHR 77
Cdd:COG3638 2 MLELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgRALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHnISLVFQNYNLIDYLTTVENVKLGGSG------------------NAEKLLEEVGIGKEYWQRnVLQLSGGQQQRVAI 139
Cdd:COG3638 80 RR-IGMIFQQFNLVPRLSVLTNVLAGRLGrtstwrsllglfppedreRALEALERVGLADKAYQR-ADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 140 ARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAISF 208
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVVF 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-206 |
1.72e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 198.74 E-value: 1.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHR 77
Cdd:COG2884 1 MIRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KhNISLVFQNYNLIDYLTTVENVKL-----GGSG-----NAEKLLEEVGI-GKEYwqRNVLQLSGGQQQRVAIARALASD 146
Cdd:COG2884 79 R-RIGVVFQDFRLLPDRTVYENVALplrvtGKSRkeirrRVREVLDLVGLsDKAK--ALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKtAHELGKCVVVVTHSKHLAEEADE-ILEIKNGAI 206
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELVDRMPKrVLELEDGRL 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-206 |
2.35e-63 |
|
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: 196.12 E-value: 2.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDK-TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYH 76
Cdd:COG4181 8 IIELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHNISLVFQNYNLIDYLTTVENV----KLGGSGN----AEKLLEEVGIGK---EYWQrnvlQLSGGQQQRVAIARALAS 145
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVmlplELAGRRDararARALLERVGLGHrldHYPA----QLSGGEQQRVALARAFAT 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-206 |
7.55e-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: 186.57 E-value: 7.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNYHRKhNI 81
Cdd:cd03259 1 LELKGLS---KTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT--GVPPERR-NI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENV----KLGGSGNAEK------LLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIafglKLRGVPKAEIrarvreLLELVGLE-GLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHskHLAEE---ADEILEIKNGAI 206
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVTH--DQEEAlalADRIAVMNEGRI 209
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-208 |
1.05e-59 |
|
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: 187.00 E-value: 1.05e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHRK 78
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HnISLVFQNYNLIDYLTTVENVKLGGSGN------------------AEKLLEEVGIGKEYWQRnVLQLSGGQQQRVAIA 140
Cdd:cd03256 79 Q-IGMIFQQFNLIERLSVLENVLSGRLGRrstwrslfglfpkeekqrALAALERVGLLDKAYQR-ADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAISF 208
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVF 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-204 |
1.43e-59 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 184.70 E-value: 1.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNY--HRKH 79
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 nISLVFQNYNLIDYLTTVENVKLGgsgnaeklleevgigkeywqrnvlqLSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:cd03229 78 -IGMVFQDFALFPHLTVLENIALG-------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSAL 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527143 160 DETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:cd03229 132 DPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-199 |
2.49e-59 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 186.83 E-value: 2.49e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKK-DKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlnyhrkH 79
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG------P 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVKLGGSGN----------AEKLLEEVGIGK--EYWQRnvlQLSGGQQQRVAIARALASDA 147
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRgvpkaerrerARELLELVGLAGfeDAYPH---QLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSkhlAEEA----DEIL 199
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEAvflaDRVV 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-206 |
3.30e-57 |
|
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: 180.22 E-value: 3.30e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-V 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNliDYL--TTV--------ENVKLGGS---GNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAH 148
Cdd:COG1122 78 GLVFQNPD--DQLfaPTVeedvafgpENLGLPREeirERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKtAHELGKCVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDlDLVAELADRVIVLDDGRI 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-206 |
7.84e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 183.38 E-value: 7.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLN-YHRkh 79
Cdd:COG3842 5 ALELENVS---KRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT--GLPpEKR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENV----KLGGSGNAE------KLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVafglRMRGVPKAEirarvaELLELVGLE-GLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 150 LLADEPTGNLD----ETTADEIIALLKktahELGKCVVVVTHSKhlaEEA----DEILEIKNGAI 206
Cdd:COG3842 157 LLLDEPLSALDaklrEEMREELRRLQR----ELGITFIYVTHDQ---EEAlalaDRIAVMNDGRI 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-208 |
1.82e-56 |
|
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: 179.03 E-value: 1.82e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHR 77
Cdd:TIGR02315 1 MLEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHnISLVFQNYNLIDYLTTVENV---KLGGSGN---------------AEKLLEEVGIGKEYWQRnVLQLSGGQQQRVAI 139
Cdd:TIGR02315 79 RR-IGMIFQHYNLIERLTVLENVlhgRLGYKPTwrsllgrfseedkerALSALERVGLADKAYQR-ADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 140 ARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAISF 208
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIVF 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-206 |
2.93e-55 |
|
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: 183.18 E-value: 2.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAY--KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNY 75
Cdd:COG1123 260 LLEVRNLSKRYpvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 HRKHnISLVFQN-YNLIDYLTTV-----ENVKLGGSGN-------AEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARA 142
Cdd:COG1123 340 LRRR-VQMVFQDpYSSLNPRMTVgdiiaEPLRLHGLLSraerrerVAELLERVGLPPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-199 |
3.35e-55 |
|
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: 174.97 E-value: 3.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKD-KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlnyhrkHN 80
Cdd:cd03293 1 LEVRNVSKTYGGGGGaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG------PD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLG----GSGNAEK------LLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGlelqGVPKAEAreraeeLLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527143 151 LADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSkhlAEEA----DEIL 199
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD---IDEAvflaDRVV 203
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-206 |
9.62e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.46 E-value: 9.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:COG4619 1 LELEGLSFRVG---GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTV-ENVKLGGSGN--------AEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLA 152
Cdd:COG4619 77 AYVPQEPALWG--GTVrDNLPFPFQLRerkfdrerALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 153 DEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-204 |
2.89e-54 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 172.27 E-value: 2.89e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKtKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnIS 82
Cdd:cd03225 1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQNYNliDYL--TTV--------ENVKLGGS---GNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:cd03225 79 LVFQNPD--DQFfgPTVeeevafglENLGLPEEeieERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHS-KHLAEEADEILEIKNG 204
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDlDLLLELADRVIVLEDG 210
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-201 |
3.04e-54 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 172.03 E-value: 3.04e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 4 VKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI----TKKGLNYHRKH 79
Cdd:TIGR03608 1 LKNIS---KKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETpplnSKKASKFRREK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 nISLVFQNYNLIDYLTTVENVKLG-------GSGNAEKL---LEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:TIGR03608 78 -LGYLFQNFALIENETVEENLDLGlkykklsKKEKREKKkeaLEKVGLNL-KLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEEADEILEI 201
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIEL 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-206 |
6.31e-54 |
|
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: 172.92 E-value: 6.31e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkglnYHRKH- 79
Cdd:COG1120 1 MLEAENLSVGYG---GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS----LSRREl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 --NISLVFQNYNLIDYLTTVENVKLG--------GSGNAE------KLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARAL 143
Cdd:COG1120 74 arRIAYVPQEPPAPFGLTVRELVALGryphlglfGRPSAEdreaveEALERTGLE-HLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHskHL---AEEADEILEIKNGAI 206
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH--DLnlaARYADRLVLLKDGRI 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-206 |
9.50e-54 |
|
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: 172.29 E-value: 9.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTK-KDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKH 79
Cdd:COG1124 1 MLEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 nISLVFQnynliDYLTTV-----------ENVKLGGSGNAEK----LLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALA 144
Cdd:COG1124 81 -VQMVFQ-----DPYASLhprhtvdrilaEPLRIHGLPDREEriaeLLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-206 |
1.22e-53 |
|
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: 171.61 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYK-TKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT---KKGLNYH 76
Cdd:cd03258 1 MIELKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHnISLVFQNYNLIDYLTTVENV----KLGGSGNAE------KLLEEVGI-GKEywQRNVLQLSGGQQQRVAIARALAS 145
Cdd:cd03258 81 RRR-IGMIFQHFNLLSSRTVFENValplEIAGVPKAEieervlELLELVGLeDKA--DAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEV 219
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-193 |
1.04e-52 |
|
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: 168.58 E-value: 1.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHR 77
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVA--ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgRQLPLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHnISLVFQNYNLIDYLTTVENVKLGgsgnaeklLEEVGIGKEYWQRNV-----------------LQLSGGQQQRVAIA 140
Cdd:TIGR02673 79 RR-IGVVFQDFRLLPDRTVYENVALP--------LEVRGKKEREIQRRVgaalrqvglehkadafpEQLSGGEQQRVAIA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIIALLKKtAHELGKCVVVVTHSKHLAE 193
Cdd:TIGR02673 150 RAIVNSPPLLLADEPTGNLDPDLSERILDLLKR-LNKRGTTVIVATHDLSLVD 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-206 |
1.86e-52 |
|
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: 168.07 E-value: 1.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDK-TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK--KGLNYHR 77
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHNISLVFQN-YNLIDYLTTVE-------NVKLGGSGNAEK------LLEEVGIGKEYWQRNVLQLSGGQQQRVAIARAL 143
Cdd:cd03257 81 RKEIQMVFQDpMSSLNPRMTIGeqiaeplRIHGKLSKKEARkeavllLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-187 |
2.04e-52 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 171.41 E-value: 2.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDK-TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYH 76
Cdd:COG1135 1 MIELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlseRELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKhNISLVFQNYNLIDYLTTVENV----KLGGSGNAE------KLLEEVGIGKeywQRNVL--QLSGGQQQRVAIARALA 144
Cdd:COG1135 81 RR-KIGMIFQHFNLLSSRTVAENValplEIAGVPKAEirkrvaELLELVGLSD---KADAYpsQLSGGQKQRVGIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:COG1135 157 NNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH 199
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-206 |
3.76e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 167.86 E-value: 3.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT--KKGLNYHRK 78
Cdd:COG1126 1 MIEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HnISLVFQNYNLIDYLTTVENVKLG-----------GSGNAEKLLEEVGIGKeywQRNVL--QLSGGQQQRVAIARALAS 145
Cdd:COG1126 78 K-VGMVFQQFNLFPHLTVLENVTLApikvkkmskaeAEERAMELLERVGLAD---KADAYpaQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527143 146 DAHVLLADEPTGNLD-ETTAdEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG1126 154 EPKVMLFDEPTSALDpELVG-EVLDVMRDLAKE-GMTMVVVTHEMGFAREvADRVVFMDGGRI 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-204 |
1.32e-50 |
|
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: 161.40 E-value: 1.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:cd03228 1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTV-ENVklggsgnaeklleevgigkeywqrnvlqLSGGQQQRVAIARALASDAHVLLADEPTGNLD 160
Cdd:cd03228 79 AYVPQDPFLFS--GTIrENI----------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 161 ETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNG 204
Cdd:cd03228 129 PETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-208 |
2.36e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 164.55 E-value: 2.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAY--KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT---KKGLNYH 76
Cdd:TIGR04521 1 IKLKNVSYIYqpGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITakkKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHnISLVFQN--YNLIDylTTVEN------VKLGGSGN-----AEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARAL 143
Cdd:TIGR04521 81 RKK-VGLVFQFpeHQLFE--ETVYKdiafgpKNLGLSEEeaeerVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAISF 208
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIVL 223
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-208 |
3.30e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 162.95 E-value: 3.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKglnyhrKHN 80
Cdd:COG1121 6 AIELENLTVSYG---GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNL-IDYLTTVEN-VKLGGSGN--------------AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALA 144
Cdd:COG1121 77 IGYVPQRAEVdWDFPITVRDvVLMGRYGRrglfrrpsradreaVDEALERVGLE-DLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHS-KHLAEEADEILEIKNGAISF 208
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDlGAVREYFDRVLLLNRGLVAH 219
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-206 |
6.61e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 159.46 E-value: 6.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhnI 81
Cdd:COG1131 1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKL-----GGSGN-----AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFfarlyGLPRKearerIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDKGRI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-206 |
8.63e-49 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 162.55 E-value: 8.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLnyhRKHN 80
Cdd:COG3839 3 SLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP---KDRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENV----KLGGSGNAE------KLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIafplKLRKVPKAEidrrvrEAAELLGLE-DLLDRKPKQLSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 151 LADEPTGNLD----ETTADEIIALLKktahELGKCVVVVTHSkhlAEEA----DEILEIKNGAI 206
Cdd:COG3839 156 LLDEPLSNLDaklrVEMRAEIKRLHR----RLGTTTIYVTHD---QVEAmtlaDRIAVMNDGRI 212
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-206 |
1.12e-48 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 158.28 E-value: 1.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLN---YH 76
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNeraKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHNISLVFQNYNLIDYLTTVENV----------KLGGSGNAEKLLEEVGIGKEYWQRNVlQLSGGQQQRVAIARALASD 146
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVamplligkksVKEAKERAYEMLEKVGLEHRINHRPS-ELSGGERQRVAIARALVNQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:TIGR02211 160 PSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-206 |
1.94e-48 |
|
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: 157.31 E-value: 1.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYH--RKH 79
Cdd:cd03262 1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 nISLVFQNYNLIDYLTTVENVKLG-----------GSGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAH 148
Cdd:cd03262 78 -VGMVFQQFNLFPHLTVLENITLApikvkgmskaeAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-206 |
4.51e-48 |
|
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: 157.01 E-value: 4.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNyhrKHNI 81
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENV----KLGGSGNAE------KLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIafglRLKKLPKAEikervaEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKhlaEEA----DEILEIKNGAI 206
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQ---EEAltmsDRIAVMNKGKI 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-208 |
1.67e-47 |
|
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: 155.00 E-value: 1.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlnyhrkHNIS 82
Cdd:cd03235 1 EVEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER------KRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQNYNL-IDYLTTVENV-------KLGGSGN--------AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASD 146
Cdd:cd03235 72 YVPQRRSIdRDFPISVRDVvlmglygHKGLFRRlskadkakVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKtAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAISF 208
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRE-LRREGMTILVVTHDLGLVLEyFDRVLLLNRTVVAS 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-206 |
1.69e-47 |
|
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: 163.78 E-value: 1.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:COG4988 337 IELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-I 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNynliDYL--TTV-ENVKLGGSgNA-----EKLLEEVGIGKEY------WQRNV----LQLSGGQQQRVAIARAL 143
Cdd:COG4988 414 AWVPQN----PYLfaGTIrENLRLGRP-DAsdeelEAALEAAGLDEFVaalpdgLDTPLgeggRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-206 |
2.08e-47 |
|
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: 155.52 E-value: 2.08e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHR 77
Cdd:COG1127 5 MIEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlseKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHnISLVFQNYNLIDYLTTVENV----------------KLggsgnAEKLLEEVGIgkeywqRNVL-----QLSGGQQQR 136
Cdd:COG1127 82 RR-IGMLFQGGALFDSLTVFENVafplrehtdlseaeirEL-----VLEKLELVGL------PGAAdkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 137 VAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKI 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-206 |
2.59e-47 |
|
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: 155.40 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKglNYHRKHN 80
Cdd:COG4555 1 MIEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKE--PREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGSGN----------AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYglfdeelkkrIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 151 LADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEAlCDRVVILHKGKV 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-206 |
6.09e-47 |
|
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: 152.59 E-value: 6.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkglnYHRKH--- 79
Cdd:cd03214 1 EVENLSVGYG---GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS----LSPKElar 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQnynlidylttvenvklggsgnaekLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:cd03214 74 KIAYVPQ------------------------ALELLGLA-HLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527143 160 DETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDlNLAARYADRVILLKDGRI 176
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-206 |
8.09e-47 |
|
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: 154.03 E-value: 8.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLnyhRKHNI 81
Cdd:cd03296 3 IEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLG--------------GSGNAEKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGlrvkprserppeaeIRAKVHELLKLVQLDW-LADRYPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLA-EEADEILEIKNGAI 206
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-206 |
1.39e-46 |
|
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: 161.09 E-value: 1.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkglNYHRK--- 78
Cdd:COG4987 334 LELEDVSFRY-PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR----DLDEDdlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLIDylTTV-ENVKLGgSGNA--EKL---LEEVGIGKeyWQRNV------------LQLSGGQQQRVAIA 140
Cdd:COG4987 409 RRIAVVPQRPHLFD--TTLrENLRLA-RPDAtdEELwaaLERVGLGD--WLAALpdgldtwlgeggRRLSGGERRRLALA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-206 |
2.49e-46 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 152.48 E-value: 2.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKT-KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI---TKKGLNYHR 77
Cdd:TIGR02982 2 ISIRNLNHYYGHgSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELhgaSKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KhNISLVFQNYNLIDYLTTVENVKLGGSGN-----------AEKLLEEVGIGK--EYWQRNvlqLSGGQQQRVAIARALA 144
Cdd:TIGR02982 82 R-RIGYIFQAHNLLGFLTARQNVQMALELQpnlsyqearerARAMLEAVGLGDhlNYYPHN---LSGGQKQRVAIARALV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:TIGR02982 158 HHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-206 |
6.17e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 154.92 E-value: 6.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkgLNYH-RKHN 80
Cdd:COG1118 3 IEVRNIS---KRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF---TNLPpRERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLG----GSGNAE------KLLEEV---GIGKEYwqrnVLQLSGGQQQRVAIARALASDA 147
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGlrvrPPSKAEirarveELLELVqleGLADRY----PSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKhlaEEA----DEILEIKNGAI 206
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQ---EEAlelaDRVVVMNQGRI 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-206 |
6.73e-46 |
|
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: 151.50 E-value: 6.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHRK 78
Cdd:cd03261 1 IELRGLTKSFG---GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseAELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 hNISLVFQNYNLIDYLTTVENVKLG----GSGNAEKL-------LEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:cd03261 78 -RMGMLFQSGALFDSLTVFENVAFPlrehTRLSEEEIreivlekLEAVGL-RGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKI 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-195 |
7.13e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 152.32 E-value: 7.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAY-KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNyhRkh 79
Cdd:COG4525 3 MLTVRHVSVRYpGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 niSLVFQNYNLIDYLTTVENVKLG----GSGN------AEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNVAFGlrlrGVPKaerrarAEELLALVGL-ADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSkhlAEEA 195
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEA 198
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-204 |
1.07e-45 |
|
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: 149.08 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYhrKHNI 81
Cdd:cd03230 1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV--KRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENvklggsgnaeklleevgigkeywqrnvLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDE 161
Cdd:cd03230 76 GYLPEEPSLYENLTVREN---------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 162 TTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:cd03230 129 ESRREFWELLRELKKE-GKTILLSSHILEEAERlCDRVAILNNG 171
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-205 |
1.26e-45 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 149.94 E-value: 1.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRkhN 80
Cdd:COG4133 2 MLEAENLSCRRG---ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRR--R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKL-----GGSGNAEK---LLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLA 152
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFwaalyGLRADREAideALEAVGLA-GLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489527143 153 DEPTGNLDETTADEIIALLKktAH-ELGKCVVVVTHSkHLAEEADEILEIKNGA 205
Cdd:COG4133 156 DEPFTALDAAGVALLAELIA--AHlARGGAVLLTTHQ-PLELAAARVLDLGDFK 206
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-204 |
3.32e-45 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 149.48 E-value: 3.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNYH--- 76
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTkVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVT--NLSYSqki 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 --RKHNISLVFQNYNLIDYLTTVENVKLG----GSGNAEKL------LEEVGIGKeywQRN--VLQLSGGQQQRVAIARA 142
Cdd:NF038007 79 ilRRELIGYIFQSFNLIPHLSIFDNVALPlkyrGVAKKERIervnqvLNLFGIDN---RRNhkPMQLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHSKHLAEEADEILEIKNG 204
Cdd:NF038007 156 MVSNPALLLADEPTGNLDSKNARAVLQQLKYI-NQKGTTIIMVTHSDEASTYGNRIINMKDG 216
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-206 |
1.09e-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: 147.79 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVsyaYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNyhrKHNI 81
Cdd:cd03301 1 VELENV---TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK---DRDI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENV----KLGGSGNAE--KLLEEV----GIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIafglKLRKVPKDEidERVREVaellQIE-HLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTmADRIAVMNDGQI 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-208 |
3.47e-44 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 147.21 E-value: 3.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYktkkDKTILNnVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLnYHRKhn 80
Cdd:COG3840 1 MLRLDDLTYRY----GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERP-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGS-----GNAEK-----LLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:COG3840 73 VSMLFQENNLFPHLTVAQNIGLGLRpglklTAEQRaqveqALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 151 LADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS----KHLaeeADEILEIKNGAISF 208
Cdd:COG3840 152 LLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDpedaARI---ADRVLLVADGRIAA 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-206 |
4.11e-44 |
|
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: 153.91 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL---DTAVKGTVLCNGEDITKKGLNYHR 77
Cdd:COG1123 4 LLEVRDLSVRY-PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHnISLVFQNY-NLIDYLT-------TVENVKLGGS---GNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASD 146
Cdd:COG1123 83 RR-IGMVFQDPmTQLNPVTvgdqiaeALENLGLSRAearARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRI 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-206 |
7.82e-43 |
|
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: 143.32 E-value: 7.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT---KKGLNYHRK 78
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HnISLVFQNYNLIDYLTTVENVKLGgsgnaeklLEEVGIGKEYWQRNV-----------------LQLSGGQQQRVAIAR 141
Cdd:cd03292 79 K-IGVVFQDFRLLPDRNVYENVAFA--------LEVTGVPPREIRKRVpaalelvglshkhralpAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 142 ALASDAHVLLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHSKHLAEEADE-ILEIKNGAI 206
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-188 |
1.84e-42 |
|
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: 142.70 E-value: 1.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL-----DTAVKGTVLCNGEDITKKGLN-Y 75
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDvL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 HRKHNISLVFQNYNLIDyLTTVENV----KLGGSGN-------AEKLLEEVGIGKEYWQR-NVLQLSGGQQQRVAIARAL 143
Cdd:cd03260 78 ELRRRVGMVFQKPNPFP-GSIYDNVayglRLHGIKLkeelderVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGkcVVVVTHS 188
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYT--IVIVTHN 199
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-187 |
2.45e-42 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 145.71 E-value: 2.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKT-KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYH 76
Cdd:PRK11153 1 MIELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlseKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RkHNISLVFQNYNLIDYLTTVENV----KLGGSGNAE------KLLEEVGIGKeywQRNVL--QLSGGQQQRVAIARALA 144
Cdd:PRK11153 81 R-RQIGMIFQHFNLLSSRTVFDNValplELAGTPKAEikarvtELLELVGLSD---KADRYpaQLSGGQKQRVAIARALA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-206 |
6.82e-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: 149.98 E-value: 6.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:COG2274 474 IELENVSFRY-PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ-I 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTV-ENVKLGGSG----NAEKLLEEVGIGKE-------YWQR---NVLQLSGGQQQRVAIARALASD 146
Cdd:COG2274 552 GVVLQDVFLFS--GTIrENITLGDPDatdeEIIEAARLAGLHDFiealpmgYDTVvgeGGSNLSGGQRQRLAIARALLRN 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:COG2274 630 PRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-206 |
1.03e-41 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 149.10 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYH 76
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldaDALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHNISLVFQNYNLIDYLTTVENVKL----GGSGNAEK------LLEEVGIGKE-YWQRNvlQLSGGQQQRVAIARALAS 145
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVpavyAGLERKQRllraqeLLQRLGLEDRvEYQPS--QLSGGQQQRVSIARALMN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-204 |
1.31e-41 |
|
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: 138.15 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnIS 82
Cdd:cd00267 1 EIENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR-IG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQnynlidylttvenvklggsgnaeklleevgigkeywqrnvlqLSGGQQQRVAIARALASDAHVLLADEPTGNLDET 162
Cdd:cd00267 77 YVPQ------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489527143 163 TADEIIALLKKTAhELGKCVVVVTHSKHLAEEA-DEILEIKNG 204
Cdd:cd00267 115 SRERLLELLRELA-EEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-207 |
1.60e-41 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 143.68 E-value: 1.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKdktiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLnyhRKHN 80
Cdd:NF040840 1 MIRIENLSKDWKEFK----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPP---EKRG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENV----KLGGSGNAE------KLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:NF040840 74 IAYVYQNYMLFPHKTVFENIafglKLRKVPKEEierkvkEIMELLGI-SHLLHRKPRTLSGGEQQRVALARALIIEPKLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 151 LADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSkhlAEEA----DEILEIKNGAIS 207
Cdd:NF040840 153 LLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHN---FEEAlslaDRVGIMLNGRLS 210
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-206 |
1.73e-41 |
|
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: 140.51 E-value: 1.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhNI 81
Cdd:cd03295 1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-KI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENV----KLGGSGNAEK------LLEEVGIG-KEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIalvpKLLKWPKEKIreradeLLALVGLDpAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 151 LADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSkhlAEEA----DEILEIKNGAI 206
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD---IDEAfrlaDRIAIMKNGEI 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-156 |
4.48e-41 |
|
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: 136.62 E-value: 4.48e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnISLVFQNYNLIDYLTTVEN 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 100 VKLGGSGN----------AEKLLEEVGIG---KEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPT 156
Cdd:pfam00005 80 LRLGLLLKglskrekdarAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-206 |
5.15e-41 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 142.78 E-value: 5.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNYHRKHnI 81
Cdd:PRK09452 15 VELRGIS---KSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT--HVPAENRH-V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLG----GSGNAE---------KL--LEEVGigkeywQRNVLQLSGGQQQRVAIARALASD 146
Cdd:PRK09452 89 NTVFQSYALFPHMTVFENVAFGlrmqKTPAAEitprvmealRMvqLEEFA------QRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKhlaEEA----DEILEIKNGAI 206
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQ---EEAltmsDRIVVMRDGRI 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-204 |
2.44e-40 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 137.25 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYH--- 76
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKael 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHNISLVFQNYNLIDYLTTVENVKL----GGSGNAE------KLLEEVGIGKEYWQRNVlQLSGGQQQRVAIARALASD 146
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMplliGKKKPAEinsralEMLAAVGLEHRANHRPS-ELSGGERQRVAIARALVNN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNG 204
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-208 |
3.32e-40 |
|
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: 136.27 E-value: 3.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 22 NVSATFEEGiFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGE--DITKKGLNY--HRKHnISLVFQNYNLIDYLTTV 97
Cdd:cd03297 16 KIDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKKINLppQQRK-IGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 98 ENVKLGGSGNA--------EKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIA 169
Cdd:cd03297 94 ENLAFGLKRKRnredrisvDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527143 170 LLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAISF 208
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQY 212
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-204 |
1.14e-39 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 135.68 E-value: 1.14e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 18 TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHRKHNISLVFQNYNLIDYL 94
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeEARAKLRAKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 95 TTVENVKL-----GGS-----GNAEKLLEEVGIGKEYWQRNVlQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTA 164
Cdd:PRK10584 104 NALENVELpallrGESsrqsrNGAKALLEQLGLGKRLDHLPA-QLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527143 165 DEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNG 204
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-206 |
1.82e-38 |
|
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: 134.93 E-value: 1.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkgLNYHRKHnISLVFQNYNLIDYLTTVENV----KLGGSGNAE- 109
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN--VPPHLRH-INMVFQSYALFPHMTVEENVafglKMRKVPRAEi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 110 -----KLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVV 184
Cdd:TIGR01187 78 kprvlEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVF 156
|
170 180
....*....|....*....|....*.
gi 489527143 185 VTHSKhlaEEA----DEILEIKNGAI 206
Cdd:TIGR01187 157 VTHDQ---EEAmtmsDRIAIMRKGKI 179
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-206 |
3.63e-38 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 138.37 E-value: 3.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:COG1132 340 IEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQ-I 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTV-ENVKLGGSG-------------NAEKLLE--------EVGigkeywQRNVlQLSGGQQQRVAI 139
Cdd:COG1132 417 GVVPQDTFLFS--GTIrENIRYGRPDatdeeveeaakaaQAHEFIEalpdgydtVVG------ERGV-NLSGGQRQRIAI 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 140 ARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-187 |
6.20e-38 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 133.29 E-value: 6.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhN 80
Cdd:COG1125 1 MIEFENVTKRYP--DGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR-R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENV----KLGG------SGNAEKLLEEVGI-GKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:COG1125 78 IGYVIQQIGLFPHMTVAENIatvpRLLGwdkeriRARVDELLELVGLdPEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489527143 150 LLADEPTGNLD----ETTADEIIALLKktahELGKCVVVVTH 187
Cdd:COG1125 158 LLMDEPFGALDpitrEQLQDELLRLQR----ELGKTIVFVTH 195
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
18-207 |
7.91e-38 |
|
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: 134.01 E-value: 7.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 18 TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlnyHRKHNISLVFQNYNLIDYLTTV 97
Cdd:TIGR03265 18 TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLP---PQKRDYGIVFQSYALFPNLTVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 98 ENVKLG----GSGNAE------KLLEEVGI---GKEYWQrnvlQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTA 164
Cdd:TIGR03265 95 DNIAYGlknrGMGRAEvaervaELLDLVGLpgsERKYPG----QLSGGQQQRVALARALATSPGLLLLDEPLSALDARVR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489527143 165 DEIIALLKKTAHELGKCVVVVTHSKhlaEEA----DEILEIKNGAIS 207
Cdd:TIGR03265 171 EHLRTEIRQLQRRLGVTTIMVTHDQ---EEAlsmaDRIVVMNHGVIE 214
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-199 |
9.42e-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: 137.03 E-value: 9.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdkTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ-I 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIdYLTTVENVKLGGSGNAEKLLEEV---------------GIGKEYWQRNVlQLSGGQQQRVAIARALASD 146
Cdd:TIGR02857 399 AWVPQHPFLF-AGTIAENIRLARPDASDAEIREAleragldefvaalpqGLDTPIGEGGA-GLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEIL 199
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIV 527
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-187 |
1.08e-37 |
|
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: 130.63 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNYHR--KH 79
Cdd:cd03219 1 LEVRGLTKRFG---GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPPHEiaRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVKLGGSGN--------------------AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAI 139
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVAAQARtgsglllararreerearerAEELLERVGLA-DLADRPAGELSYGQQRRLEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527143 140 ARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTH 187
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEH 201
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-206 |
1.64e-37 |
|
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: 130.15 E-value: 1.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNyHRKHNI 81
Cdd:cd03299 1 LKVENLSKDWKEFK----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT--NLP-PEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLG---GSGNAEKLLEEV-------GIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGlkkRKVDKKEIERKVleiaemlGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSkhLAEE---ADEILEIKNGAI 206
Cdd:cd03299 153 LDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHD--FEEAwalADKVAIMLNGKL 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-187 |
3.29e-37 |
|
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: 129.77 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayktkkdK-----TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNY 75
Cdd:COG0411 4 LLEVRGLT--------KrfgglVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDIT--GLPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 HR--KHNISLVFQNYNLIDYLTTVENVKLGGSGN-------------------------AEKLLEEVGIGkEYWQRNVLQ 128
Cdd:COG0411 74 HRiaRLGIARTFQNPRLFPELTVLENVLVAAHARlgrgllaallrlprarreerearerAEELLERVGLA-DRADEPAGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 129 LSGGQQQRVAIARALASDAHVLLADEPTG--NLDETtaDEIIALLKKTAHELGKCVVVVTH 187
Cdd:COG0411 153 LSYGQQRRLEIARALATEPKLLLLDEPAAglNPEET--EELAELIRRLRDERGITILLIEH 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-187 |
6.12e-37 |
|
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: 130.94 E-value: 6.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDK-TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL---DTAVKGTVLCNGEDITK---KGL 73
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKlseKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 74 NYHRKHNISLVFQN-YNLIDYLTTVEN-------VKLGGSGN-----AEKLLEEVGIGKEywqRNVL-----QLSGGQQQ 135
Cdd:COG0444 81 RKIRGREIQMIFQDpMTSLNPVMTVGDqiaeplrIHGGLSKAearerAIELLERVGLPDP---ERRLdryphELSGGMRQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527143 136 RVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITH 209
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-195 |
8.14e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 129.05 E-value: 8.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYhrkhn 80
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 iSLVFQNYNLIDYLTTVENVKLG----GSGNAEK------LLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:PRK11248 73 -GVVFQNEGLLPWRNVQDNVAFGlqlaGVEKMQRleiahqMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 151 LADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSkhlAEEA 195
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD---IEEA 192
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-208 |
1.32e-36 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 127.55 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNYHR--KH 79
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPHEraRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVKLGGS----GNAEKLLEEV----GIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:cd03224 76 GIGYVPEGRRIFPELTVEENLLLGAYarrrAKRKARLERVyelfPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAhELGKCVVVVTHSKHLAEE-ADEILEIKNGAISF 208
Cdd:cd03224 156 LDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEiADRAYVLERGRVVL 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-207 |
1.71e-36 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.52 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHR-KH 79
Cdd:PRK09493 1 MIEFKNVS---KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVKLG-----GSGNAE------KLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAH 148
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFGplrvrGASKEEaekqarELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAIS 207
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKvASRLIFIDKGRIA 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-206 |
1.92e-36 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.89 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK-KGLNYHRKh 79
Cdd:COG4604 1 MIEIKNVSKRYG---GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 nISLVFQNYNLIDYLTTVENVKLG------GSGNAE------KLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:COG4604 77 -LAILRQENHINSRLTVRELVAFGrfpyskGRLTAEdreiidEAIAYLDLE-DLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH-----SKHlaeeADEILEIKNGAI 206
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHdinfaSCY----ADHIVAMKDGRV 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-206 |
2.01e-36 |
|
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: 126.84 E-value: 2.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 24 SATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNyhrKHNISLVFQNYNLIDYLTTVENVKLG 103
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPVSMLFQENNLFAHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 104 GS----------GNAEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKK 173
Cdd:cd03298 95 LSpglkltaedrQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLD 173
|
170 180 190
....*....|....*....|....*....|....
gi 489527143 174 TAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:cd03298 174 LHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-188 |
3.57e-36 |
|
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: 132.48 E-value: 3.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhNI 81
Cdd:TIGR02868 335 LELRDLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR-RV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTV-ENVKLGgSGNA-----EKLLEEVGIGKeyWQR-------NVLQ-----LSGGQQQRVAIARAL 143
Cdd:TIGR02868 412 SVCAQDAHLFD--TTVrENLRLA-RPDAtdeelWAALERVGLAD--WLRalpdgldTVLGeggarLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTahELGKCVVVVTHS 188
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-206 |
4.15e-36 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.17 E-value: 4.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNgeDIT---------KK 71
Cdd:PRK11264 3 AIEVKNLV---KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITidtarslsqQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 72 GLNYHRKHNISLVFQNYNLIDYLTTVENVKLG-----------GSGNAEKLLEEVGI-GKE--YWQRnvlqLSGGQQQRV 137
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNFNLFPHRTVLENIIEGpvivkgepkeeATARARELLAKVGLaGKEtsYPRR----LSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 138 AIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDvADRAIFMDQGRI 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-206 |
5.71e-36 |
|
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: 125.45 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKglnyHRKHNIS 82
Cdd:cd03226 1 RIENISFSYK--KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK----ERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQNYNLIDYLTTVEN-VKLG------GSGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEP 155
Cdd:cd03226 75 YVMQDVDYQLFTDSVREeLLLGlkeldaGNEQAETVLKDLDL-YALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527143 156 TGNLDETTADEIIALLKKTAHElGKCVVVVTH-SKHLAEEADEILEIKNGAI 206
Cdd:cd03226 154 TSGLDYKNMERVGELIRELAAQ-GKAVIVITHdYEFLAKVCDRVLLLANGAI 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-206 |
7.93e-36 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.90 E-value: 7.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGE------DITKKGLNY 75
Cdd:COG4161 3 IQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 HRKhNISLVFQNYNLIDYLTTVEN-----VKLGG------SGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALA 144
Cdd:COG4161 80 LRQ-KVGMVFQQYNLWPHLTVMENlieapCKVLGlskeqaREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 145 SDAHVLLADEPTGNLD-ETTAD--EIIALLKKTahelGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG4161 158 MEPQVLLFDEPTAALDpEITAQvvEIIRELSQT----GITQVIVTHEVEFARKvASQVVYMEKGRI 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
2-211 |
8.86e-36 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 124.97 E-value: 8.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTILNnvsatFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlNYHRKhnI 81
Cdd:TIGR01277 1 LALDKVRYEYEHLPMEFDLN-----VADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-PYQRP--V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLGGSG----NAEK------LLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:TIGR01277 73 SMLFQENNLFAHLTVRQNIGLGLHPglklNAEQqekvvdAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAISFLSD 211
Cdd:TIGR01277 152 LDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHlSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
35-206 |
9.72e-36 |
|
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: 128.68 E-value: 9.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI--TKKGLNY--HRKHnISLVFQNYNLIDYLTTVENVKLG----GSG 106
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqdSARGIFLppHRRR-IGYVFQEARLFPHLSVRGNLLYGrkraPRA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 107 NAEKLLEEV----GIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCV 182
Cdd:COG4148 109 ERRISFDEVvellGIG-HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPI 187
|
170 180
....*....|....*....|....*...
gi 489527143 183 VVVTHSkhlAEE----ADEILEIKNGAI 206
Cdd:COG4148 188 LYVSHS---LDEvarlADHVVLLEQGRV 212
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-206 |
1.26e-35 |
|
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: 123.48 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:cd03246 1 LEVENVSFRYPGAE-PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYlTTVENVklggsgnaeklleevgigkeywqrnvlqLSGGQQQRVAIARALASDAHVLLADEPTGNLD- 160
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI----------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDv 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527143 161 --ETTADEIIALLKKTahelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03246 130 egERALNQAIAALKAA----GATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-203 |
1.64e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.13 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYaykTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAG-LDTA--VKGTVLCNGEDITkkGLNYHR 77
Cdd:COG4136 1 MLSLENLTI---TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGRRLT--ALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHnISLVFQNYNLIDYLTTVENVKLG-----GSGN----AEKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAH 148
Cdd:COG4136 76 RR-IGILFQDDLLFPHLSVGENLAFAlpptiGRAQrrarVEQALEEAGLAG-FADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKN 203
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-208 |
1.38e-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: 1.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktILNNVSATFEEGIfYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhnI 81
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVK----LGG--SGNAEK----LLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDyiawLKGipSKEVKArvdeVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 152 ADEPTGNLDettADEIIA---LLKKTAHElgKCVVVVTH-SKHLAEEADEILEIKNGAISF 208
Cdd:cd03264 154 VDEPTAGLD---PEERIRfrnLLSELGED--RIVILSTHiVEDVESLCNQVAVLNKGKLVF 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-204 |
1.94e-34 |
|
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: 121.12 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYK---TKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL--DTAVKGTVLCNGEDITKKGLNYH 76
Cdd:cd03213 4 LSFRNLTVTVKsspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 rkhnISLVFQNYNLIDYLTTVENVklggsgnaeklleevgigkeYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPT 156
Cdd:cd03213 84 ----IGYVPQDDILHPTLTVRETL--------------------MFAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489527143 157 GNLDETTADEIIALLKKTAHElGKCVVVVTH--SKHLAEEADEILEIKNG 204
Cdd:cd03213 140 SGLDSSSALQVMSLLRRLADT-GRTIICSIHqpSSEIFELFDKLLLLSQG 188
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-206 |
2.62e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.48 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkglnyHRKHNI 81
Cdd:PRK11247 13 LLLNAVS---KRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA------EAREDT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLGGSGN----AEKLLEEVGIGKEY--WQRnvlQLSGGQQQRVAIARALASDAHVLLADEP 155
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGLKGQwrdaALQALAAVGLADRAneWPA---ALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527143 156 TGNLDETTADEIIALLKKTAHELGKCVVVVTH--SKHLAeEADEILEIKNGAI 206
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQHGFTVLLVTHdvSEAVA-MADRVLLIEEGKI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-206 |
3.00e-34 |
|
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: 122.75 E-value: 3.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHRKHNISLVFQNYNLIDYLTT 96
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 97 VENVKLG----GSGNAEKL------LEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADE 166
Cdd:cd03294 120 LENVAFGlevqGVPRAEREeraaeaLELVGLEG-WEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489527143 167 IIALLKKTAHELGKCVVVVTHSkhLAEE---ADEILEIKNGAI 206
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHD--LDEAlrlGDRIAIMKDGRL 239
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-187 |
3.03e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 122.22 E-value: 3.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVsyaYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKH- 79
Cdd:COG4598 8 ALEVRDL---HKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 -----------NISLVFQNYNLIDYLTTVENVK------LGGS-----GNAEKLLEEVGIG--KEYWQRnvlQLSGGQQQ 135
Cdd:COG4598 85 adrrqlqrirtRLGMVFQSFNLWSHMTVLENVIeapvhvLGRPkaeaiERAEALLAKVGLAdkRDAYPA---HLSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527143 136 RVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTH 187
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTH 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-206 |
5.51e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.06 E-value: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLnyhRKHNI 81
Cdd:PRK11432 7 VVLKNIT---KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI---QQRDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENV----KLGGSGNAE---------KLLEEVGIGKEYwqrnVLQLSGGQQQRVAIARALASDAH 148
Cdd:PRK11432 81 CMVFQSYALFPHMSLGENVgyglKMLGVPKEErkqrvkealELVDLAGFEDRY----VDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 149 VLLADEPTGNLDET---TADEIIALLKKtahELGKCVVVVTHSKhlaEEA----DEILEIKNGAI 206
Cdd:PRK11432 157 VLLFDEPLSNLDANlrrSMREKIRELQQ---QFNITSLYVTHDQ---SEAfavsDTVIVMNKGKI 215
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-206 |
6.38e-34 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 123.66 E-value: 6.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKglnYHRKHNI 81
Cdd:PRK10851 3 IEIANIKKSFGRTQ---VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL---HARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLGGS-------GNAE-------KLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAFGLTvlprrerPNAAaikakvtQLLEMVQLA-HLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVMSQGNI 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
7.71e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 121.64 E-value: 7.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhN 80
Cdd:PRK13632 7 MIKVENVSFSY-PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK-K 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGSGNA-----------EKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:PRK13632 85 IGIIFQNPDNQFIGATVEDDIAFGLENKkvppkkmkdiiDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-204 |
1.32e-33 |
|
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: 119.53 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtKKDKTILNNVSATFEEG-IFyTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDItkkglNYHRKH- 79
Cdd:cd03263 1 LQIRNLTKTYK-KGTKPAVDDLSLNVYKGeIF-GLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-----RTDRKAa 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 --NISLVFQNYNLIDYLTTVENVKL-----GGSG-----NAEKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:cd03263 74 rqSLGYCPQFDALFDELTVREHLRFyarlkGLPKseikeEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDG 208
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-206 |
1.33e-33 |
|
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: 121.00 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGED-ITKKGLNYHRKHn 80
Cdd:TIGR04520 1 IEVENVSFSY-PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDtLDEENLWEIRKK- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYN--LIDylTTVEN-VKLG----GSGNAE------KLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:TIGR04520 79 VGMVFQNPDnqFVG--ATVEDdVAFGlenlGVPREEmrkrvdEALKLVGM-EDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-206 |
1.56e-33 |
|
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: 120.68 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKT------KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---K 71
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 72 GLNYHRKhNISLVFQN-YNLIDYLTTVENV---------KLGGSGNAEK---LLEEVGIGKEYWQRNVLQLSGGQQQRVA 138
Cdd:TIGR02769 82 QRRAFRR-DVQLVFQDsPSAVNPRMTVRQIigeplrhltSLDESEQKARiaeLLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 139 IARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQI 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-208 |
2.14e-33 |
|
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: 117.80 E-value: 2.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkgLNYHRKHNI 81
Cdd:cd03247 1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD--LEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTvenvklggsgnaekLLEEVGIgkeywqrnvlQLSGGQQQRVAIARALASDAHVLLADEPTGNLDE 161
Cdd:cd03247 78 SVLNQRPYLFD--TT--------------LRNNLGR----------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527143 162 TTADEIIALLKKTAHElgKCVVVVTHskHLA--EEADEILEIKNGAISF 208
Cdd:cd03247 132 ITERQLLSLIFEVLKD--KTLIWITH--HLTgiEHMDKILFLENGKIIM 176
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-206 |
3.37e-33 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 118.46 E-value: 3.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkglnYHR---K 78
Cdd:cd03245 3 IEFRNVSFSYPNQEIPA-LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQ----LDPadlR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLIdYLTTVENVKLGG-SGNAEKLLEEVGIG--KEYWQRNV----LQ-------LSGGQQQRVAIARALA 144
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDNITLGApLADDERILRAAELAgvTDFVNKHPngldLQigergrgLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-188 |
4.20e-33 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 119.37 E-value: 4.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL-----DTAVKGTVLCNGEDITKKG--LN 74
Cdd:COG1117 12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYDPDvdVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 75 YHRKHnISLVFQNYNL----IdYlttvENV----KLGGSGN-------AEKLLEEVGIgkeyW-------QRNVLQLSGG 132
Cdd:COG1117 89 ELRRR-VGMVFQKPNPfpksI-Y----DNVayglRLHGIKSkseldeiVEESLRKAAL----WdevkdrlKKSALGLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 133 QQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLkktaHELGK--CVVVVTHS 188
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELI----LELKKdyTIVIVTHN 212
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-206 |
6.21e-33 |
|
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: 118.41 E-value: 6.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnIS 82
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQNYNLIDylTTV-ENVKLGGSGNAEKLLEEV---------------GIGKEYWQRNVlQLSGGQQQRVAIARALASD 146
Cdd:cd03249 81 LVSQEPVLFD--GTIaENIRYGKPDATDEEVEEAakkanihdfimslpdGYDTLVGERGS-QLSGGQKQRIAIARALLRN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAheLGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-206 |
7.23e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 118.19 E-value: 7.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGE--DIT-----KKGLN 74
Cdd:PRK11124 3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSktpsdKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 75 YHRkhNISLVFQNYNLIDYLTTVEN-----VK-LGGSGN-----AEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARAL 143
Cdd:PRK11124 80 LRR--NVGMVFQQYNLWPHLTVQQNlieapCRvLGLSKDqalarAEKLLERLRL-KPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 144 ASDAHVLLADEPTGNLD-ETTAdEIIALLKKTAhELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDpEITA-QIVSIIRELA-ETGITQVIVTHEVEVARKtASRVVYMENGHI 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-206 |
9.12e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 118.29 E-value: 9.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI---TKKGLNYHR 77
Cdd:COG4559 1 MLEAENLSVRLG---GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 ---KHNISLVFQnynlidyLTTVENVKLGGSGN----------AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALA 144
Cdd:COG4559 78 avlPQHSSLAFP-------FTVEEVVALGRAPHgssaaqdrqiVREALALVGLA-HLAGRSYQTLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 145 -------SDAHVLLADEPTGNLDettadeiIA-------LLKKTAHE-LGkcVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALD-------LAhqhavlrLARQLARRgGG--VVAVLHDLNLAAQyADRILLLHQGRL 218
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
2-188 |
1.02e-32 |
|
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: 118.17 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAV-----KGTVLCNGEDITKKGLN-Y 75
Cdd:TIGR00972 2 IEIENLNLFYG---EKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDLVpgvriEGKVLFDGQDIYDKKIDvV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 HRKHNISLVFQNYNLIDyLTTVENVKLG----GSGN-------AEKLLEEVGIGKEYWQR---NVLQLSGGQQQRVAIAR 141
Cdd:TIGR00972 79 ELRRRVGMVFQKPNPFP-MSIYDNIAYGprlhGIKDkkeldeiVEESLKKAALWDEVKDRlhdSALGLSGGQQQRLCIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527143 142 ALASDAHVLLADEPTGNLDETTADEIIALLkktaHELGK--CVVVVTHS 188
Cdd:TIGR00972 158 ALAVEPEVLLLDEPTSALDPIATGKIEELI----QELKKkyTIVIVTHN 202
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-192 |
1.12e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 118.15 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 6 NVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT-------------KKG 72
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 73 LNYHRKHnISLVFQNYNLIDYLTTVENV-----------KLGGSGNAEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIAR 141
Cdd:PRK10619 87 LRLLRTR-LTMVFQHFNLWSHMTVLENVmeapiqvlglsKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489527143 142 ALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLA 192
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFA 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
1.82e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.18 E-value: 1.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAY--KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTV----LCNGEDI------ 68
Cdd:PRK13631 21 ILRVKNLYCVFdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKnnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 69 ----TKKGLNYHR-KHNISLVFQ--NYNLidYLTTVEN------VKLGGSGN-----AEKLLEEVGIGKEYWQRNVLQLS 130
Cdd:PRK13631 101 tnpySKKIKNFKElRRRVSMVFQfpEYQL--FKDTIEKdimfgpVALGVKKSeakklAKFYLNKMGLDDSYLERSPFGLS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 131 GGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLkKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTmEHVLEVADEVIVMDKGKI 254
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-204 |
2.48e-32 |
|
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: 116.80 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYhrkhniSLVFQNYNLIDYLTTVEN 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDR------MVVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 100 VKLG--------GSGNAEKLLEE----VGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEI 167
Cdd:TIGR01184 75 IALAvdrvlpdlSKSERRAIVEEhialVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527143 168 IALLKKTAHELGKCVVVVTHSkhlAEEA----DEILEIKNG 204
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHD---VDEAlllsDRVVMLTNG 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-206 |
5.64e-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: 115.79 E-value: 5.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA-I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTVE-NVKLGG-SGNAEKLLEEVGIGK---------EYWQRNV----LQLSGGQQQRVAIARALASD 146
Cdd:cd03253 78 GVVPQDTVLFN--DTIGyNIRYGRpDATDEEVIEAAKAAQihdkimrfpDGYDTIVgergLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLKDGRI 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-193 |
1.95e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 115.17 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKT------KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLN 74
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 75 YHR--KHNISLVFQN----YN-------LID----YLTTVEnvKLGGSGNAEKLLEEVGIGKEYWQRNVLQLSGGQQQRV 137
Cdd:PRK10419 83 QRKafRRDIQMVFQDsisaVNprktvreIIReplrHLLSLD--KAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 138 AIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAE 193
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVE 216
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
5-206 |
2.29e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 115.65 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 5 KNVSYAYK--TKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKH--- 79
Cdd:PRK13646 6 DNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvrk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVKLGGSGN-----------AEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAH 148
Cdd:PRK13646 86 RIGMVFQFPESQLFEDTVEREIIFGPKNfkmnldevknyAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-206 |
2.97e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.48 E-value: 2.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHR 77
Cdd:PRK13548 2 MLEARNLSVRLG---GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 -----KHNISLVFqnynlidyltTVEN-VKLGGSGN----------AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIAR 141
Cdd:PRK13548 79 avlpqHSSLSFPF----------TVEEvVAMGRAPHglsraeddalVAAALAQVDLA-HLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 142 ALASDAH------VLLADEPTGNLD----ETTADeiiaLLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:PRK13548 148 VLAQLWEpdgpprWLLLDEPTSALDlahqHHVLR----LARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-208 |
6.88e-31 |
|
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: 112.46 E-value: 6.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTI-LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRkh 79
Cdd:cd03266 1 MITADALTKRFRDVKKTVQaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVKLGG----------SGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAglyglkgdelTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHSKHLAEE-ADEILEIKNGAISF 208
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERlCDRVVVLHRGRVVY 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-206 |
8.13e-31 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 113.26 E-value: 8.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKG---TVL---CNGEDITKkgln 74
Cdd:COG1119 3 LLELRNVTVRRG---GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWE---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 75 yHRKHnISLV---FQNYnlIDYLTTVENVKLGGS---------------GNAEKLLEEVGIGkEYWQRNVLQLSGGQQQR 136
Cdd:COG1119 76 -LRKR-IGLVspaLQLR--FPRDETVLDVVLSGFfdsiglyreptdeqrERARELLELLGLA-HLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527143 137 VAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHskHLAEEADEI---LEIKNGAI 206
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH--HVEEIPPGIthvLLLKDGRV 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
5-206 |
2.03e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.19 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 5 KNVSYAY--KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT----KKGLNYHRK 78
Cdd:PRK13634 6 QKVEHRYqyKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HnISLVFQ--NYNLIDylTTVENVKLGGSGN-----------AEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALAS 145
Cdd:PRK13634 86 K-VGIVFQfpEHQLFE--ETVEKDICFGPMNfgvseedakqkAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAM 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:PRK13634 163 EPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSmEDAARYADQIVVMHKGTV 224
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-206 |
2.98e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 113.26 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAY--KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKK-------- 71
Cdd:PRK13651 3 IKVKNIVKIFnkKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 72 -------GLNYHRK--------HNISLVFQ--NYNLIDylTTVEN------VKLGGSGN-----AEKLLEEVGIGKEYWQ 123
Cdd:PRK13651 83 vleklviQKTRFKKikkikeirRRVGVVFQfaEYQLFE--QTIEKdiifgpVSMGVSKEeakkrAAKYIELVGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 124 RNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHS-KHLAEEADEILEIK 202
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDlDNVLEWTKRTIFFK 239
|
....
gi 489527143 203 NGAI 206
Cdd:PRK13651 240 DGKI 243
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-206 |
4.99e-30 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 116.12 E-value: 4.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkglnYH---RK 78
Cdd:TIGR03375 464 IEFRNVSFAYPGQETPA-LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQ----IDpadLR 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLIdYLTTVENVKLGGSG-NAEKLLEEV--------------GIGKEYWQRNVlQLSGGQQQRVAIARAL 143
Cdd:TIGR03375 539 RNIGYVPQDPRLF-YGTLRDNIALGAPYaDDEEILRAAelagvtefvrrhpdGLDMQIGERGR-SLSGGQRQAVALARAL 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-199 |
8.14e-30 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.86 E-value: 8.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 18 TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeditkkglnyHRKHN--ISLVFQNYNLIDYL- 94
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV--------------RRAGGarVAYVPQRSEVPDSLp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 95 -TTVENVKLGGSGN--------------AEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:NF040873 72 lTVRDLVAMGRWARrglwrrltrddraaVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527143 160 DETTADEIIALLKKtAHELGKCVVVVTHSKHLAEEADEIL 199
Cdd:NF040873 151 DAESRERIIALLAE-EHARGATVVVVTHDLELVRRADPCV 189
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-187 |
8.85e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.37 E-value: 8.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYK--TKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYH--- 76
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 -RKHnISLVFQ--NYNLIDYlTTVENVKLGGSG------NAEKLLEE----VGIGKEYWQRNVLQLSGGQQQRVAIARAL 143
Cdd:PRK13649 83 iRKK-VGLVFQfpESQLFEE-TVLKDVAFGPQNfgvsqeEAEALAREklalVGISESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTH 187
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTH 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
1.06e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 111.05 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHn 80
Cdd:PRK13652 3 LIETRDLCYSYSGSKE--ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGSGN-----------AEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGPINlgldeetvahrVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHL-AEEADEILEIKNGAI 206
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKGRI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-156 |
1.34e-29 |
|
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: 109.69 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNYHR--K 78
Cdd:COG0410 3 MLEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT--GLPPHRiaR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLIDYLTTVENVKLGG-----SGNAEKLLEEVG----IGKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:COG0410 78 LGIGYVPEGRRIFPSLTVEENLLLGAyarrdRAEVRADLERVYelfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
....*..
gi 489527143 150 LLADEPT 156
Cdd:COG0410 158 LLLDEPS 164
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-208 |
1.37e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.91 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAY--KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYH--R 77
Cdd:PRK13637 3 IKIENLTHIYmeGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdiR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KhNISLVFQ--NYNLIDylTTVEN------VKLGGSGN-----AEKLLEEVGIGKE-YWQRNVLQLSGGQQQRVAIARAL 143
Cdd:PRK13637 83 K-KVGLVFQypEYQLFE--ETIEKdiafgpINLGLSEEeienrVKRAMNIVGLDYEdYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 144 ASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAISF 208
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGKCEL 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-195 |
1.38e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.62 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlNYHRKhn 80
Cdd:PRK11607 19 LLEIRNLT---KSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGG----------SGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLkqdklpkaeiASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527143 151 LADEPTGNLDETTAD----EIIALLKKtaheLGKCVVVVTHSKhlaEEA 195
Cdd:PRK11607 172 LLDEPMGALDKKLRDrmqlEVVDILER----VGVTCVMVTHDQ---EEA 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-188 |
1.43e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 109.67 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDitkkglnyHR-----KHNISLVFQNYNLIDYLTTVENVKLG------ 103
Cdd:PRK10771 30 ILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--------HTttppsRRPVSMLFQENNLFSHLTVAQNIGLGlnpglk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 104 ----GSGNAEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELG 179
Cdd:PRK10771 102 lnaaQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQ 180
|
....*....
gi 489527143 180 KCVVVVTHS 188
Cdd:PRK10771 181 LTLLMVSHS 189
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-208 |
3.14e-29 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 109.33 E-value: 3.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKG----------TVLCNGE---D 67
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRlarD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 68 ITKKglnyhRKHNiSLVFQNYNLIDYLTTVENVKLGGSGN------------------AEKLLEEVGIGKEYWQRnVLQL 129
Cdd:PRK09984 81 IRKS-----RANT-GYIFQQFNLVNRLSVLENVLIGALGStpfwrtcfswftreqkqrALQALTRVGMVHFAHQR-VSTL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 130 SGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLA-EEADEILEIKNGAISF 208
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlRYCERIVALRQGHVFY 233
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-206 |
9.84e-29 |
|
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: 9.84e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHNI 81
Cdd:cd03216 1 LELRGIT---KRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQnynlidylttvenvklggsgnaeklleevgigkeywqrnvlqLSGGQQQRVAIARALASDAHVLLADEPTGNLDE 161
Cdd:cd03216 78 AMVYQ------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527143 162 TTADEIIALLKKTAHElGKCVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:cd03216 116 AEVERLFKVIRRLRAQ-GVAVIFISHRlDEVFEIADRVTVLRDGRV 160
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-206 |
1.24e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.70 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYaykTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI--------TKKG 72
Cdd:PRK09536 3 MIDVSDLSV---EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVealsaraaSRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 73 LNYHRKHNISLVFQNYNLIDYLTTVENVKLGGSGNA-----EKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETdraavERAMERTGVAQ-FADRPVTSLSGGERQRVLLARALAQAT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:PRK09536 159 PVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARyCDELVLLADGRV 217
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
35-204 |
1.44e-28 |
|
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: 109.43 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI--TKKG--LNYHRKHnISLVFQNYNLIDYLTTVENVKLG------- 103
Cdd:TIGR02142 28 IFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdSRKGifLPPEKRR-IGYVFQEARLFPHLSVRGNLRYGmkrarps 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 104 -GSGNAEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCV 182
Cdd:TIGR02142 107 eRRISFERVIELLGIG-HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPI 185
|
170 180
....*....|....*....|...
gi 489527143 183 VVVTHS-KHLAEEADEILEIKNG 204
Cdd:TIGR02142 186 LYVSHSlQEVLRLADRVVVLEDG 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
3-186 |
2.54e-28 |
|
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: 106.20 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVK---GTVLCNGEDITKKGLNYHrkh 79
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQFQKC--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 nISLVFQNYNLIDYLTTVENV---------KLGGSGNAEKLLEEVGIGKEYWQR----NVLQLSGGQQQRVAIARALASD 146
Cdd:cd03234 83 -VAYVRQDDILLPGLTVRETLtytailrlpRKSSDAIRKKRVEDVLLRDLALTRiggnLVKGISGGERRRVSIAVQLLWD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVT 186
Cdd:cd03234 162 PKVLILDEPTSGLDSFTALNLVSTLSQLAR--RNRIVILT 199
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-206 |
3.93e-28 |
|
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: 105.68 E-value: 3.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHNI 81
Cdd:TIGR03410 1 LEVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLG--GSGNAEK-----LLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADE 154
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTGlaALPRRSRkipdeIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527143 155 PTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARElADRYYVMERGRV 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-204 |
4.55e-28 |
|
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: 102.91 E-value: 4.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeditkkglnyhrkhni 81
Cdd:cd03221 1 IELENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 slvfqnynlidylTTVENVKLGgsgnaeklleevgigkeYwqrnVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDE 161
Cdd:cd03221 58 -------------TWGSTVKIG-----------------Y----FEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDL 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 162 TTADEIIALLKktahELGKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:cd03221 104 ESIEALEEALK----EYPGTVILVSHDRYFLDQvATKIIELEDG 143
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-204 |
4.83e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 106.74 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhN 80
Cdd:PRK13647 5 IEVEDLHFRYK---DGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS-K 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVE--------NVKLGGS---GNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:PRK13647 81 VGLVFQDPDDQVFSSTVWddvafgpvNMGLDKDeveRRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEwADQVIVLKEG 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-187 |
6.23e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 105.77 E-value: 6.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL-----DTAVKGTVLCNGEDITKKGLNYH 76
Cdd:PRK14247 4 IEIRDLKVSFGQVE---VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHnISLVFQNYNLIDYLTTVENVKLGGSGN-----AEKLLEEVGIGKEYWQ-----RNVL-----QLSGGQQQRVAIAR 141
Cdd:PRK14247 81 RRR-VQMVFQIPNPIPNLSIFENVALGLKLNrlvksKKELQERVRWALEKAQlwdevKDRLdapagKLSGGQQQRLCIAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527143 142 ALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELgkCVVVVTH 187
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTH 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-201 |
6.98e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 109.34 E-value: 6.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayktkkdKTI-----LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNY 75
Cdd:COG1129 4 LLEMRGIS--------KSFggvkaLDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 HRKHNISLVFQNYNLIDYLTTVENVKLG----GSGN---------AEKLLEEVGIGKEYWQRnVLQLSGGQQQRVAIARA 142
Cdd:COG1129 76 AQAAGIAIIHQELNLVPNLSVAENIFLGreprRGGLidwramrrrARELLARLGLDIDPDTP-VGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 143 LASDAHVLLADEPTGNLDETTAD---EIIALLKktahELGKCVVVVTHskHLaeeaDEILEI 201
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVErlfRIIRRLK----AQGVAIIYISH--RL----DEVFEI 206
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-207 |
8.84e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.81 E-value: 8.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 5 KNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLcngedITKKGLNY--HRKHNIS 82
Cdd:PRK11000 7 RNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLF-----IGEKRMNDvpPAERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQNYNLIDYLTTVEN----VKLGGSGNAE--KLLEEVGigkeywqrNVLQL-----------SGGQQQRVAIARALAS 145
Cdd:PRK11000 79 MVFQSYALYPHLSVAENmsfgLKLAGAKKEEinQRVNQVA--------EVLQLahlldrkpkalSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 146 DAHVLLADEPTGNLDET----TADEIIALLKKtaheLGKCVVVVTHSKHLAEE-ADEILEIKNGAIS 207
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAAlrvqMRIEISRLHKR----LGRTMIYVTHDQVEAMTlADKIVVLDAGRVA 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-206 |
1.11e-27 |
|
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: 104.37 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRkhNI 81
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRR--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENV----KLGGSGNAE------KLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLyihaRLYGVPGAErreridELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRI 210
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-206 |
3.68e-27 |
|
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: 103.08 E-value: 3.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:cd03251 1 VEFKNVTFRY-PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTV-ENVKLGGSGNAEKLLEEV---------------GIGKEYWQRNVlQLSGGQQQRVAIARALAS 145
Cdd:cd03251 79 GLVSQDVFLFN--DTVaENIAYGRPGATREEVEEAaraanahefimelpeGYDTVIGERGV-KLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-206 |
3.81e-27 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 107.60 E-value: 3.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKtILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLnyhrK 78
Cdd:PRK11160 339 LTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseAAL----R 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLIDYlTTVENVKLGG-SGNAEKL---LEEVGIGKEYWQRNVL---------QLSGGQQQRVAIARALAS 145
Cdd:PRK11160 414 QAISVVSQRVHLFSA-TLRDNLLLAApNASDEALievLQQVGLEKLLEDDKGLnawlgeggrQLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKtaHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-187 |
4.98e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 4.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHn 80
Cdd:PRK11231 2 TLRTENLTVGYG---TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENV------------KLGGSGNA--EKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASD 146
Cdd:PRK11231 78 LALLPQHHLTPEGITVRELVaygrspwlslwgRLSAEDNArvNQAMEQTRI-NHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTH 187
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLH 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
20-201 |
7.27e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 7.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHNISLVFQNYNLIDYLTTVEN 99
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 100 VKLGGSGN---------AEKLLEEvgIGKEY-----WQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTAD 165
Cdd:COG3845 101 IVLGLEPTkggrldrkaARARIRE--LSERYgldvdPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEAD 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 489527143 166 EIIALLKKTAHElGKCVVVVTHskHLaeeaDEILEI 201
Cdd:COG3845 179 ELFEILRRLAAE-GKSIIFITH--KL----REVMAI 207
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-206 |
1.03e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEG--IFytIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeditKKGlnyhrk 78
Cdd:COG0488 315 VLELEGLSKSYG---DKTLLDDLSLRIDRGdrIG--LIGPNGAGKSTLLKLLAGELEPDSGTV--------KLG------ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVF--QNYNLIDY-LTTVENVKLGGSGNAEK----LLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:COG0488 376 ETVKIGYfdQHQEELDPdKTVLDELRDGAPGGTEQevrgYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAhelGkCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRvATRILEFEDGGV 507
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-206 |
1.58e-26 |
|
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: 105.92 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKT-KKDKTILNNVSATFEEGIFYTIVGPSGAGKT----TLLSLLAGLDTAVKGTVLCNGEDITK---KG 72
Cdd:COG4172 6 LLSVEDLSVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlseRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 73 LNYHRKHNISLVFQnynliDYLT------TVEN-------VKLGGSGNAEK-----LLEEVGIgKEYWQRnvL-----QL 129
Cdd:COG4172 86 LRRIRGNRIAMIFQ-----EPMTslnplhTIGKqiaevlrLHRGLSGAAARaraleLLERVGI-PDPERR--LdayphQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 130 SGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEI 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-206 |
1.59e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.92 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 4 VKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngedITKKGLNyhrkhnISL 83
Cdd:COG0488 1 LENLSKSFG---GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV------SIPKGLR------IGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 84 VFQNYNLIDYLTTVENVkLGGSG-------------------------------------------NAEKLLEEVGIGKE 120
Cdd:COG0488 66 LPQEPPLDDDLTVLDTV-LDGDAelraleaeleeleaklaepdedlerlaelqeefealggweaeaRAEEILSGLGFPEE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 121 YWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLD-ETtadeiIALLKKTAHELGKCVVVVTHSKHLAEE-ADEI 198
Cdd:COG0488 145 DLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDlES-----IEWLEEFLKNYPGTVLVVSHDRYFLDRvATRI 219
|
....*...
gi 489527143 199 LEIKNGAI 206
Cdd:COG0488 220 LELDRGKL 227
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-204 |
1.76e-26 |
|
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: 100.62 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKT--ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGeditkkglnyhrkh 79
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQN---YNlidylTTV-ENVKLGGSGNAEKLLE--------------------EVGIgkeywqrNVLQLSGGQQQ 135
Cdd:cd03250 67 SIAYVSQEpwiQN-----GTIrENILFGKPFDEERYEKvikacalepdleilpdgdltEIGE-------KGINLSGGQKQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 136 RVAIARALASDAHVLLADEPTGNLDETTADEII--ALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNG 204
Cdd:cd03250 135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLLLN--NKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-206 |
1.92e-26 |
|
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: 100.75 E-value: 1.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkglNYHRKHNI 81
Cdd:cd03268 1 LKTNDLT---KTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK---NIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLGGSG------NAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEP 155
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLlgirkkRIDEVLDVVGL-KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 156 TGNLDETTADEIIALLKKTAHElGKCVVVvthSKHLAEE----ADEILEIKNGAI 206
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQ-GITVLI---SSHLLSEiqkvADRIGIINKGKL 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-206 |
1.96e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 102.50 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLnYHRKHN 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENV-WDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGSGN-----------AEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:PRK13650 83 IGMVFQNPDNQFVGATVEDDVAFGLENkgipheemkerVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-209 |
1.97e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 105.90 E-value: 1.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 12 KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTA---VKGTVLCNGEDITKKGLnyhrkHNIS-LVFQN 87
Cdd:TIGR00955 33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEM-----RAISaYVQQD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 88 YNLIDYLTTVEN------VKLGGSGNAEK-------LLEEVG--------IGKEywqRNVLQLSGGQQQRVAIARALASD 146
Cdd:TIGR00955 108 DLFIPTLTVREHlmfqahLRMPRRVTKKEkrervdeVLQALGlrkcantrIGVP---GRVKGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTH--SKHLAEEADEILEIKNGAISFL 209
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHqpSSELFELFDKIILMAEGRVAYL 248
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-206 |
2.39e-26 |
|
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: 101.01 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNY-HRKhn 80
Cdd:cd03248 12 VKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSK-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNL--------IDY-LTTV--ENVKLGGSG-NAEKLLEEV--GIGKEYWQRNVlQLSGGQQQRVAIARALASD 146
Cdd:cd03248 90 VSLVGQEPVLfarslqdnIAYgLQSCsfECVKEAAQKaHAHSFISELasGYDTEVGEKGS-QLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDeTTADEIIALLKKTAHElGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03248 169 PQVLILDEATSALD-AESEQQVQQALYDWPE-RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-206 |
2.69e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 105.57 E-value: 2.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:TIGR00958 479 IEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-V 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNL--------IDY-LTTVENVKLGGSG---NAEKLLEEV--GIGKEYWQRNVlQLSGGQQQRVAIARALASDA 147
Cdd:TIGR00958 558 ALVGQEPVLfsgsvrenIAYgLTDTPDEEIMAAAkaaNAHDFIMEFpnGYDTEVGEKGS-QLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 148 HVLLADEPTGNLDEttadEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:TIGR00958 637 RVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-193 |
2.83e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 100.72 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKtiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHR 77
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQA--LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknREVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHnISLVFQNYNLIDYLTTVENVKL-----GGSGN-----AEKLLEEVGI---GKEYwqrnVLQLSGGQQQRVAIARALA 144
Cdd:PRK10908 79 RQ-IGMIFQDHHLLMDRTVYDNVAIpliiaGASGDdirrrVSAALDKVGLldkAKNF----PIQLSGGEQQRVGIARAVV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHSKHLAE 193
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLIS 201
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-206 |
4.72e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 104.72 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:PRK11176 342 IEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ-V 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNL--------IDYLTT--------VENVKLG-GSGNAEKL---LEEVgIGKeywqrNVLQLSGGQQQRVAIAR 141
Cdd:PRK11176 420 ALVSQNVHLfndtiannIAYARTeqysreqiEEAARMAyAMDFINKMdngLDTV-IGE-----NGVLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 142 ALASDAHVLLADEPTGNLDeTTADEII--AL--LKKTahelgKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK11176 494 ALLRDSPILILDEATSALD-TESERAIqaALdeLQKN-----RTSLVIAHRLSTIEKADEILVVEDGEI 556
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-206 |
7.52e-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: 99.61 E-value: 7.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnIS 82
Cdd:cd03254 4 EFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM-IG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQNynliDYL---TTVENVKLGGSGNAE----KLLEEVGIG----------KEYWQRNVLQLSGGQQQRVAIARALAS 145
Cdd:cd03254 81 VVLQD----TFLfsgTIMENIRLGRPNATDeeviEAAKEAGAHdfimklpngyDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKI 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-204 |
8.72e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 8.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYK--TKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT----KKGLNY 75
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 HRKhNISLVFQNYNLIDYLTTV-ENVKLG----------GSGNAEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALA 144
Cdd:PRK13641 83 LRK-KVSLVFQFPEAQLFENTVlKDVEFGpknfgfsedeAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHS-KHLAEEADEILEIKNG 204
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVLEHG 221
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-206 |
9.79e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.95 E-value: 9.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKglnyhrkhn 80
Cdd:COG4152 1 MLELKGLT---KRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 islvfqNYNLIDYL---------TTVENV-----KLGG------SGNAEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIA 140
Cdd:COG4152 69 ------DRRRIGYLpeerglypkMKVGEQlvylaRLKGlskaeaKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 141 RALASDAHVLLADEPTGNLD----ETTADEIIALLKKtahelGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDpvnvELLKDVIRELAAK-----GTTVIFSSHQMELVEElCDRIVIINKGRK 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-206 |
1.23e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 99.74 E-value: 1.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL----DTAVK--GTVLCNGEDITKKGLNYH 76
Cdd:PRK14246 9 DVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiyDSKIKvdGKVLYFGKDIFQIDAIKL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 RKHnISLVFQNYNLIDYLTTVENVK--LGGSGNAEK---------LLEEVGIGKEYWQR---NVLQLSGGQQQRVAIARA 142
Cdd:PRK14246 89 RKE-VGMVFQQPNPFPHLSIYDNIAypLKSHGIKEKreikkiveeCLRKVGLWKEVYDRlnsPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGkcVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIA--IVIVSHNpQQVARVADYVAFLYNGEL 230
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-206 |
3.27e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 99.31 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 6 NVSYAY--KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI---TKKGLNYHR-KH 79
Cdd:PRK13645 11 NVSYTYakKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanLKKIKEVKRlRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQ--NYNLidYLTTVE-NVKLG----GSGNAE------KLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASD 146
Cdd:PRK13645 91 EIGLVFQfpEYQL--FQETIEkDIAFGpvnlGENKQEaykkvpELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEADEILEIKNGAI 206
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNmDQVLRIADEVIVMHEGKV 229
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-160 |
4.11e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 100.30 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNV--SYAYKTKkdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlnyHRK 78
Cdd:PRK11650 3 GLKLQAVrkSYDGKTQ----VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE---PAD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLIDYLTTVENV----KLGGSGNAE---------KLLEevgIGkEYWQRNVLQLSGGQQQRVAIARALAS 145
Cdd:PRK11650 76 RDIAMVFQNYALYPHMSVRENMayglKIRGMPKAEieervaeaaRILE---LE-PLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170
....*....|....*
gi 489527143 146 DAHVLLADEPTGNLD 160
Cdd:PRK11650 152 EPAVFLFDEPLSNLD 166
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-204 |
5.41e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 98.37 E-value: 5.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKT------KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKglNY 75
Cdd:COG4167 5 LEVRNLSKTFKYrtglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYG--DY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 -HRKHNISLVFQNYN-----------LIDylttvENVKLGGSGNAEK-------LLEEVGIGKEYWQRNVLQLSGGQQQR 136
Cdd:COG4167 83 kYRCKHIRMIFQDPNtslnprlnigqILE-----EPLRLNTDLTAEEreerifaTLRLVGLLPEHANFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 137 VAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS----KHLaeeADEILEIKNG 204
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHlgivKHI---SDKVLVMHQG 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-188 |
5.59e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 98.23 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYK--TKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlNYHRK 78
Cdd:COG1101 1 MLELKNLSKTFNpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQN------YNlidyLTTVENV----------KLGGSGNAEK------LLEEVGIGKEywQR---NVLQLSGGQ 133
Cdd:COG1101 80 KYIGRVFQDpmmgtaPS----MTIEENLalayrrgkrrGLRRGLTKKRrelfreLLATLGLGLE--NRldtKVGLLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 134 QQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS 188
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-187 |
6.32e-25 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 96.66 E-value: 6.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAyktKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRkhNI 81
Cdd:TIGR01189 1 LAARNLACS---RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE--NI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKL------GGSGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEP 155
Cdd:TIGR01189 76 LYLGHLPGLKPELSALENLHFwaaihgGAQRTIEDALAAVGL-TGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|...
gi 489527143 156 TGNLDETTADEIIALLkkTAH-ELGKCVVVVTH 187
Cdd:TIGR01189 155 TTALDKAGVALLAGLL--RAHlARGGIVLLTTH 185
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-204 |
7.67e-25 |
|
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: 96.58 E-value: 7.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGeditkKGLNYHRKHNI 81
Cdd:cd03269 1 LEVENVT---KRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SL------VFQNYNLID---YLTTVENVKLG-GSGNAEKLLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:cd03269 73 GYlpeergLYPKMKVIDqlvYLAQLKGLKKEeARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 152 ADEPTGNLDETTADeiiaLLKKTAHEL---GKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:cd03269 152 LDEPFSGLDPVNVE----LLKDVIRELaraGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-211 |
8.40e-25 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 101.03 E-value: 8.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKT--ILNNVSATFEEG--IFytIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHR 77
Cdd:COG4615 328 LELRGVTYRYPGEDGDEgfTLGPIDLTIRRGelVF--IVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHnISLVFQNYNLIDYLttvenvkLGGSGN-----AEKLLEEVGIgkeywQRNV---------LQLSGGQQQRVAIARAL 143
Cdd:COG4615 406 QL-FSAVFSDFHLFDRL-------LGLDGEadparARELLERLEL-----DHKVsvedgrfstTDLSQGQRKRLALLVAL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 144 ASDAHVLLadeptgnLDETTAD-----------EIIALLKKtaheLGKCVVVVTHSKHLAEEADEILEIKNGAISFLSD 211
Cdd:COG4615 473 LEDRPILV-------FDEWAADqdpefrrvfytELLPELKA----RGKTVIAISHDDRYFDLADRVLKMDYGKLVELTG 540
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-206 |
1.84e-24 |
|
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: 100.21 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkglNYHRKhni 81
Cdd:COG4618 331 LSVENLTVVPPGSK-RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDRE--- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 slVFQNYnlIDYL---------TTVENVKLGGSGNAEKLLE--------------------EVGIGKeywqrnvLQLSGG 132
Cdd:COG4618 403 --ELGRH--IGYLpqdvelfdgTIAENIARFGDADPEKVVAaaklagvhemilrlpdgydtRIGEGG-------ARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 133 QQQRVAIARALASDAHVLLADEPTGNLDE------TTAdeiIALLKKTahelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDDegeaalAAA---IRALKAR----GATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-206 |
2.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.08 E-value: 2.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKT---KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHR 77
Cdd:PRK13633 4 MIKCKNVSYKYESneeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHNISLVFQNY-NLIDYLTTVENVKLGGSG----------NAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASD 146
Cdd:PRK13633 84 RNKAGMVFQNPdNQIVATIVEEDVAFGPENlgippeeireRVDESLKKVGM-YEYRRHAPHLLSGGQKQRVAIAGILAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13633 163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-204 |
2.95e-24 |
|
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: 94.62 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 5 KNVSYAYKTKK-DKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTA--VKGTVLCNGEDITKkglNYHRKhnI 81
Cdd:cd03232 7 KNLNYTVPVKGgKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDK---NFQRS--T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLGGsgnaeklleevgigkeyWQRNvlqLSGGQQQRVAIARALASDAHVLLADEPTGNLDE 161
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSA-----------------LLRG---LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 162 TTADEIIALLKKTAHElGKCVVVVTH--SKHLAEEADEILEIKNG 204
Cdd:cd03232 142 QAAYNIVRFLKKLADS-GQAILCTIHqpSASIFEKFDRLLLLKRG 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-201 |
3.16e-24 |
|
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: 94.04 E-value: 3.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkdktiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHN 80
Cdd:cd03215 4 VLEVRGLSVKGA-------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLV---FQNYNLIDYLTTVENVKLGgsgnaeklleevgigkeywqrnvLQLSGGQQQRVAIARALASDAHVLLADEPTG 157
Cdd:cd03215 77 IAYVpedRKREGLVLDLSVAENIALS-----------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 158 NLDETTADEIIALLKKTAHElGKCVVVVThskhlaEEADEILEI 201
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADA-GKAVLLIS------SELDELLGL 170
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-206 |
3.40e-24 |
|
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: 99.41 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:TIGR02203 331 VEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ-V 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYlTTVENVKLGGSGNAEK-----------LLEEV-----GIGKEYWQRNVLqLSGGQQQRVAIARALAS 145
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRTEQADRaeieralaaayAQDFVdklplGLDTPIGENGVL-LSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRI 545
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-206 |
3.47e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.73 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKD--KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT----KKGLN 74
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 75 YHRKhNISLVFQ--NYNLIDYlTTVENVKLG------GSGNAEKL----LEEVGIGKEYWQRNVLQLSGGQQQRVAIARA 142
Cdd:PRK13643 81 PVRK-KVGVVFQfpESQLFEE-TVLKDVAFGpqnfgiPKEKAEKIaaekLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLkKTAHELGKCVVVVTH-SKHLAEEADEILEIKNGAI 206
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHlMDDVADYADYVYLLEKGHI 222
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-206 |
5.58e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 98.76 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 16 DKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLdTAVKGTVLCNGEDITKKGLNYHRKHnISLVFQNYNLIdYLT 95
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLP-HGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 96 TVENVKLGGSGNAE----KLLEEVGIgKEYWQR-----------NVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLD 160
Cdd:PRK11174 439 LRDNVLLGNPDASDeqlqQALENAWV-SEFLPLlpqgldtpigdQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527143 161 ETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK11174 518 AHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQI 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-206 |
6.18e-24 |
|
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: 94.86 E-value: 6.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:cd03252 1 ITFEHVRFRYKPD-GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ-V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNyNLIDYLTTVENVKLGGSGNAEKLLEEV---------------GIGKEYWQRNVlQLSGGQQQRVAIARALASD 146
Cdd:cd03252 79 GVVLQE-NVLFNRSIRDNIALADPGMSMERVIEAaklagahdfiselpeGYDTIVGEQGA-GLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-188 |
7.90e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL-----DTAVKGTVLCNGEDI-TKKGLN 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIySPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 75 YHRKHNISLVFQNYNLIDyLTTVENV----KLGGSGNAEKLLEEVG---IGKEYWQR-------NVLQLSGGQQQRVAIA 140
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVvyglRLKGIKDKQVLDEAVEkslKGASIWDEvkdrlhdSALGLSGGQQQRVCIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIiallKKTAHELGK--CVVVVTHS 188
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKI----EETLLGLKDdyTMLLVTRS 206
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-190 |
8.77e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.10 E-value: 8.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL-----DTAVKGTVLCNGEDITKKGLNYH 76
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 R-KHNISLVFQNYNLIDyLTTVENVKLG-----------------GSGNAEKLLEEVgigKEYWQRNVLQLSGGQQQRVA 138
Cdd:PRK14258 85 RlRRQVSMVHPKPNLFP-MSVYDNVAYGvkivgwrpkleiddiveSALKDADLWDEI---KHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527143 139 IARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKH 190
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLH 212
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-199 |
2.05e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHn 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYlTTVENVKL-----GGSGNAEKL---LEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLA 152
Cdd:PRK10247 83 VSYCAQTPTLFGD-TVYDNLIFpwqirNQQPDPAIFlddLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489527143 153 DEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEIL 199
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-194 |
2.24e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 95.03 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK--KGLNYHRKHNISLVFQN-YNLIDYLTT 96
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadPEAQKLLRQKIQIVFQNpYGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 97 VE---------NVKLGGSGNAEKLLE---EVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTA 164
Cdd:PRK11308 111 VGqileeplliNTSLSAAERREKALAmmaKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190
....*....|....*....|....*....|....
gi 489527143 165 DEIIALLKKTAHELGKCVVVVTHS----KHLAEE 194
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDlsvvEHIADE 224
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-210 |
2.85e-23 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 96.58 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKtiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL-F 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLttvenvkLGGSGNA------EKLLEEVGIGK----EYWQRNVLQLSGGQQQRVAIARALASDAHVLL 151
Cdd:PRK10522 400 SAVFTDFHLFDQL-------LGPEGKPanpalvEKWLERLKMAHklelEDGRISNLKLSKGQKKRLALLLALAEERDILL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 152 adeptgnLDETTAD-----------EIIALLKktahELGKCVVVVTHSKHLAEEADEILEIKNGAISFLS 210
Cdd:PRK10522 473 -------LDEWAADqdphfrrefyqVLLPLLQ----EMGKTIFAISHDDHYFIHADRLLEMRNGQLSELT 531
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-187 |
3.41e-23 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.17 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYaykTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRkhn 80
Cdd:PRK13538 1 MLEARNLAC---ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 iSLVF---QNyNLIDYLTTVENV----KLGGSGNAEKL---LEEVGI-GKEywqrNVL--QLSGGQQQRVAIARALASDA 147
Cdd:PRK13538 75 -DLLYlghQP-GIKTELTALENLrfyqRLHGPGDDEALweaLAQVGLaGFE----DVPvrQLSAGQQRRVALARLWLTRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKktAH-ELGKCVVVVTH 187
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLA--QHaEQGGMVILTTH 187
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-206 |
3.64e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 93.93 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhNI 81
Cdd:PRK13635 6 IRVEHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR-QV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVEN-VKLGGSGNA----------EKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:PRK13635 84 GMVFQNPDNQFVGATVQDdVAFGLENIGvpreemvervDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 151 LADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
3.85e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 3.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAyktKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkgLNYHRKHN 80
Cdd:PRK13539 2 MLEGEDLACV---RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID---DPDVAEAC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYnLIDYLTTVENVKL------GGSGNAEKLLEEVGIGkeywqrNVLQ-----LSGGQQQRVAIARALASDAHV 149
Cdd:PRK13539 76 HYLGHRNA-MKPALTVAENLEFwaaflgGEELDIAAALEAVGLA------PLAHlpfgyLSAGQKRRVALARLLVSNRPI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527143 150 LLADEPTGNLDeTTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEI 198
Cdd:PRK13539 149 WILDEPTAALD-AAAVALFAELIRAHLAQGGIVIAATHIPLGLPGAREL 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-206 |
6.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 93.13 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKH 79
Cdd:PRK13644 1 MIRLENVSYSYP---DGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVKLGGSGN-----------AEKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAH 148
Cdd:PRK13644 78 LVGIVFQNPETQFVGRTVEEDLAFGPENlclppieirkrVDRALAEIGLEK-YRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTaHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
8.41e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 92.51 E-value: 8.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHn 80
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVE-NVKLGGSGNA----------EKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHV 149
Cdd:PRK13648 85 IGIVFQNPDNQFVGSIVKyDVAFGLENHAvpydemhrrvSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 150 LLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTV 220
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-207 |
8.88e-23 |
|
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: 95.11 E-value: 8.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:TIGR01842 317 LSVENVTIVPPGGK-KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH-I 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYlTTVENV-KLGGSGNAEKLLE--------------------EVGIGKEywqrnvlQLSGGQQQRVAIA 140
Cdd:TIGR01842 395 GYLPQDVELFPG-TVAENIaRFGENADPEKIIEaaklagvhelilrlpdgydtVIGPGGA-------TLSGGQRQRIALA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 141 RALASDAHVLLADEPTGNLDE----TTADEIIALLKKtahelGKCVVVVTHSKHLAEEADEILEIKNGAIS 207
Cdd:TIGR01842 467 RALYGDPKLVVLDEPNSNLDEegeqALANAIKALKAR-----GITVVVITHRPSLLGCVDKILVLQDGRIA 532
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-206 |
1.24e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT--KKGLNYHRK 78
Cdd:PRK13639 1 ILETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 hNISLVFQNYNLIDYLTTVE--------NVKLGGSGNAEKL---LEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:PRK13639 79 -TVGIVFQNPDDQLFAPTVEedvafgplNLGLSKEEVEKRVkeaLKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVyADKVYVMSDGKI 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-206 |
1.36e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.87 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDT--AVKGTVLCN--------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 65 --------GEDITK---------KGLNYHRKHNISLVFQ-NYNLIDYLTTVENV-----KLGGSGN-----AEKLLEEVG 116
Cdd:TIGR03269 78 vgepcpvcGGTLEPeevdfwnlsDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVlealeEIGYEGKeavgrAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 117 IGKE--YWQRNvlqLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE 194
Cdd:TIGR03269 158 LSHRitHIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIED 234
|
250
....*....|...
gi 489527143 195 -ADEILEIKNGAI 206
Cdd:TIGR03269 235 lSDKAIWLENGEI 247
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-205 |
2.75e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYaykTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI---TKKGLNYHR 77
Cdd:PRK11831 7 LVDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLYTVR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KhNISLVFQNYNLIDYLTTVENVklggsgnAEKLLEEVGIGKEYWQRNVL-----------------QLSGGQQQRVAIA 140
Cdd:PRK11831 84 K-RMSMLFQSGALFTDMNVFDNV-------AYPLREHTQLPAPLLHSTVMmkleavglrgaaklmpsELSGGMARRAALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHskhlaeEADEILEIKNGA 205
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSH------DVPEVLSIADHA 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-206 |
2.86e-22 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 94.04 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-I 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYlTTVENVKLGGSGNA--EKLLEEV--------------GIGKEYWQRNVlQLSGGQQQRVAIARALAS 145
Cdd:TIGR01193 551 NYLPQEPYIFSG-SILENLLLGAKENVsqDEIWAACeiaeikddienmplGYQTELSEEGS-SISGGQKQRIALARALLT 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 146 DAHVLLADEPTGNLDETTADEIIALLKKTAHelgKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-206 |
3.37e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.87 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKTKKdkTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRkHNIS 82
Cdd:PRK13657 336 EFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLR-RNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQNYNLIDYlTTVENVKLG--GSGNAEKLLE-EVGIGKEYWQRNVL-----------QLSGGQQQRVAIARALASDAH 148
Cdd:PRK13657 413 VVFQDAGLFNR-SIEDNIRVGrpDATDEEMRAAaERAQAHDFIERKPDgydtvvgergrQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-206 |
4.04e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 90.92 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLnYHRKHN 80
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENV-WNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGSGNA----EKLLEEVGIGK------EYWQRNVLQLSGGQQQRVAIARALASDAHVL 150
Cdd:PRK13642 83 IGMVFQNPDNQFVGATVEDDVAFGMENQgiprEEMIKRVDEALlavnmlDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 151 LADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-206 |
5.13e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 93.21 E-value: 5.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAY--------KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTL-LSLLAGLDTAvkGTVLCNGEDITK-- 70
Cdd:COG4172 276 LEARDLKVWFpikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLIPSE--GEIRFDGQDLDGls 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 71 -KGLNYHRKHnISLVFQN-YNLIDYLTTVENV--------KLGGSGN-----AEKLLEEVGIGKEYWQRNVLQLSGGQQQ 135
Cdd:COG4172 354 rRALRPLRRR-MQVVFQDpFGSLSPRMTVGQIiaeglrvhGPGLSAAerrarVAEALEEVGLDPAARHRYPHEFSGGQRQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489527143 136 RVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKV 504
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-155 |
5.22e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 89.70 E-value: 5.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKTKKDKTILNNVSATFEEGifyTIV---GPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT-------- 69
Cdd:COG1137 3 TLEAENLV---KSYGKRTVVKDVSLEVNQG---EIVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIThlpmhkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 70 KKGLNYhrkhnisL-----VFQNynlidyLTTVENV-------KLGGSGNAEK---LLEEVGIGKeywQRNVL--QLSGG 132
Cdd:COG1137 77 RLGIGY-------LpqeasIFRK------LTVEDNIlavlelrKLSKKEREERleeLLEEFGITH---LRKSKaySLSGG 140
|
170 180
....*....|....*....|...
gi 489527143 133 QQQRVAIARALASDAHVLLADEP 155
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEP 163
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-206 |
2.83e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.70 E-value: 2.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL---DTAVKGTVLCNGEDITKKGLnYHRK 78
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTV-WDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNY-NLIDYLTTVENVKLGGSGNA----------EKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDA 147
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGATVGDDVAFGLENRAvprpemikivRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 148 HVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
17-187 |
2.84e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 87.32 E-value: 2.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 17 KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAG--LDTAVKGTVLCNGEDITkkglnyhrkhnislvfQNYNLIDYL 94
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG----------------REASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 95 TTVENVKLggsgnAEKLLEEVGIGKEY-WQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKK 173
Cdd:COG2401 107 GRKGDFKD-----AVELLNAVGLSDAVlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170
....*....|....
gi 489527143 174 TAHELGKCVVVVTH 187
Cdd:COG2401 182 LARRAGITLVVATH 195
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-160 |
3.47e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.02 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKG---LNYHRKHnISLVFQN-YNLIDYLT 95
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRR-MQMVFQDpYASLNPRM 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 96 TVENV--------KLGGSGN----AEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLD 160
Cdd:COG4608 113 TVGDIiaeplrihGLASKAErrerVAELLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-204 |
4.90e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 4.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAykTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeditkkglnyHRKHN 80
Cdd:COG4178 362 ALALEDLTLR--TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI--------------ARPAG 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVF---QNY----NLIDYLT---TVENVklggsGNAE--KLLEEVGIGK--------EYWQRnvlQLSGGQQQRVAIA 140
Cdd:COG4178 426 ARVLFlpqRPYlplgTLREALLypaTAEAF-----SDAElrEALEAVGLGHlaerldeeADWDQ---VLSLGEQQRLAFA 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIIALLKktaHELGKC-VVVVTHSKHLAEEADEILEIKNG 204
Cdd:COG4178 498 RLLLHKPDWLFLDEATSALDEENEAALYQLLR---EELPGTtVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-187 |
1.02e-20 |
|
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: 85.62 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAyktKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRkhNI 81
Cdd:cd03231 1 LEADELTCE---RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR--GL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVK----LGGSGNAEKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTG 157
Cdd:cd03231 76 LYLGHAPGIKTTLSVLENLRfwhaDHSDEQVEEALARVGLNG-FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190
....*....|....*....|....*....|.
gi 489527143 158 NLDETTADEIIALLKktAH-ELGKCVVVVTH 187
Cdd:cd03231 155 ALDKAGVARFAEAMA--GHcARGGMVVLTTH 183
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-187 |
1.72e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.71 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTI--LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCN-GE---DITKKG-L 73
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDewvDMTKPGpD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 74 NYHR-KHNISLVFQNYNLIDYLTTVENVKLG---------GSGNAEKLLEEVGIGKEYwQRNVL-----QLSGGQQQRVA 138
Cdd:TIGR03269 359 GRGRaKRYIGILHQEYDLYPHRTVLDNLTEAiglelpdelARMKAVITLKMVGFDEEK-AEEILdkypdELSEGERHRVA 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527143 139 IARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSH 486
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-205 |
2.21e-20 |
|
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: 85.18 E-value: 2.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKT-----KKDKTI--LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTV----------LC 63
Cdd:COG4778 4 LLEVENLS---KTftlhlQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdggwvdLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 64 NGEDITKKGLnyhRKHNISLVFQNYNLIDYLTTVENV-----KLGGS-----GNAEKLLEEVGIGKEYWQRNVLQLSGGQ 133
Cdd:COG4778 81 QASPREILAL---RRRTIGYVSQFLRVIPRVSALDVVaepllERGVDreearARARELLARLNLPERLWDLPPATFSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 134 QQRVAIARALASDAHVLLADEPTGNLDETTADEIIALL--KKTAhelGKCVVVVTHSKHLAEE-ADEILEIKNGA 205
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIeeAKAR---GTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-173 |
2.94e-20 |
|
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: 84.90 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK--------KGL 73
Cdd:cd03218 1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpmhkrarLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 74 NY-------HRK----HNISLVFQnynlIDYLTTVENVKLggsgnAEKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARA 142
Cdd:cd03218 78 GYlpqeasiFRKltveENILAVLE----IRGLSKKEREEK-----LEELLEEFHITH-LRKSKASSLSGGERRRVEIARA 147
|
170 180 190
....*....|....*....|....*....|.
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLKK 173
Cdd:cd03218 148 LATNPKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-187 |
3.56e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.67 E-value: 3.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGE--DITKKGLNYHR 77
Cdd:PRK13636 5 ILKVEELNYNYS---DGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KhNISLVFQNYNLIDYLTTV-ENVKLGGSG----------NAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASD 146
Cdd:PRK13636 82 E-SVGMVFQDPDNQLFSASVyQDVSFGAVNlklpedevrkRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATH 200
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-206 |
4.40e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 87.57 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI---TKKGLnyhRK 78
Cdd:COG5265 358 VRFENVSFGYDP--ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdvTQASL---RA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HnISLVFQN---------YNlIDYlttvenvklggsGNAEKLLEEV-------GIG------KEYWQRNV----LQLSGG 132
Cdd:COG5265 433 A-IGIVPQDtvlfndtiaYN-IAY------------GRPDASEEEVeaaaraaQIHdfieslPDGYDTRVgergLKLSGG 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 133 QQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:COG5265 499 EKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-206 |
6.62e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 83.35 E-value: 6.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLD--TAVKGTVLCNGEDITKKGLNYHRKH 79
Cdd:cd03217 1 LEIKDLHVSVG---GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQnynlidYLTTVENVKLggsgnaEKLLEEVGIGkeywqrnvlqLSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:cd03217 78 GIFLAFQ------YPPEIPGVKN------ADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527143 160 DeTTADEIIALLKKTAHELGKCVVVVTHSKHLAE--EADEILEIKNGAI 206
Cdd:cd03217 136 D-IDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRVHVLYDGRI 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-173 |
8.13e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 86.68 E-value: 8.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKK--------DKTILNNVSATFEEGIFYTIVGPSGAGKTT----LLSLLAGldtavKGTVLCNGEDI 68
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 69 TkkglNYHRK------HNISLVFQNYN-----------LIDYLTTVENVKLGGSGNAEKL---LEEVGIGKEYWQRNVLQ 128
Cdd:PRK15134 350 H----NLNRRqllpvrHRIQVVFQDPNsslnprlnvlqIIEEGLRVHQPTLSAAQREQQViavMEEVGLDPETRHRYPAE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 129 LSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKK 173
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS 470
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-187 |
8.91e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.55 E-value: 8.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKK-DKTILNNVSATFEEGIFYTIVGPSGAGKT----TLLSLLAGlDTAVKGTVLCNGEDI---TKKG 72
Cdd:PRK09473 12 LLDVKDLRVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREIlnlPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 73 LNYHRKHNISLVFQnynliDYLTTVENVKLGGSGNAEKLLEEVGIGK-EYWQRNVLQL-------------------SGG 132
Cdd:PRK09473 91 LNKLRAEQISMIFQ-----DPMTSLNPYMRVGEQLMEVLMLHKGMSKaEAFEESVRMLdavkmpearkrmkmyphefSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 133 QQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITH 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-206 |
9.36e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.24 E-value: 9.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK---KGLNYHRKHNISLVFQNYNLIDYLTT 96
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 97 VEN----VKLGGSGNAEK------LLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADE 166
Cdd:PRK10070 124 LDNtafgMELAGINAEERrekaldALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527143 167 IIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEV 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-207 |
1.09e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.38 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVsyaykTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT--------KKG 72
Cdd:PRK09700 265 VFEVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 73 LNY---HRKHNisLVFQNYNLIDYLTTVENVKLGGSGN-------------AEKLLEEVGIGKEYWQRNVLQLSGGQQQR 136
Cdd:PRK09700 340 MAYiteSRRDN--GFFPNFSIAQNMAISRSLKDGGYKGamglfhevdeqrtAENQRELLALKCHSVNQNITELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 137 VAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVthSKHLAE---EADEILEIKNGAIS 207
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMV--SSELPEiitVCDRIAVFCEGRLT 488
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-204 |
1.56e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 1.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAY-KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKT-TLLSLLAGLDTA----VKGTVLCNGEDI------ 68
Cdd:PRK15134 5 LLAIENLSVAFrQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhaseq 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 69 TKKGLnyhRKHNISLVFQN--------YNLIDYLTTVENVKLGGSGNAEK-----LLEEVGIgkeywqRNVL-------- 127
Cdd:PRK15134 85 TLRGV---RGNKIAMIFQEpmvslnplHTLEKQLYEVLSLHRGMRREAARgeilnCLDRVGI------RQAAkrltdyph 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 128 QLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-204 |
1.83e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.35 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLdTAVKGTVLCNGEDITKKGLN-------YHRKHNISL----VFQny 88
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPfampVFQ-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 89 nlidYLTtvenvkLGGSGNA---------EKLLEEVGIGKEYwQRNVLQLSGGQQQRVAIARALA-------SDAHVLLA 152
Cdd:COG4138 89 ----YLA------LHQPAGAsseaveqllAQLAEALGLEDKL-SRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 153 DEPTGNLD---ETTADEIIALLkktaHELGKCVVVVTHS-KHLAEEADEILEIKNG 204
Cdd:COG4138 158 DEPMNSLDvaqQAALDRLLREL----CQQGITVVMSSHDlNHTLRHADRVWLLKQG 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-206 |
2.09e-19 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.21 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 16 DKTILNNVSATFEEGIFYTIVGPSGAGKTtlLSLLAGLD------TAVKGTVLCNGEDITKKGLnyhRKHNISLVFQN-- 87
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVAPCAL---RGRKIATIMQNpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 88 --YNLIDYLTT--VENVK-LGGSGNAEKL---LEEVGIG--KEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTG 157
Cdd:PRK10418 90 saFNPLHTMHThaRETCLaLGKPADDATLtaaLEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489527143 158 NLDETTADEIIALLKKTAHELGKCVVVVTHSKH-LAEEADEILEIKNGAI 206
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGvVARLADDVAVMSHGRI 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-206 |
2.54e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.52 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGE--DITKKGLNYHRK 78
Cdd:PRK13638 1 MLATSDLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HnISLVFQN------YNLID--YLTTVENVKLGGSGNAEKLLEEVGI--GKEYWQRNVLQLSGGQQQRVAIARALASDAH 148
Cdd:PRK13638 78 Q-VATVFQDpeqqifYTDIDsdIAFSLRNLGVPEAEITRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEE-ADEILEIKNGAI 206
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEiSDAVYVLRQGQI 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-195 |
2.87e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.22 E-value: 2.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 17 KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKG-----TVLCNGEDI--TKKGLNYHRKhnISLVFQNYN 89
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnYRDVLEFRRR--VGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 90 LIDyLTTVENVKLG-----------GSGNAEKLLEEVGIG---KEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEP 155
Cdd:PRK14271 112 PFP-MSIMDNVLAGvrahklvprkeFRGVAQARLTEVGLWdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527143 156 TGNLDETTADEIIALLKKTAHELgkCVVVVTHSkhLAEEA 195
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRL--TVIIVTHN--LAQAA 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-205 |
2.95e-19 |
|
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: 80.66 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAykTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeditkkglNYHRKHNI 81
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------------GMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNynliDYLTTvenvklgGSgnaeklLEEVGIgkeY-WQRNvlqLSGGQQQRVAIARALASDAHVLLADEPTGNLD 160
Cdd:cd03223 67 LFLPQR----PYLPL-------GT------LREQLI---YpWDDV---LSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 161 ETTADEIIALLKktahELGKCVVVVTHSKHLAEEADEILEIKNGA 205
Cdd:cd03223 124 EESEDRLYQLLK----ELGITVISVGHRPSLWKFHDRVLDLDGEG 164
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-188 |
4.17e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.58 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL-----DTAVKGTVLCNGEDITKKGLNYH 76
Cdd:PRK14267 5 IETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 R-KHNISLVFQNYNLIDYLTTVENV----KLGGSGNAEKLLEEV---GIGKE-YWQ--RNVL-----QLSGGQQQRVAIA 140
Cdd:PRK14267 82 EvRREVGMVFQYPNPFPHLTIYDNVaigvKLNGLVKSKKELDERvewALKKAaLWDevKDRLndypsNLSGGQRQRLVIA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELgkCVVVVTHS 188
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHS 207
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-208 |
5.26e-19 |
|
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: 81.15 E-value: 5.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 5 KNVSYAYKTKKDK-TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL---DTAVKGTVLCNGEDItKKGLNYHRkHN 80
Cdd:cd03233 7 RNISFTTGKGRSKiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPY-KEFAEKYP-GE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGS--GNAeklleevgigkeywqrNVLQLSGGQQQRVAIARALASDAHVLLADEPTGN 158
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRckGNE----------------FVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527143 159 LDETTADEIIALLKKTAHELGKCVVVVTH--SKHLAEEADEILEIKNGAISF 208
Cdd:cd03233 149 LDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGRQIY 200
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-206 |
6.57e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 83.99 E-value: 6.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 16 DKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnISLVFQNYNLIDYlT 95
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 96 TVENVKLGGSGNAEKLLEEV---------------GIGKEYWQRNVLqLSGGQQQRVAIARALASDAHVLLADEPTGNLD 160
Cdd:PRK10789 405 VANNIALGRPDATQQEIEHVarlasvhddilrlpqGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489527143 161 ETTADEIIALLKKTAHelGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK10789 484 GRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHI 527
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-204 |
6.75e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.55 E-value: 6.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlnYHRKHNI 81
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA--RHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLGG------SGNAEKL---LEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLA 152
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGryfglsAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489527143 153 DEPTGNLDeTTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:PRK13537 163 DEPTTGLD-PQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEG 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
35-199 |
7.64e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.00 E-value: 7.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGE---DITKK-GLNYHrKHNISLVFQNYNLIDYLTTVENVKLG--GSGNA 108
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKGiCLPPE-KRRIGYVFQDARLFPHYKVRGNLRYGmaKSMVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 109 E--KLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVT 186
Cdd:PRK11144 108 QfdKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVS 186
|
170
....*....|...
gi 489527143 187 HSkhlaeeADEIL 199
Cdd:PRK11144 187 HS------LDEIL 193
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-206 |
8.77e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.08 E-value: 8.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHN 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQ---ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGSgNAEKLLEEVGIGKEY------WQRNVLQ---LSGGQQQRVAIARALASDAHVLL 151
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMGGF-FAERDQFQERIKWVYelfprlHERRIQRagtMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-171 |
2.22e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.67 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL--DTAVKGTVLCNGEDITKKGLNYHRK 78
Cdd:PRK13549 5 LLEMKNIT---KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLIDYLTTVENVKLG------GSGN-------AEKLLEEVGIGKEYWQRnVLQLSGGQQQRVAIARALAS 145
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGneitpgGIMDydamylrAQKLLAQLKLDINPATP-VGNLGLGQQQLVEIAKALNK 160
|
170 180
....*....|....*....|....*.
gi 489527143 146 DAHVLLADEPTGNLdetTADEIIALL 171
Cdd:PRK13549 161 QARLLILDEPTASL---TESETAVLL 183
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-208 |
2.55e-18 |
|
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: 80.07 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 14 KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYhrKHNISLVF-------- 85
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF--LRRIGVVFgqktqlww 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 86 -----QNYNLIDYLTTVENVKLGgsGNAEKLLEEVGIGKEYWQrNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLD 160
Cdd:cd03267 109 dlpviDSFYLLAAIYDLPPARFK--KRLDELSELLDLEELLDT-PVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489527143 161 ETTADEIIALLKKTAHELGKCVVVVTHSKH-LAEEADEILEIKNGAISF 208
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKdIEALARRVLVIDKGRLLY 234
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-206 |
3.26e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.42 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 17 KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkglnYHRKH---NISLVFQNYNLIDY 93
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQH----YASKEvarRIGLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 94 LTTVENVKLG--------------GSGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:PRK10253 96 ITVQELVARGryphqplftrwrkeDEEAVTKAMQATGI-THLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527143 160 DETTADEIIALLKKTAHELGKCVVVVTHSKHLA-EEADEILEIKNGAI 206
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKI 222
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
12-210 |
3.67e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 82.23 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 12 KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL--DTAVKGTVLCNGEDITKKGLNyhrkhNISLVFQNYN 89
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQILK-----RTGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 90 LIDYLTTVEN------VKLGGSGN-------AEKLLEEVG--------IGKEYwqrnVLQLSGGQQQRVAIARALASDAH 148
Cdd:PLN03211 151 LYPHLTVRETlvfcslLRLPKSLTkqekilvAESVISELGltkcentiIGNSF----IRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTH--SKHLAEEADEILEIKNGAISFLS 210
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHqpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-201 |
4.54e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 4.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHNI 81
Cdd:COG3845 258 LEVENLSV--RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLV---FQNYNLIDYLTTVENVKLGGSG-----------------NAEKLLEEVGI-GKEYWQRnVLQLSGGQQQRVAIA 140
Cdd:COG3845 336 AYIpedRLGRGLVPDMSVAENLILGRYRrppfsrggfldrkairaFAEELIEEFDVrTPGPDTP-ARSLSGGNQQKVILA 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVThskhlaEEADEILEI 201
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLIS------EDLDEILAL 468
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-204 |
4.56e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.79 E-value: 4.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL--DTAVKGTVLCNGEDITKKGLNYHRK 78
Cdd:TIGR02633 1 LLEMKGIV---KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLIDYLTTVENVKLGGS--------------GNAEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALA 144
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEitlpggrmaynamyLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 145 SDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNG 204
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-196 |
4.82e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.98 E-value: 4.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI------TKKGLNYHRKHNIslvfqnynLIDY 93
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldaVRQSLGMCPQHNI--------LFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 94 LTTVENV----KLGGSG------NAEKLLEEVGIgkeYWQRN--VLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDE 161
Cdd:TIGR01257 1018 LTVAEHIlfyaQLKGRSweeaqlEMEAMLEDTGL---HHKRNeeAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190
....*....|....*....|....*....|....*
gi 489527143 162 TTADEIIALLKKtaHELGKCVVVVTHskHLaEEAD 196
Cdd:TIGR01257 1095 YSRRSIWDLLLK--YRSGRTIIMSTH--HM-DEAD 1124
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-192 |
6.76e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 4 VKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK-KGLNYHRKhnIS 82
Cdd:PRK10575 14 LRNVSFRVP---GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARK--VA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQNYNLIDYLTTVENVKLG-----------GSGNAEKLLEE---VGIgKEYWQRNVLQLSGGQQQRVAIARALASDAH 148
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGrypwhgalgrfGAADREKVEEAislVGL-KPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLA 192
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMA 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-204 |
8.42e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 8.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKT-TLLSLLAGLDTAvKGTVLCNG------------- 65
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQA-GGLVQCDKmllrrrsrqviel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 66 EDITKKGLNYHRKHNISLVFQN-YNLIDYLTTV-----ENVKL--GGSGN-----AEKLLEEVGI--GKEYWQRNVLQLS 130
Cdd:PRK10261 91 SEQSAAQMRHVRGADMAMIFQEpMTSLNPVFTVgeqiaESIRLhqGASREeamveAKRMLDQVRIpeAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 131 GGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKH-LAEEADEILEIKNG 204
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQG 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-205 |
1.26e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHNISLVFQNYNLIDYLTTVEN 99
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 100 VKLGG-----------------SGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDET 162
Cdd:PRK09700 101 LYIGRhltkkvcgvniidwremRVRAAMMLLRVGL-KVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 163 TADEIIALLKKTAHElGKCVVVVTHS-KHLAEEADEILEIKNGA 205
Cdd:PRK09700 180 EVDYLFLIMNQLRKE-GTAIVYISHKlAEIRRICDRYTVMKDGS 222
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-187 |
1.73e-17 |
|
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: 79.98 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCnGEDItkkglnyhrkhNI 81
Cdd:TIGR03719 323 IEAENLTKAFG---DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV-----------KL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLGGsgnaeklLEEVGIGK------EY----------WQRNVLQLSGGQQQRVAIARALAS 145
Cdd:TIGR03719 388 AYVDQSRDALDPNKTVWEEISGG-------LDIIKLGKreipsrAYvgrfnfkgsdQQKKVGQLSGGERNRVHLAKTLKS 460
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489527143 146 DAHVLLADEPTGNLD-ETTADEIIALLkktahELGKCVVVVTH 187
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDvETLRALEEALL-----NFAGCAVVISH 498
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-201 |
1.85e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSyayktkkDKTILNNVSatFE----E--GIFytivGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT----- 69
Cdd:COG1129 256 VLEVEGLS-------VGGVVRDVS--FSvragEilGIA----GLVGAGRTELARALFGADPADSGEIRLDGKPVRirspr 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 70 ---KKGLNY---HRKH-----------NISLVFQNynlidylttvenvKLGGSG---------NAEKLLEEVGIGKEYWQ 123
Cdd:COG1129 323 daiRAGIAYvpeDRKGeglvldlsireNITLASLD-------------RLSRGGlldrrreraLAEEYIKRLRIKTPSPE 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 124 RNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVThSkhlaeEADEILEI 201
Cdd:COG1129 390 QPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVIS-S-----ELPELLGL 460
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-204 |
3.02e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 21 NNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkGLNYHRKHNISLV--FQNYNLIDYLTTVE 98
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGHQIARMGVVrtFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 99 N--------VKLG-----------------GSGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLAD 153
Cdd:PRK11300 100 NllvaqhqqLKTGlfsgllktpafrraeseALDRAATWLERVGL-LEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489527143 154 EPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEE-ADEILEIKNG 204
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQG 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-211 |
3.37e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI----TKKGLNyhrkHNISLVFQNYNLIDYLT 95
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALA----AGVAIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 96 TVENVKLG------GSGNAEKLLEEVG-----IGKEY-WQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLdetT 163
Cdd:PRK11288 96 VAENLYLGqlphkgGIVNRRLLNYEAReqlehLGVDIdPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL---S 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489527143 164 ADEiIALLKKTAHEL---GKCVVVVTHskhlaeEADEILEIKNgAISFLSD 211
Cdd:PRK11288 173 ARE-IEQLFRVIRELraeGRVILYVSH------RMEEIFALCD-AITVFKD 215
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-196 |
4.95e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 75.76 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhn 80
Cdd:PRK13540 1 MLDVIELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQ-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENV--KLGGSGNAEKLLEEVGIGK--EYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPT 156
Cdd:PRK13540 76 LCFVGHRSGINPYLTLRENClyDIHFSPGAVGITELCRLFSleHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527143 157 GNLDETTADEIIAllKKTAHEL-GKCVVVVTHSKHLAEEAD 196
Cdd:PRK13540 156 VALDELSLLTIIT--KIQEHRAkGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
35-201 |
7.42e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.12 E-value: 7.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHNISLVFQNYNLIDYLTTVENVKLG-------GSGN 107
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGrefvnrfGRID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 108 -------AEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETtadEIIALLkKTAHEL-- 178
Cdd:PRK10762 115 wkkmyaeADKLLARLNL-RFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT---ETESLF-RVIRELks 189
|
170 180
....*....|....*....|....
gi 489527143 179 -GKCVVVVTHskhlaeEADEILEI 201
Cdd:PRK10762 190 qGRGIVYISH------RLKEIFEI 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-204 |
1.80e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.90 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 5 KNVSYAYKTKKdkTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVkgtvlcNGEDITKKGLNyhrkhnISLV 84
Cdd:TIGR03719 8 NRVSKVVPPKK--EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDF------NGEARPQPGIK------VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 85 FQNYNLIDYLTTVENVKLG------------------GSGNAE--KLLEEVGIGKEY----------------------- 121
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGvaeikdaldrfneisakyAEPDADfdKLAAEQAELQEIidaadawdldsqleiamdalrcp 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 122 -WQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDEttadEIIALLKKTAHELGKCVVVVTHSKH-LAEEADEIL 199
Cdd:TIGR03719 154 pWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHDRYfLDNVAGWIL 229
|
....*
gi 489527143 200 EIKNG 204
Cdd:TIGR03719 230 ELDRG 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-204 |
1.85e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 23 VSATFEEGIFYTIVGPSGAGKTTLLSLLAGLdTAVKGTVLCNG---EDITKKGLNYHR----KHNISL----VFQnynli 91
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGqplEAWSAAELARHRaylsQQQTPPfampVFQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 92 dYLTTVENVKlGGSGNAEKLLEEV----GIGKEYwQRNVLQLSGGQQQRVAIA-------RALASDAHVLLADEPTGNLD 160
Cdd:PRK03695 89 -YLTLHQPDK-TRTEAVASALNEVaealGLDDKL-GRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 161 ETTADEIIALLKKTAhELGKCVVVVTHS-KHLAEEADEILEIKNG 204
Cdd:PRK03695 166 VAQQAALDRLLSELC-QQGIAVVMSSHDlNHTLRHADRVWLLKQG 209
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-206 |
2.02e-16 |
|
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: 74.45 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDkTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:cd03244 3 IEFKNVSLRYRPNLP-PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDylTTV-ENVKLGGSGNAEKL---LEEVGIgKEYWQ-----------RNVLQLSGGQQQRVAIARALASD 146
Cdd:cd03244 81 SIIPQDPVLFS--GTIrSNLDPFGEYSDEELwqaLERVGL-KEFVEslpggldtvveEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKktaHELGKC-VVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIR---EAFKDCtVLTIAHRLDTIIDSDRILVLDKGRV 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-193 |
3.93e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.05 E-value: 3.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 22 NVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDI---TKKGLNYHRKhNISLVFQN-YNLIDYLTTV 97
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRR-DIQFIFQDpYASLDPRQTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 98 -----ENVKLGGSGNAEK-------LLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTAD 165
Cdd:PRK10261 421 gdsimEPLRVHGLLPGKAaaarvawLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
|
170 180
....*....|....*....|....*...
gi 489527143 166 EIIALLKKTAHELGKCVVVVTHSKHLAE 193
Cdd:PRK10261 501 QIINLLLDLQRDFGIAYLFISHDMAVVE 528
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-167 |
6.00e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 73.77 E-value: 6.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDIT--------KKGL 73
Cdd:PRK10895 4 LTAKNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplharaRRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 74 NYHRKHniSLVFQNYNLIDYLTTVENVKLGGSGN-----AEKLLEEVGIgkEYWQRNVLQ-LSGGQQQRVAIARALASDA 147
Cdd:PRK10895 81 GYLPQE--ASIFRRLSVYDNLMAVLQIRDDLSAEqredrANELMEEFHI--EHLRDSMGQsLSGGERRRVEIARALAANP 156
|
170 180
....*....|....*....|
gi 489527143 148 HVLLADEPTGNLDETTADEI 167
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDI 176
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-211 |
6.30e-16 |
|
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: 73.71 E-value: 6.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDktiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGL------N 74
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKG---CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELyqlseaE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 75 YHRKHNISLVFQNYNLIDYLTTveNVKLGGS-------------GN----AEKLLEEVGIGKEYWQRNVLQLSGGQQQRV 137
Cdd:TIGR02323 80 RRRLMRTEWGFVHQNPRDGLRM--RVSAGANigerlmaigarhyGNiratAQDWLEEVEIDPTRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 138 AIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAE-EADEILEIKNGAI--SFLSD 211
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVMQQGRVveSGLTD 234
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
20-206 |
7.41e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.39 E-value: 7.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKT-TLLSLLAGLDtaVKGTVLC-----NGEDITKKGLNYHRK---HNISLVFQN--- 87
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLID--YPGRVMAeklefNGQDLQRISEKERRNlvgAEVAMIFQDpmt 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 88 ---------YNLIDYLttveNVKLGGSGNAEK-----LLEEVGIGKEYWQRNVL--QLSGGQQQRVAIARALASDAHVLL 151
Cdd:PRK11022 101 slnpcytvgFQIMEAI----KVHQGGNKKTRRqraidLLNQVGIPDPASRLDVYphQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 152 ADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHL-AEEADEILEIKNGAI 206
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQV 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-198 |
8.32e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.48 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhnI 81
Cdd:PRK13536 42 IDLAGVSKSYG---DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR--I 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTVENVKLGGS--GNAEKLLEEVGIGKEYWQR-------NVLQLSGGQQQRVAIARALASDAHVLLA 152
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRyfGMSTREIEAVIPSLLEFARleskadaRVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489527143 153 DEPTGNLDeTTADEII-----ALLKKtahelGKCVVVVThskHLAEEADEI 198
Cdd:PRK13536 197 DEPTTGLD-PHARHLIwerlrSLLAR-----GKTILLTT---HFMEEAERL 238
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-204 |
8.42e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.53 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 5 KNVSYAYKTKKDK-TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAG-LDTAV--KGTVLCNGEDITK---KGLNYHR 77
Cdd:TIGR00956 763 RNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErVTTGVitGGDRLVNGRPLDSsfqRSIGYVQ 842
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHNI---------SLVFQNY----------NLIDYLTTVENVkLGGSGNAEKLLEEVGIGkeywqrnvlqLSGGQQQRVA 138
Cdd:TIGR00956 843 QQDLhlptstvreSLRFSAYlrqpksvsksEKMEYVEEVIKL-LEMESYADAVVGVPGEG----------LNVEQRKRLT 911
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 139 IARALASDAHVLL-ADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTH--SKHLAEEADEILEIKNG 204
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIHqpSAILFEEFDRLLLLQKG 979
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
36-187 |
8.75e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 73.66 E-value: 8.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 36 VGPSGAGKTTLLSLLAGLDT-----AVKGTVLCNGEDITKKGLN-YHRKHNISLVFQNYNLIDYlTTVENVKLGG----- 104
Cdd:PRK14243 42 IGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpVEVRRRIGMVFQKPNPFPK-SIYDNIAYGAringy 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 105 SGNAEKLLE----------EVgigKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLkkt 174
Cdd:PRK14243 121 KGDMDELVErslrqaalwdEV---KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELM--- 194
|
170
....*....|....*
gi 489527143 175 aHELGK--CVVVVTH 187
Cdd:PRK14243 195 -HELKEqyTIIIVTH 208
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-199 |
2.10e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 72.45 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGeditkkglnyhrKHN 80
Cdd:PRK09544 4 LVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG------------KLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLT-TVENVKL--GGSGNAEKL--LEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEP 155
Cdd:PRK09544 69 IGYVPQKLYLDTTLPlTVNRFLRlrPGTKKEDILpaLKRVQAGH-LIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 156 TGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLA-EEADEIL 199
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVL 192
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-193 |
2.20e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT----------ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK 70
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKQwfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 71 KGLNYHR--KHNISLVFQnynliDYLTTVENVKLGGSGNAEKL-------------------LEEVGIGKEYWQRNVLQL 129
Cdd:PRK15079 88 MKDDEWRavRSDIQMIFQ-----DPLASLNPRMTIGEIIAEPLrtyhpklsrqevkdrvkamMLKVGLLPNLINRYPHEF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 130 SGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS----KHLAE 193
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDlavvKHISD 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-208 |
2.31e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.04 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKT-------------------KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTV 61
Cdd:COG1134 4 MIEVENVSKSYRLyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 62 LCNGEditkkglnyhrkhnISlvfqnyNLIDY-------LTTVENVKLGGS------GNAEKLLEEV----GIGkEYWQR 124
Cdd:COG1134 84 EVNGR--------------VS------ALLELgagfhpeLTGRENIYLNGRllglsrKEIDEKFDEIvefaELG-DFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 125 NVLQLSGGQQQRVAIARALASDAHVLLadeptgnLDETTA-----------DEIIALLKKtahelGKCVVVVTHSKHLAE 193
Cdd:COG1134 143 PVKTYSSGMRARLAFAVATAVDPDILL-------VDEVLAvgdaafqkkclARIRELRES-----GRTVIFVSHSMGAVR 210
|
250
....*....|....*.
gi 489527143 194 E-ADEILEIKNGAISF 208
Cdd:COG1134 211 RlCDRAIWLEKGRLVM 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-206 |
2.63e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.13 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVS--YAYKT----KKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLN 74
Cdd:PRK15112 4 LLEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 75 YhRKHNISLVFQNYN-----------LIDYLTTVeNVKLGGSGNAEKL---LEEVGIGKEYWQRNVLQLSGGQQQRVAIA 140
Cdd:PRK15112 84 Y-RSQRIRMIFQDPStslnprqrisqILDFPLRL-NTDLEPEQREKQIietLRQVGLLPDHASYYPHMLAPGQKQRLGLA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 141 RALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS----KHLaeeADEILEIKNGAI 206
Cdd:PRK15112 162 RALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHlgmmKHI---SDQVLVMHQGEV 228
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
9-187 |
4.11e-15 |
|
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: 71.29 E-value: 4.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 9 YAYKTKKdKTiLNNVSATFEEGIFY-----TIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKglnyhrkhnisl 83
Cdd:cd03237 1 YTYPTMK-KT-LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 84 vfQNYNLIDYLTTVENV---KLGGSGNAEKLLEEV----GIGKEYwQRNVLQLSGGQQQRVAIARALASDAHVLLADEPT 156
Cdd:cd03237 67 --PQYIKADYEGTVRDLlssITKDFYTHPYFKTEIakplQIEQIL-DREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
170 180 190
....*....|....*....|....*....|.
gi 489527143 157 GNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:cd03237 144 AYLDVEQRLMASKVIRRFAENNEKTAFVVEH 174
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-206 |
5.24e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.83 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnI 81
Cdd:PRK10790 341 IDIDNVSFAYR--DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG-V 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQN-YNLIDylTTVENVKLGGSGNAEKL---LEEV-----------GI----GKeywQRNvlQLSGGQQQRVAIARA 142
Cdd:PRK10790 418 AMVQQDpVVLAD--TFLANVTLGRDISEEQVwqaLETVqlaelarslpdGLytplGE---QGN--NLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEI----IALLKKTAhelgkcVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIqqalAAVREHTT------LVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
26-203 |
5.52e-15 |
|
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: 70.33 E-value: 5.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 26 TFEEGIFyTIVGPSGAGKTTLL-SLLAGL--DTAVKGTVLCNGEDITKKGlnyHRKHNISLVFQN-----YNLIDYLTTV 97
Cdd:cd03240 19 EFFSPLT-LIVGQNGAGKTTIIeALKYALtgELPPNSKGGAHDPKLIREG---EVRAQVKLAFENangkkYTITRSLAIL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 98 ENVKLGGSGNAEKLLEevgigkeywqRNVLQLSGGQQQ------RVAIARALASDAHVLLADEPTGNLDETTAD----EI 167
Cdd:cd03240 95 ENVIFCHQGESNWPLL----------DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeslaEI 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 489527143 168 IALLKKTAHELgkcVVVVTHSKHLAEEADEILEIKN 203
Cdd:cd03240 165 IEERKSQKNFQ---LIVITHDEELVDAADHIYRVEK 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-187 |
5.92e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.46 E-value: 5.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCnGEdiTKKglnyhrkhnI 81
Cdd:PRK11819 325 IEAENLSKSFG---DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--TVK---------L 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYLTTV-ENVklggSGNAEKLleEVGiGKE-----Y----------WQRNVLQLSGGQQQRVAIARALAS 145
Cdd:PRK11819 390 AYVDQSRDALDPNKTVwEEI----SGGLDII--KVG-NREipsraYvgrfnfkggdQQKKVGVLSGGERNRLHLAKTLKQ 462
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 146 DAHVLLADEPTGNLD-ET-TADEiIALLkktahELGKCVVVVTH 187
Cdd:PRK11819 463 GGNVLLLDEPTNDLDvETlRALE-EALL-----EFPGCAVVISH 500
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
35-187 |
1.00e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.15 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGL--------------DTAVK---GTVLCNG-EDITKKGLNYHRK----HNISLVFQNyNLID 92
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGElipnlgdyeeepswDEVLKrfrGTELQNYfKKLYNGEIKVVHKpqyvDLIPKVFKG-KVRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 93 YLTTVENvklggSGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLD----ETTADEII 168
Cdd:PRK13409 183 LLKKVDE-----RGKLDEVVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDirqrLNVARLIR 256
|
170
....*....|....*....
gi 489527143 169 ALLKktahelGKCVVVVTH 187
Cdd:PRK13409 257 ELAE------GKYVLVVEH 269
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-206 |
1.12e-14 |
|
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: 69.75 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKtILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhNI 81
Cdd:cd03369 7 IEVENLSVRYAPDLPP-VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS-SL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYNLIDYlTTVENVKLGGSGNAEKLLEEVGIgkeywQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDE 161
Cdd:cd03369 85 TIIPQDPTLFSG-TIRSNLDPFDEYSDEEIYGALRV-----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489527143 162 TTAdeiiALLKKTAHEL--GKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03369 159 ATD----ALIQKTIREEftNSTILTIAHRLRTIIDYDKILVMDAGEV 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
7-187 |
1.71e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 71.38 E-value: 1.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 7 VSYAYKTKKdktiLNNVSATFEEGIFY-----TIVGPSGAGKTTLLSLLAGLDTAVKGTVLcngEDITkkglnyhrkhnI 81
Cdd:PRK13409 341 VEYPDLTKK----LGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELK-----------I 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQnYNLIDYLTTVE------NVKLGGSGNAEKLLEEVGIGKEYwQRNVLQLSGGQQQRVAIARALASDAHVLLADEP 155
Cdd:PRK13409 403 SYKPQ-YIKPDYDGTVEdllrsiTDDLGSSYYKSEIIKPLQLERLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190
....*....|....*....|....*....|....*
gi 489527143 156 TGNLD---ETTADEIIallKKTAHELGKCVVVVTH 187
Cdd:PRK13409 481 SAHLDveqRLAVAKAI---RRIAEEREATALVVDH 512
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
7-187 |
2.15e-14 |
|
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: 70.97 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 7 VSYAYKTKKdktiLNNVSATFEEGIFY-----TIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeDITKKglnyhrkhnI 81
Cdd:COG1245 342 VEYPDLTKS----YGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEV-----DEDLK---------I 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQnYNLIDYLTTVE-------NVKLGGSGNAEKLLEEVGIGKEYwQRNVLQLSGGQQQRVAIARALASDAHVLLADE 154
Cdd:COG1245 404 SYKPQ-YISPDYDGTVEeflrsanTDDFGSSYYKTEIIKPLGLEKLL-DKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|...
gi 489527143 155 PTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDH 514
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-206 |
3.10e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.92 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 4 VKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAG-LDTAVKGTVLCNGEditkkgLNYHRKhnIS 82
Cdd:PLN03130 617 IKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT------VAYVPQ--VS 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LVFQnynlidyLTTVENVKLGGSGNAEKL--------------------LEEVGigkeywQRNVlQLSGGQQQRVAIARA 142
Cdd:PLN03130 689 WIFN-------ATVRDNILFGSPFDPERYeraidvtalqhdldllpggdLTEIG------ERGV-NISGGQKQRVSMARA 754
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLKKtaHEL-GKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PLN03130 755 VYSNSDVYIFDDPLSALDAHVGRQVFDKCIK--DELrGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-208 |
3.63e-14 |
|
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: 68.33 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 10 AYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDitkkglnyhrkhnISLVFQNYN 89
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV-------------SSLLGLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 90 LIDYLTTVENVKLGGS--GNAEKLLEEV--------GIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:cd03220 95 FNPELTGRENIYLNGRllGLSRKEIDEKideiiefsELG-DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489527143 160 DETTADEIIALLKKTaHELGKCVVVVTHSKHLAEE-ADEILEIKNGAISF 208
Cdd:cd03220 174 DAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-188 |
3.65e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 3.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 18 TILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDiTKKGLnyhRKHNISLVFQNYNL-IDYLTT 96
Cdd:PRK15056 21 TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQAL---QKNLVAYVPQSEEVdWSFPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 97 VENVKLGG---------------SGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDE 161
Cdd:PRK15056 97 VEDVVMMGryghmgwlrrakkrdRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180
....*....|....*....|....*..
gi 489527143 162 TTADEIIALLKKTAHElGKCVVVVTHS 188
Cdd:PRK15056 176 KTEARIISLLRELRDE-GKTMLVSTHN 201
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-187 |
4.48e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 4.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDktiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLnYH---- 76
Cdd:PRK11701 6 LLSVRGLTKLYGPRKG---CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL-YAlsea 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 77 -RKH----NISLVFQNYNliDYL-TTVE---NV--KLGGSGN---------AEKLLEEVGIGKEYWQRNVLQLSGGQQQR 136
Cdd:PRK11701 82 eRRRllrtEWGFVHQHPR--DGLrMQVSaggNIgeRLMAVGArhygdiratAGDWLERVEIDAARIDDLPTTFSGGMQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489527143 137 VAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH 210
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-172 |
7.33e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 7.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTA--VKGTVLCNGEDITKKGLNYHRKHNISLVFQNYNLIDYLTTV 97
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRFKDIRDSEALGIVIIHQELALIPYLSIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 98 ENVKLGG-------------SGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTA 164
Cdd:NF040905 97 ENIFLGNerakrgvidwnetNRRARELLAKVGL-DESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDS 175
|
....*...
gi 489527143 165 DEIIALLK 172
Cdd:NF040905 176 AALLDLLL 183
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-207 |
7.95e-14 |
|
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: 69.59 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeditkkglnyHRKHNI 81
Cdd:TIGR00957 637 ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV--------------HMKGSV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNyNLIDYLTTVENVKLGGSGN---------AEKLLEEV-----GIGKEYWQRNVlQLSGGQQQRVAIARALASDA 147
Cdd:TIGR00957 702 AYVPQQ-AWIQNDSLRENILFGKALNekyyqqvleACALLPDLeilpsGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489527143 148 HVLLADEPTGNLDETTADEII-------ALLKktahelGKCVVVVTHSKHLAEEADEILEIKNGAIS 207
Cdd:TIGR00957 780 DIYLFDDPLSAVDAHVGKHIFehvigpeGVLK------NKTRILVTHGISYLPQVDVIIVMSGGKIS 840
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-193 |
8.61e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.74 E-value: 8.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVsyaYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLD--TAVKGTVLCNGEDITKKGLNYHRK 78
Cdd:CHL00131 7 ILEIKNL---HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQN------YNLIDYLTTVENVKLGGSGNAE-----------KLLEEVGIGKEYWQRNVLQ-LSGGQQQRVAIA 140
Cdd:CHL00131 84 LGIFLAFQYpieipgVSNADFLRLAYNSKRKFQGLPEldplefleiinEKLKLVGMDPSFLSRNVNEgFSGGEKKRNEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 141 RALASDAHVLLADEPTGNLDettadeiIALLKKTAHEL------GKCVVVVTHSKHLAE 193
Cdd:CHL00131 164 QMALLDSELAILDETDSGLD-------IDALKIIAEGInklmtsENSIILITHYQRLLD 215
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-206 |
2.06e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.46 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAG-LDTAVKGTVLCNGEditkkgLNYHRKhn 80
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS------VAYVPQ-- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQnynlidyLTTVENVKLGGSGNAEKLLEEVGIG--------------KEYWQRNVlQLSGGQQQRVAIARALASD 146
Cdd:PLN03232 687 VSWIFN-------ATVRENILFGSDFESERYWRAIDVTalqhdldllpgrdlTEIGERGV-NISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 147 AHVLLADEPTGNLDETTADEIIALLKKtaHEL-GKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PLN03232 759 SDIYIFDDPLSALDAHVAHQVFDSCMK--DELkGKTRVLVTNQLHFLPLMDRIILVSEGMI 817
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-187 |
3.54e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.03 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYK------------------TKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVL 62
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfrrEYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 63 CNGEDITKKGLNYhrKHNISLVF-QNYNLIDYLTTVENVKLGGS----------GNAEKLLEEVGIGkEYWQRNVLQLSG 131
Cdd:COG4586 81 VLGYVPFKRRKEF--ARRIGVVFgQRSQLWWDLPAIDSFRLLKAiyripdaeykKRLDELVELLDLG-ELLDTPVRQLSL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 132 GQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTH 187
Cdd:COG4586 158 GQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSH 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-205 |
3.77e-13 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 65.82 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHN---ISLVFQNYNLIDyLTT 96
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVAYAAQKPWLLN-ATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 97 VENVKLGGSGNAEKL--------------LEEVGIGKEYWQRNVlQLSGGQQQRVAIARALASDAHVLLADEPTGNLDET 162
Cdd:cd03290 96 EENITFGSPFNKQRYkavtdacslqpdidLLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489527143 163 TADEII-ALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGA 205
Cdd:cd03290 175 LSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-204 |
5.09e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 5 KNVSYAYKTKKdkTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVkgtvlcNGEDITKKGLNyhrkhnISLV 84
Cdd:PRK11819 10 NRVSKVVPPKK--QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEF------EGEARPAPGIK------VGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 85 FQNYNLIDYLTTVENVKLG------------------GSGNAE--KLLEEVGIGKEY----------------------- 121
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEEGvaevkaaldrfneiyaayAEPDADfdALAAEQGELQEIidaadawdldsqleiamdalrcp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 122 -WQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDEttadEIIALLKKTAHELGKCVVVVTHSKH-LAEEADEIL 199
Cdd:PRK11819 156 pWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESVAWLEQFLHDYPGTVVAVTHDRYfLDNVAGWIL 231
|
....*
gi 489527143 200 EIKNG 204
Cdd:PRK11819 232 ELDRG 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
35-187 |
9.27e-13 |
|
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: 66.35 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGL--------------DTAVK---GTVLCNG-EDITKKGLNYHRK----HNISLVFQNyNLID 92
Cdd:COG1245 104 ILGPNGIGKSTALKILSGElkpnlgdydeepswDEVLKrfrGTELQDYfKKLANGEIKVAHKpqyvDLIPKVFKG-TVRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 93 YLTTVENvklggSGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLD---ETTADEIIa 169
Cdd:COG1245 183 LLEKVDE-----RGKLDELAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqRLNVARLI- 255
|
170
....*....|....*...
gi 489527143 170 llKKTAhELGKCVVVVTH 187
Cdd:COG1245 256 --RELA-EEGKYVLVVEH 270
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-198 |
1.27e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 65.31 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKttllSLLAgldtavkgTVLC---------------- 63
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVkAVDRVSLTLNEGEIRGLVGESGSGK----SLIA--------KAICgitkdnwhvtadrfrw 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 64 NGEDITKKGLNYHRK---HNISLVFQNYN-LIDYLTTVE--------NVKLGGS---------GNAEKLLEEVGIgKEYw 122
Cdd:COG4170 71 NGIDLLKLSPRERRKiigREIAMIFQEPSsCLDPSAKIGdqlieaipSWTFKGKwwqrfkwrkKRAIELLHRVGI-KDH- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 123 qRNVL-----QLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHS-KHLAEEAD 196
Cdd:COG4170 149 -KDIMnsyphELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDlESISQWAD 227
|
..
gi 489527143 197 EI 198
Cdd:COG4170 228 TI 229
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-187 |
1.59e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.71 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 37 GPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITkkglNYHRKHNISLVFQNYNLIDYLTTVENVK----LGG------SG 106
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT----RGDRSRFMAYLGHLPGLKADLSTLENLHflcgLHGrrakqmPG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 107 NAeklLEEVGIGkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDEttadEIIALLKK--TAH-ELGKCVV 183
Cdd:PRK13543 120 SA---LAIVGLA-GYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLVNRmiSAHlRGGGAAL 191
|
....
gi 489527143 184 VVTH 187
Cdd:PRK13543 192 VTTH 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-208 |
2.68e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.69 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKdktILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHN 80
Cdd:PRK15439 11 LLCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNYNLIDYLTTVENVKLGGSGNA------EKLLEEVGIgkeywQRNvLQLSGG-----QQQRVAIARALASDAHV 149
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILFGLPKRQasmqkmKQLLAALGC-----QLD-LDSSAGslevaDRQIVEILRGLMRDSRI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 150 LLADEPTGNLD--ETTA--DEIIALLKKtahelGKCVVVVTHSKH-LAEEADEILEIKNGAISF 208
Cdd:PRK15439 162 LILDEPTASLTpaETERlfSRIRELLAQ-----GVGIVFISHKLPeIRQLADRISVMRDGTIAL 220
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-160 |
2.84e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.65 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 6 NVSYayktkKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAG-------LDTAVKGTVLCNGEDItkkglnYHRK 78
Cdd:PRK10938 267 VVSY-----NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysNDLTLFGRRRGSGETI------WDIK 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 HNISLVFQNYNLiDYL--TTVENVKLGG-----------SGNAEKL----LEEVGIGKEYWQRNVLQLSGGQQQRVAIAR 141
Cdd:PRK10938 336 KHIGYVSSSLHL-DYRvsTSVRNVILSGffdsigiyqavSDRQQKLaqqwLDILGIDKRTADAPFHSLSWGQQRLALIVR 414
|
170
....*....|....*....
gi 489527143 142 ALASDAHVLLADEPTGNLD 160
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLD 433
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-201 |
4.68e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.98 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHNISLVFQNYNLIDYLTTVEN 99
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 100 VKLGGS-------------GNAEKLLEEVGIGKEYWQRnVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADE 166
Cdd:PRK10982 94 MWLGRYptkgmfvdqdkmyRDTKAIFDELDIDIDPRAK-VATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNH 172
|
170 180 190
....*....|....*....|....*....|....*
gi 489527143 167 IIALLKKTaHELGKCVVVVTHskhlaeEADEILEI 201
Cdd:PRK10982 173 LFTIIRKL-KERGCGIVYISH------KMEEIFQL 200
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-206 |
7.67e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.92 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAyktKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTA--------VKGTVLCNGEDITKkg 72
Cdd:PRK13547 1 MLTADHLHVA---RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarVTGDVTLNGEPLAA-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 73 LNYHRKHNISLVFQNYNLIDYLTTVENVKLGG---------------SGNAEKLLEEVGiGKEYWQRNVLQLSGGQQQRV 137
Cdd:PRK13547 76 IDAPRLARLRAVLPQAAQPAFAFSAREIVLLGrypharragalthrdGEIAWQALALAG-ATALVGRDVTTLSGGELARV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 138 AIARALA---------SDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHL-AEEADEILEIKNGAI 206
Cdd:PRK13547 155 QFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRIAMLADGAI 233
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-203 |
9.31e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 9.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCN-GEDITKKGLNYHR--- 77
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRski 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 --------------KHNISLVFQNYNLIDYLTTVEN-----------------VKLGG-------SGNAEKLL------- 112
Cdd:PTZ00265 463 gvvsqdpllfsnsiKNNIKYSLYSLKDLEALSNYYNedgndsqenknkrnscrAKCAGdlndmsnTTDSNELIemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 113 -----EEVGIGKEYW----------------QRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTAdeiiALL 171
Cdd:PTZ00265 543 tikdsEVVDVSKKVLihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE----YLV 618
|
250 260 270
....*....|....*....|....*....|....*.
gi 489527143 172 KKTAHEL----GKCVVVVTHSKHLAEEADEILEIKN 203
Cdd:PTZ00265 619 QKTINNLkgneNRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-162 |
1.21e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNgediTKKGLNYHRKHNIS 82
Cdd:PRK11147 321 EMENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEVAYFDQHRAE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 83 LvfqnynliDYLTTVE-NVKLGGsgnaekllEEVGI-GKEywqRNVL------------------QLSGGQQQRVAIARA 142
Cdd:PRK11147 394 L--------DPEKTVMdNLAEGK--------QEVMVnGRP---RHVLgylqdflfhpkramtpvkALSGGERNRLLLARL 454
|
170 180
....*....|....*....|.
gi 489527143 143 LASDAHVLLADEPTGNLD-ET 162
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDvET 475
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
12-178 |
3.02e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 12 KTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLA----GLDTAVKGTVLCNG---EDITKkglnyHRKHNISLV 84
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpEEIKK-----HYRGDVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 85 FQNYNLIDYLTTVENV----KLGGSGNAEKLLEEvgigKEYWQ---------------RN-------VLQLSGGQQQRVA 138
Cdd:TIGR00956 144 AETDVHFPHLTVGETLdfaaRCKTPQNRPDGVSR----EEYAKhiadvymatyglshtRNtkvgndfVRGVSGGERKRVS 219
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489527143 139 IARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHEL 178
Cdd:TIGR00956 220 IAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANIL 259
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
19-208 |
6.73e-11 |
|
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: 61.08 E-value: 6.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 19 ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEditkkglnyhrkhnISLVFQnYNLIDYLTTVE 98
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQ-TSWIMPGTIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 99 NVKLGGSG---------NAEKLLEEVGIGKEYwQRNVL-----QLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTA 164
Cdd:TIGR01271 506 NIIFGLSYdeyrytsviKACQLEEDIALFPEK-DKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489527143 165 DEIIA------LLKKTAhelgkcVVVVTHSKHLaEEADEILEIKNGAISF 208
Cdd:TIGR01271 585 KEIFEsclcklMSNKTR------ILVTSKLEHL-KKADKILLLHEGVCYF 627
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-187 |
6.95e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 6.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 28 EEGIFYTIVGPSGAGKTTLLSLLAG--------------LDTAVK---GTVLCNG-EDITKKGLNYHRK-HNISLVFQNY 88
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGklkpnlgkfddppdWDEILDefrGSELQNYfTKLLEGDVKVIVKpQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 89 --NLIDYLTTVENvklggSGNAEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLD---ETT 163
Cdd:cd03236 104 kgKVGELLKKKDE-----RGKLDELVDQLEL-RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDikqRLN 177
|
170 180
....*....|....*....|....
gi 489527143 164 ADEIIALLKKTahelGKCVVVVTH 187
Cdd:cd03236 178 AARLIRELAED----DNYVLVVEH 197
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-206 |
7.03e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 60.71 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL-DTAVKGTVLCNGEDITKKGLNYHRKH 79
Cdd:PRK13549 259 ILEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAIAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQN---YNLIDYLTTVENVKL--------GGSGNAEKlleEVGIGKEYWQR----------NVLQLSGGQQQRVA 138
Cdd:PRK13549 339 GIAMVPEDrkrDGIVPVMGVGKNITLaaldrftgGSRIDDAA---ELKTILESIQRlkvktaspelAIARLSGGNQQKAV 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 139 IARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVthSKHLAEE---ADEILEIKNGAI 206
Cdd:PRK13549 416 LAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI--SSELPEVlglSDRVLVMHEGKL 483
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-172 |
7.43e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 7.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 6 NVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAG---LD--------------------TAVKGTVL 62
Cdd:PRK11147 5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDdgriiyeqdlivarlqqdppRNVEGTVY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 63 cngeDITKKGLNY-----HRKHNIS-LVFQNYN--LIDYLTTVENVklggsgnaeklLEEVGIgkeyWQ-----RNVLQ- 128
Cdd:PRK11147 85 ----DFVAEGIEEqaeylKRYHDIShLVETDPSekNLNELAKLQEQ-----------LDHHNL----WQlenriNEVLAq 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 129 -----------LSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLK 172
Cdd:PRK11147 146 lgldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-205 |
8.85e-11 |
|
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: 58.49 E-value: 8.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLslLAGLDTAvkgtvlcnGEDITKKGLNYHRKHNISLVFQNYNLIDylttven 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYAS--------GKARLISFLPKFSRNKLIFIDQLQFLID------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 100 vklggsgnaeklleeVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAH--VLLADEPTGNLDETTADEIIALLKKTAhE 177
Cdd:cd03238 74 ---------------VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLI-D 137
|
170 180
....*....|....*....|....*...
gi 489527143 178 LGKCVVVVTHSKHLAEEADEILEIKNGA 205
Cdd:cd03238 138 LGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
27-202 |
1.39e-10 |
|
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: 58.43 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 27 FEEGIFYTIVGPSGAGKTTLLSLLAgldTAVKGTVLCNGEDItkkGLNYHRKHN-----ISLVFQN----YNLIDYL--- 94
Cdd:cd03279 25 LDNNGLFLICGPTGAGKSTILDAIT---YALYGKTPRYGRQE---NLRSVFAPGedtaeVSFTFQLggkkYRVERSRgld 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 95 -TTVENVKLGGSGNAEKLLEevgigkeywqRNVLQLSGGQQQRVAIARALASDAHV----------LLADEPTGNLDETT 163
Cdd:cd03279 99 yDQFTRIVLLPQGEFDRFLA----------RPVSTLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEA 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 489527143 164 ADEIIALLKKTaHELGKCVVVVTHSKHLAEEADEILEIK 202
Cdd:cd03279 169 LEAVATALELI-RTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-204 |
2.94e-10 |
|
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: 59.07 E-value: 2.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGL-DTAVKGTVLCNGEDITKKGLNYHRKH 79
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQN---YNLIDYLTTVENVKLG------GSGNAEKLLEEVGIGKEYWQRNV---------LQLSGGQQQRVAIAR 141
Cdd:TIGR02633 337 GIAMVPEDrkrHGIVPILGVGKNITLSvlksfcFKMRIDAAAELQIIGSAIQRLKVktaspflpiGRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489527143 142 ALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVthSKHLAEE---ADEILEIKNG 204
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVV--SSELAEVlglSDRVLVIGEG 479
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-207 |
4.18e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYktkkdktiLNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKK----GLNY-- 75
Cdd:PRK10762 258 LKVDNLSGPG--------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdGLANgi 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 -----HRKHNiSLVF-----QNYNL--IDYLTtvenvKLGGSGNAEKLLEEVG-------IGKEYWQRNVLQLSGGQQQR 136
Cdd:PRK10762 330 vyiseDRKRD-GLVLgmsvkENMSLtaLRYFS-----RAGGSLKHADEQQAVSdfirlfnIKTPSMEQAIGLLSGGNQQK 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489527143 137 VAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVthSKHLAE---EADEILEIKNGAIS 207
Cdd:PRK10762 404 VAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILV--SSEMPEvlgMSDRILVMHEGRIS 474
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-208 |
4.47e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 58.64 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 17 KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCngeditkkglnyhrKHNISLVFQNYNLIDyLTT 96
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA--------------ERSIAYVPQQAWIMN-ATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 97 VENVKLGGSGNAEKLLEEV--------------GIGKEYWQRNVlQLSGGQQQRVAIARALASDAHVLLADEPTGNLDET 162
Cdd:PTZ00243 738 RGNILFFDEEDAARLADAVrvsqleadlaqlggGLETEIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527143 163 TADEII--ALLKKTAhelGKCVVVVTHSKHLAEEADEILEIKNGAISF 208
Cdd:PTZ00243 817 VGERVVeeCFLGALA---GKTRVLATHQVHVVPRADYVVALGDGRVEF 861
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-203 |
6.94e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLL------------------------------- 50
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgd 1245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 51 --------------------AGLDTAV---KGTVLCNGEDITKKGLNYHRkHNISLVFQNYNLIDyLTTVENVKLGgsgN 107
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggSGEDSTVfknSGKILLDGVDICDYNLKDLR-NLFSIVSQEPMLFN-MSIYENIKFG---K 1320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 108 AEKLLEEVGIGKEY-------------WQRNV----LQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIAL 170
Cdd:PTZ00265 1321 EDATREDVKRACKFaaidefieslpnkYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
250 260 270
....*....|....*....|....*....|...
gi 489527143 171 LKKTAHELGKCVVVVTHSKHLAEEADEILEIKN 203
Cdd:PTZ00265 1401 IVDIKDKADKTIITIAHRIASIKRSDKIVVFNN 1433
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-204 |
8.73e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 8.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 30 GIFYTIVGPSGAGKTTLLSLLAG-LDTAVKGTVLCNGEDITKKGLNYHRKHNISlvfqnynlidylttvenvklggsgna 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALAReLGPPGGGVIYIDGEDILEEVLDQLLLIIVG-------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 109 eklleevgigkeywqRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIAL-----LKKTAHELGKCVV 183
Cdd:smart00382 56 ---------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLLLKSEKNLTVI 120
|
170 180
....*....|....*....|....*..
gi 489527143 184 VVTH------SKHLAEEADEILEIKNG 204
Cdd:smart00382 121 LTTNdekdlgPALLRRRFDRRIVLLLI 147
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-172 |
1.17e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.26 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKTKKDkTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRkHNI 81
Cdd:TIGR00957 1285 VEFRNYCLRYREDLD-LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR-FKI 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLV-----------------FQNYNLIDYLTTVENVKLGG--SGNAEKLLEEVGIGKEywqrnvlQLSGGQQQRVAIARA 142
Cdd:TIGR00957 1363 TIIpqdpvlfsgslrmnldpFSQYSDEEVWWALELAHLKTfvSALPDKLDHECAEGGE-------NLSVGQRQLVCLARA 1435
|
170 180 190
....*....|....*....|....*....|
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLK 172
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTIR 1465
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-207 |
1.36e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 30 GIFytivGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHNISL---------------VFQNYN----- 89
Cdd:PRK11288 283 GLF----GLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLcpedrkaegiipvhsVADNINisarr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 90 -------LIDYLTTVENvklggsgnAEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDET 162
Cdd:PRK11288 359 hhlragcLINNRWEAEN--------ADRFIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489527143 163 TADEIIALLKKTAhELGKCVVVVthSKHLAEE---ADEILEIKNGAIS 207
Cdd:PRK11288 431 AKHEIYNVIYELA-AQGVAVLFV--SSDLPEVlgvADRIVVMREGRIA 475
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
19-208 |
1.73e-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: 56.02 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 19 ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHR----KHNIsLVFQNYNLIDYL 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMpgtiKENI-IFGVSYDEYRYK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 95 TTVENVKLGG--SGNAEK---LLEEVGIgkeywqrnvlQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEII- 168
Cdd:cd03291 131 SVVKACQLEEdiTKFPEKdntVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFe 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527143 169 -ALLKKTAHelgKCVVVVTHSKHLAEEADEILEIKNGAISF 208
Cdd:cd03291 201 sCVCKLMAN---KTRILVTSKMEHLKKADKILILHEGSSYF 238
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
110-205 |
2.75e-09 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 54.96 E-value: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 110 KLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASD----AHVLlaDEPTGNLDETTADEIIALLKKTaHELGKCVVVV 185
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGltgvLYVL--DEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVV 195
|
90 100
....*....|....*....|
gi 489527143 186 THSKHLAEEADEILEIKNGA 205
Cdd:cd03270 196 EHDEDTIRAADHVIDIGPGA 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-198 |
3.52e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.58 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKT-ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLD------TAVKgtVLCNGEDITKKGL 73
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwrvTADR--MRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 74 NYHRK---HNISLVFQNYNliDYLTTVENV------KLGGSG--------------NAEKLLEEVGIG--KEYWQRNVLQ 128
Cdd:PRK15093 81 RERRKlvgHNVSMIFQEPQ--SCLDPSERVgrqlmqNIPGWTykgrwwqrfgwrkrRAIELLHRVGIKdhKDAMRSFPYE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 129 LSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKH-LAEEADEI 198
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmLSQWADKI 229
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-207 |
5.73e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLcngeditkkglnyhRKHNISLVFQNYNLIDYLTTVENVKLGGS----GNAEK 110
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVF--------------RSAKVRMAVFSQHHVDGLDLSSNPLLYMMrcfpGVPEQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 111 LLE----EVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDettADEIIALLKKTAHELGKcVVVVT 186
Cdd:PLN03073 606 KLRahlgSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LDAVEALIQGLVLFQGG-VLMVS 681
|
170 180
....*....|....*....|..
gi 489527143 187 HSKHL-AEEADEILEIKNGAIS 207
Cdd:PLN03073 682 HDEHLiSGSVDELWVVSEGKVT 703
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
19-204 |
9.35e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 9.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 19 ILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTA--VKGTVLCNGedITKKGLNYHR------KHNI--------- 81
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISG--FPKKQETFARisgyceQNDIhspqvtvre 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNY-------------NLIDylTTVENVKLGGSGNAeklleEVGIGkeywqrNVLQLSGGQQQRVAIARALASDAH 148
Cdd:PLN03140 973 SLIYSAFlrlpkevskeekmMFVD--EVMELVELDNLKDA-----IVGLP------GVTGLSTEQRKRLTIAVELVANPS 1039
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 149 VLLADEPTGNLDETTADEIIALLKKTAhELGKCVVVVTH--SKHLAEEADEILEIKNG 204
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMRTVRNTV-DTGRTVVCTIHqpSIDIFEAFDELLLMKRG 1096
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-189 |
1.22e-08 |
|
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: 53.70 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLdTAVKGTVLCNGEDITKKGLNYHRKhNI 81
Cdd:cd03289 3 MTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVPLQKWRK-AF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYnLIDYLTTVENVKLGGSGNAEKLL---EEVGIgkeywqRNVLQ----------------LSGGQQQRVAIARA 142
Cdd:cd03289 80 GVIPQKV-FIFSGTFRKNLDPYGKWSDEEIWkvaEEVGL------KSVIEqfpgqldfvlvdggcvLSHGHKQLMCLARS 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLKktaHELGKCVVVVTHSK 189
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLK---QAFADCTVILSEHR 196
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-207 |
2.46e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.13 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 22 NVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITK--------KGLNY---HRKH----------- 79
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAlstaqrlaRGLVYlpeDRQSsglyldaplaw 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVKLggsgnaEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:PRK15439 361 NVCALTHNRRGFWIKPARENAVL------ERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489527143 160 DETTADEIIALLKKTAHElgkCVVVVTHSKHLAE---EADEILEIKNGAIS 207
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAQ---NVAVLFISSDLEEieqMADRVLVMHQGEIS 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-203 |
2.55e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 17 KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVL---------CNGED--ITKKGLNY-------HRK 78
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETpaLPQPALEYvidgdreYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 79 --------------HNISLVFQNYNLIDYLTTvenvklggSGNAEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALA 144
Cdd:PRK10636 94 leaqlhdanerndgHAIATIHGKLDAIDAWTI--------RSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489527143 145 SDAHVLLADEPTGNLDettADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKN 203
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-206 |
2.80e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 2.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhNISLV-----------------FQNYNLIDYLTTV 97
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR-VLSIIpqspvlfsgtvrfnidpFSEHNDADLWEAL 1345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 98 E--NVKLGGSGNAEKLLEEVGIGKEywqrnvlQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTAdeiiALLKKTA 175
Cdd:PLN03232 1346 EraHIKDVIDRNPFGLDAEVSEGGE-------NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD----SLIQRTI 1414
|
170 180 190
....*....|....*....|....*....|...
gi 489527143 176 -HELGKC-VVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:PLN03232 1415 rEEFKSCtMLVIAHRLNTIIDCDKILVLSSGQV 1447
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-193 |
3.88e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.99 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYkTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLdTAVKGTVLCNGEDITKKGLNYHRKhNI 81
Cdd:TIGR01271 1218 MDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVTLQTWRK-AF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNYnLIDYLTTVENVKLGGSGNAE---KLLEEVGIgkeywqRNVLQ----------------LSGGQQQRVAIARA 142
Cdd:TIGR01271 1295 GVIPQKV-FIFSGTFRKNLDPYEQWSDEeiwKVAEEVGL------KSVIEqfpdkldfvlvdggyvLSNGHKQLMCLARS 1367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489527143 143 LASDAHVLLADEPTGNLDETTADEIIALLKktaHELGKCVVVVthSKHLAE 193
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLK---QSFSNCTVIL--SEHRVE 1413
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-185 |
4.30e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 4.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTL-LSLLA---GldTAVKGTVLCNGEDIT------- 69
Cdd:NF040905 257 VFEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVFGrsyG--RNISGTVFKDGKEVDvstvsda 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 70 -KKGLNY---HRKHNislvfqNYNLIDylTTVENVKLGG-SGNAEKLL----EEVGIGKEYWQR------NVLQ----LS 130
Cdd:NF040905 335 iDAGLAYvteDRKGY------GLNLID--DIKRNITLANlGKVSRRGVidenEEIKVAEEYRKKmniktpSVFQkvgnLS 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489527143 131 GGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVV 185
Cdd:NF040905 407 GGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVI 460
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-191 |
5.00e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 52.48 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTV-LCNGEDitkkgLNYHRKH 79
Cdd:PRK10636 312 LLKMEKVSAGYG---DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIK-----LGYFAQH 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISLVFQNYNLIDYLTTVENVK--------LGGSG-NAEKLLEEVGigkeywqrnvlQLSGGQQQRVAIARALASDAHVL 150
Cdd:PRK10636 384 QLEFLRADESPLQHLARLAPQEleqklrdyLGGFGfQGDKVTEETR-----------RFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489527143 151 LADEPTGNLDEttadEIIALLKKTAHELGKCVVVVTHSKHL 191
Cdd:PRK10636 453 LLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHL 489
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-160 |
5.76e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.20 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 2 LEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeditkkglNYHRKHNI 81
Cdd:PRK15064 320 LEVENLTKGFD---NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSENANI 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 82 SLVFQNY--------NLIDYLTTVENVK---------LGgsgnaeKLLeevgIGKEYWQRNVLQLSGGQQQRVAIARALA 144
Cdd:PRK15064 385 GYYAQDHaydfendlTLFDWMSQWRQEGddeqavrgtLG------RLL----FSQDDIKKSVKVLSGGEKGRMLFGKLMM 454
|
170
....*....|....*.
gi 489527143 145 SDAHVLLADEPTGNLD 160
Cdd:PRK15064 455 QKPNVLVMDEPTNHMD 470
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-207 |
3.14e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVsyaykTKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHN 80
Cdd:PRK10982 250 ILEVRNL-----TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 81 ISLVFQNY-------NL-IDYLTTVENVKlgGSGNAEKLLEEVGIGKE-YW------------QRNVLQLSGGQQQRVAI 139
Cdd:PRK10982 325 FALVTEERrstgiyaYLdIGFNSLISNIR--NYKNKVGLLDNSRMKSDtQWvidsmrvktpghRTQIGSLSGGNQQKVII 402
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489527143 140 ARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVTHSKHLAEEADEILEIKNGAIS 207
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA 470
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
26-202 |
5.15e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 26 TFEEGIFYTIVGPSGAGKTTLL---SLLAGLDTAVkgtvlcngediTKKGLNYHRKHNISLVFQNYNLIdylttvenvkl 102
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILdaiGLALGGAQSA-----------TRRRSGVKAGCIVAAVSAELIFT----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 103 ggsgnaeklleevgigkeywqrnVLQLSGGQQQRVAIARALASDAH----VLLADEPTGNLDETTADEIIALLKKTAheL 178
Cdd:cd03227 75 -----------------------RLQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHL--V 129
|
170 180
....*....|....*....|....*
gi 489527143 179 GKC-VVVVTHSKHLAEEADEILEIK 202
Cdd:cd03227 130 KGAqVIVITHLPELAELADKLIHIK 154
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-190 |
5.56e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 17 KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTV-LCNGEDITKKGLNyhrkhniSLVFQNYNLIDylt 95
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVsLDPNERLGKLRQD-------QFAFEEFTVLD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 96 TV------------------------------------ENVKLGG---SGNAEKLLEEVGIGKEYWQRNVLQLSGGQQQR 136
Cdd:PRK15064 84 TVimghtelwevkqerdriyalpemseedgmkvadlevKFAEMDGytaEARAGELLLGVGIPEEQHYGLMSEVAPGWKLR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489527143 137 VAIARALASDAHVLLADEPTGNLDETTadeiIALLKKTAHELGKCVVVVTHSKH 190
Cdd:PRK15064 164 VLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHDRH 213
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-188 |
5.96e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 20 LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVlcngeDItkkglnyhrKHNISLVFQNYNLIDYLTTVEN 99
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DI---------KGSAALIAISSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 100 VKLGG--SGNAEKLLEEV--------GIGKeYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIA 169
Cdd:PRK13545 106 IELKGlmMGLTKEKIKEIipeiiefaDIGK-FIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170
....*....|....*....
gi 489527143 170 LLKKTaHELGKCVVVVTHS 188
Cdd:PRK13545 185 KMNEF-KEQGKTIFFISHS 202
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-156 |
6.51e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 3 EVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGlnyHRK---H 79
Cdd:NF033858 3 RLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADAR---HRRavcP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISlvfqnY-------NLIDYLTTVENV----KLGGSGNAEK------LLEEVGI--------GKeywqrnvlqLSGGQQ 134
Cdd:NF033858 77 RIA-----YmpqglgkNLYPTLSVFENLdffgRLFGQDAAERrrrideLLRATGLapfadrpaGK---------LSGGMK 142
|
170 180
....*....|....*....|..
gi 489527143 135 QRVAIARALASDAHVLLADEPT 156
Cdd:NF033858 143 QKLGLCCALIHDPDLLILDEPT 164
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-177 |
1.31e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKhNISLV-----------------FQNYNLIDYLTTV 97
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK-VLGIIpqapvlfsgtvrfnldpFNEHNDADLWESL 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 98 ENVKLGGS--GNAEKLLEEVGIGKEywqrnvlQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTAdeiiALLKKTA 175
Cdd:PLN03130 1349 ERAHLKDVirRNSLGLDAEVSEAGE-------NFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD----ALIQKTI 1417
|
..
gi 489527143 176 HE 177
Cdd:PLN03130 1418 RE 1419
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-198 |
3.39e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.02 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYayktKKDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVL---CNGEDITKKGLNYhR 77
Cdd:PRK13541 1 MLSLHQLQF----NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYyknCNINNIAKPYCTY-I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 78 KHNISLVFQnynlidyLTTVENVKLGGS--GNAEKLLEEVGIGK--EYWQRNVLQLSGGQQQRVAIARALASDAHVLLAD 153
Cdd:PRK13541 76 GHNLGLKLE-------MTVFENLKFWSEiyNSAETLYAAIHYFKlhDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLD 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489527143 154 EPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEEADEI 198
Cdd:PRK13541 149 EVETNLSKENRDLLNNLIVMKANS-GGIVLLSSHLESSIKSAQIL 192
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-187 |
3.52e-06 |
|
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: 45.64 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 27 FEEGIFYTIVGPSGAGKTTLLSLLAGldtavkgTVLCNGEDITkkglnyhrkhnislvfqnynlIDYLTTVenvklggsg 106
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAG-------QLIPNGDNDE---------------------WDGITPV--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 107 naeklleevgigkeyWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHELGKCVVVVT 186
Cdd:cd03222 65 ---------------YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVE 129
|
.
gi 489527143 187 H 187
Cdd:cd03222 130 H 130
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
35-207 |
7.87e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnISLVFQNYNLIDYlTTVENVK--LGGSgNAE--K 110
Cdd:PTZ00243 1341 IVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ-FSMIPQDPVLFDG-TVRQNVDpfLEAS-SAEvwA 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 111 LLEEVGIGK------EYWQRNVLQ----LSGGQQQRVAIARA-LASDAHVLLADEPTGNLDETTADEIIALLKK--TAHE 177
Cdd:PTZ00243 1418 ALELVGLRErvasesEGIDSRVLEggsnYSVGQRQLMCMARAlLKKGSGFILMDEATANIDPALDRQIQATVMSafSAYT 1497
|
170 180 190
....*....|....*....|....*....|
gi 489527143 178 lgkcVVVVTHSKHLAEEADEILEIKNGAIS 207
Cdd:PTZ00243 1498 ----VITIAHRLHTVAQYDKIIVMDHGAVA 1523
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
110-205 |
1.01e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 110 KLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASD----AHVLlaDEPTGNLDETTADEIIALLKKTaHELGKCVVVV 185
Cdd:TIGR00630 470 GFLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIGSGltgvLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVV 546
|
90 100
....*....|....*....|
gi 489527143 186 THSKHLAEEADEILEIKNGA 205
Cdd:TIGR00630 547 EHDEDTIRAADYVIDIGPGA 566
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
96-205 |
1.62e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.20 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 96 TVENVkLGGSGNAEKLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASD----AHVLlaDEPTGNLDETTADEIIALL 171
Cdd:PRK00635 445 SIEEV-LQGLKSRLSILIDLGLPYLTPERALATLSGGEQERTALAKHLGAEligiTYIL--DEPSIGLHPQDTHKLINVI 521
|
90 100 110
....*....|....*....|....*....|....
gi 489527143 172 KKTAHElGKCVVVVTHSKHLAEEADEILEIKNGA 205
Cdd:PRK00635 522 KKLRDQ-GNTVLLVEHDEQMISLADRIIDIGPGA 554
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-188 |
1.75e-05 |
|
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: 45.00 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 33 YTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKkglnyhrkhNISLVFQN------YNLIDYLTTVEN-----VK 101
Cdd:TIGR01257 1968 FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT---------NISDVHQNmgycpqFDAIDDLLTGREhlylyAR 2038
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 102 LGG--SGNAEKL----LEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTA----DEIIALL 171
Cdd:TIGR01257 2039 LRGvpAEEIEKVanwsIQSLGL-SLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARrmlwNTIVSII 2117
|
170
....*....|....*..
gi 489527143 172 KKtahelGKCVVVVTHS 188
Cdd:TIGR01257 2118 RE-----GRAVVLTSHS 2129
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-206 |
4.18e-05 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 42.97 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 17 KTILNNVSATFEEGIFYTIVGPSGAGKTTL-LSLLAGLDTaVKGTVLCNGEDITKKGLNYHRKHnISLVFQNYNLIDYlT 95
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRMVDI-FDGKIVIDGIDISKLPLHTLRSR-LSIILQDPILFSG-S 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 96 TVENVKLGGSGNAEKLLEEVGIGKeywQRNVLQ----------------LSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:cd03288 111 IRFNLDPECKCTDDRLWEALEIAQ---LKNMVKslpggldavvteggenFSVGQRQLFCLARAFVRKSSILIMDEATASI 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489527143 160 DETTaDEIIALLKKTAHElGKCVVVVTHSKHLAEEADEILEIKNGAI 206
Cdd:cd03288 188 DMAT-ENILQKVVMTAFA-DRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-86 |
6.93e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 42.47 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 1 MLEVKNVSYAYKtkkDKTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLD--TAVKGTVLCNGEDITKKGLNYHRK 78
Cdd:PRK09580 1 MLSIKDLHVSVE---DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAG 77
|
....*...
gi 489527143 79 HNISLVFQ 86
Cdd:PRK09580 78 EGIFMAFQ 85
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
27-187 |
7.55e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.92 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 27 FEEGIFyTIVGPSGAGKTTLLSLLA-------------GLDTAVKGTVLCNGE-DITKKGLNY----------------- 75
Cdd:COG0419 21 FDDGLN-LIVGPNGAGKSTILEAIRyalygkarsrsklRSDLINVGSEEASVElEFEHGGKRYrierrqgefaefleakp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 -HRKHNISLVFQNYNLIDYLTTVENVKLGGSGNAEKLLEEVGIGKEYWQR-----NVLQLSGGQQQRVAIARALAsdahv 149
Cdd:COG0419 100 sERKEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlsgldPIETLSGGERLRLALADLLS----- 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 489527143 150 LLADepTGNLDETTADEIIALLKKTAhelgkcvvVVTH 187
Cdd:COG0419 175 LILD--FGSLDEERLERLLDALEELA--------IITH 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-189 |
1.03e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 17 KTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLA---------------------GLDTAVKGTVLcnGEDITKKGLny 75
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvGDDTTALQCVL--NTDIERTQL-- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 76 hRKHNISLVFQNYNL-IDYLTTVENVKLGGSGN---AEKLLEEV-----------------------GIGKEYWQRNVLQ 128
Cdd:PLN03073 266 -LEEEAQLVAQQRELeFETETGKGKGANKDGVDkdaVSQRLEEIykrlelidaytaearaasilaglSFTPEMQVKATKT 344
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 129 LSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAhelgKCVVVVTHSK 189
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP----KTFIVVSHAR 401
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-177 |
1.63e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 26 TFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEDITKKGLNYHRKHnISLVFQNYNlIDYL---------TT 96
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL-VSDEWQRNN-TDMLspgeddtgrTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 97 VENVKLGGSGNA--EKLLEEVGIGKeYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKT 174
Cdd:PRK10938 103 AEIIQDEVKDPArcEQLAQQFGITA-LLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASL 181
|
...
gi 489527143 175 AHE 177
Cdd:PRK10938 182 HQS 184
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
110-201 |
2.52e-04 |
|
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: 40.68 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 110 KLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALA--SDAHVL-LADEPTGNLDETTADEIIALLKKTAhELGKCVVVVT 186
Cdd:cd03271 151 QTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSkrSTGKTLyILDEPTTGLHFHDVKKLLEVLQRLV-DKGNTVVVIE 229
|
90
....*....|....*
gi 489527143 187 HSKHLAEEADEILEI 201
Cdd:cd03271 230 HNLDVIKCADWIIDL 244
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
110-201 |
2.72e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 110 KLLEEVGIGKEYWQRNVLQLSGGQQQRVAIARALASDA-----HVLlaDEPTGNLDetTADeiIALLKKTAHEL---GKC 181
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRStgrtlYIL--DEPTTGLH--FDD--IKKLLEVLQRLvdkGNT 884
|
90 100
....*....|....*....|
gi 489527143 182 VVVVTHSKHLAEEADEILEI 201
Cdd:TIGR00630 885 VVVIEHNLDVIKTADYIIDL 904
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
124-201 |
3.41e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 124 RNVLQLSGGQQQRVAIARALASDA-----HVLlaDEPTGNLDETTADEIIALLKKTAHElGKCVVVVTHSKHLAEEADEI 198
Cdd:PRK00635 805 RPLSSLSGGEIQRLKLAYELLAPSkkptlYVL--DEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVVKVADYV 881
|
...
gi 489527143 199 LEI 201
Cdd:PRK00635 882 LEL 884
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
7-176 |
3.88e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 7 VSYAYKTKKdkTILNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAG-LDTA--VKGTVLCNG----EDITKKGLNYHRKH 79
Cdd:PLN03140 170 INLAKKTKL--TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDPSlkVSGEITYNGyrlnEFVPRKTSAYISQN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 80 NISL-----------------VFQNYNLIDYLTTVEN-------------VKLGGSGNAE---------KLL-----EEV 115
Cdd:PLN03140 248 DVHVgvmtvketldfsarcqgVGTRYDLLSELARREKdagifpeaevdlfMKATAMEGVKsslitdytlKILgldicKDT 327
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489527143 116 GIGKEYwQRNVlqlSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAH 176
Cdd:PLN03140 328 IVGDEM-IRGI---SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVH 384
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
129-202 |
6.89e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 129 LSGGQQQ------RVAIARALASDAHVLLADEPTGNLDE---TTADEIIALLKKTAHELGKcVVVVTHSKHLAEEADEIL 199
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEdrrTNLKDIIEYSLKDSSDIPQ-VIMISHHRELLSVADVAY 880
|
...
gi 489527143 200 EIK 202
Cdd:PRK01156 881 EVK 883
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
108-206 |
7.10e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 39.72 E-value: 7.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 108 AEKLLEEVGIgKEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNLDETTADEIIALLKKTAHElGKCVVVVTH 187
Cdd:NF000106 125 ADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQ 202
|
90 100
....*....|....*....|
gi 489527143 188 SKHLAEE-ADEILEIKNGAI 206
Cdd:NF000106 203 YMEEAEQlAHELTVIDRGRV 222
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
35-60 |
4.77e-03 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 35.93 E-value: 4.77e-03
10 20
....*....|....*....|....*.
gi 489527143 35 IVGPSGAGKTTLLSLLAGLDTAVKGT 60
Cdd:COG4917 6 LIGRSGAGKTTLTQALNGEELEYRKT 31
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-188 |
8.46e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 36.33 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 14 KKDKTI--LNNVSATFEEGIFYTIVGPSGAGKTTLLSLLAGLDTAVKGTVLCNGEditkkglnyhrkhnISLVFQNYNLI 91
Cdd:PRK13546 32 HKNKTFfaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489527143 92 DYLTTVENVK-----LGGSGNAEKLL-------EEVGigkEYWQRNVLQLSGGQQQRVAIARALASDAHVLLADEPTGNL 159
Cdd:PRK13546 98 GQLTGIENIEfkmlcMGFKRKEIKAMtpkiiefSELG---EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180
....*....|....*....|....*....
gi 489527143 160 DETTADEIIALLKKTaHELGKCVVVVTHS 188
Cdd:PRK13546 175 DQTFAQKCLDKIYEF-KEQNKTIFFVSHN 202
|
|
| |
