|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-219 |
2.69e-117 |
|
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: 332.72 E-value: 2.69e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 1 MLRLQFHKKLPFHDLNIDYTFEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYL 80
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 81 FQNLALFPNMNVYENIAFGLKVKkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLL 160
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLKRK-----RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 161 DEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLEKRK 219
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
16-216 |
4.81e-65 |
|
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: 200.05 E-value: 4.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWddsnisLHLPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:cd03259 18 DLSLTVEPgEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV------TGVPPERRNIGMVFQDYALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKKkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:cd03259 92 NIAFGLKLRGVP---KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 175 CMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:cd03259 169 LREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-216 |
7.40e-64 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 201.53 E-value: 7.40e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 5 QFHKKLPFHDLNIDYTFEKP---VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDdsnisLHLPVTERKVGYLF 81
Cdd:COG1118 7 NISKRFGSFTLLDDVSLEIAsgeLVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-----TNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 82 QNLALFPNMNVYENIAFGLKVKKKKkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLD 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRVRPPS---KAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 162 EPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
27-216 |
2.02e-61 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 195.32 E-value: 2.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDdsnislHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKk 106
Cdd:COG3842 35 ALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT------GLPPEKRNVGMVFQDYALFPHLTVAENVAFGLRMRGV- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDF 186
Cdd:COG3842 108 --PKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQREL 185
|
170 180 190
....*....|....*....|....*....|
gi 489818851 187 HIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:COG3842 186 GITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-214 |
3.71e-61 |
|
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: 194.93 E-value: 3.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 1 MLRLQFHKKLPFHDLNIDYTF-EKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGY 79
Cdd:COG4148 2 MLEVDFRLRRGGFTLDVDFTLpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 80 LFQNLALFPNMNVYENIAFGLKVKKkkkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLL 159
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLYGRKRAP-----RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 160 LDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGR 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
12-216 |
1.72e-58 |
|
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: 184.08 E-value: 1.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 12 FHDLNIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNislhLPVTERKVGYLFQNLALFPNM 90
Cdd:cd03299 13 FKLKNVSLEVERGdYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK--DITN----LPPEKRDISYVPQNYALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:cd03299 87 TVYKNIAYGLKKRKV---DKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 171 TRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
30-216 |
7.48e-58 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 186.05 E-value: 7.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwdDSNislHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKkkkE 109
Cdd:COG3839 36 GPSGCGKSTLLRMIAGLEDPTSGEILIGGR---DVT---DLPPKDRNIAMVFQSYALYPHMTVYENIAFPLKLRKV---P 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 110 QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDeetrlicMKLVGQMA---KDF 186
Cdd:COG3839 107 KAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD-------AKLRVEMRaeiKRL 179
|
170 180 190
....*....|....*....|....*....|....
gi 489818851 187 H----IPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:COG3839 180 HrrlgTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2-216 |
1.05e-56 |
|
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: 183.39 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYL 80
Cdd:TIGR02142 1 LSARFSKRLGDFSLDADFTLPGQgVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 81 FQNLALFPNMNVYENIAFGLKVKKKkkkeqAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLL 160
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRARP-----SERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 161 DEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
28-215 |
3.24e-54 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 176.80 E-value: 3.24e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddSNISLhLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKKk 107
Cdd:NF040840 31 ILGPSGAGKTVLLELIAGIWPPDSGKIYLDG-----KDITN-LPPEKRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVP- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 108 keQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFH 187
Cdd:NF040840 104 --KEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFG 181
|
170 180
....*....|....*....|....*...
gi 489818851 188 IPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:NF040840 182 FTAIHVTHNFEEALSLADRVGIMLNGRL 209
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-216 |
1.78e-52 |
|
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: 168.20 E-value: 1.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 6 FHKKLPFHDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnislhLPVTERKVGYLFQNLA 85
Cdd:cd03301 10 FGNVTALDDLNLDIA-DGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD------LPPKDRDIAMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 86 LFPNMNVYENIAFGLKVKKKKkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFN 165
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRKVP---KDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489818851 166 GLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
16-215 |
3.40e-52 |
|
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: 167.67 E-value: 3.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISlHLPVTER------KVGYLFQNLALFP 88
Cdd:cd03255 22 GVSLSIEKgEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGT-----DIS-KLSEKELaafrrrHIGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 89 NMNVYENIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:cd03255 96 DLTALENVELPLLLAGV---PKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 169 EETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTeEILVMREGRL 215
Cdd:cd03255 173 SETGKEVMELLRELNKEAGTTIVVVTHDPELAEYAD-RIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-214 |
2.13e-51 |
|
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: 164.28 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 6 FHKKLPFHDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhlPVTERKVGYLFQNLA 85
Cdd:cd03229 10 YGQKTVLNDVSLNIE-AGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL--PPLRRRIGMVFQDFA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 86 LFPNMNVYENIAFGLkvkkkkkkeqaeiqqqvrkmsdylqishllyssvqklSGGEKQRVAMARAMITEPKLLLLDEPFN 165
Cdd:cd03229 87 LFPHLTVLENIALGL-------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489818851 166 GLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
26-217 |
1.10e-50 |
|
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: 164.43 E-value: 1.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSnislHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVK-K 104
Cdd:cd03296 31 VALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DAT----DVPVQERNVGFVFQHYALFRHMTVFDNVAFGLRVKpR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAK 184
Cdd:cd03296 105 SERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHD 184
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 185 DFHIPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:cd03296 185 ELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQ 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
27-216 |
1.71e-50 |
|
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: 163.56 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsniSLHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKk 106
Cdd:cd03300 30 TLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD------ITNLPPHKRPVNTVFQNYALFPHLTVFENIAFGLRLKKL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR---LICMKlvgQMA 183
Cdd:cd03300 103 --PKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRkdmQLELK---RLQ 177
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 184 KDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:cd03300 178 KELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
16-215 |
5.24e-50 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 162.50 E-value: 5.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvteRKVGYLFQN--LALFpNMNV 92
Cdd:COG1122 19 DVSLSIEKgEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR----RKVGLVFQNpdDQLF-APTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:COG1122 94 EEDVAFGPENLGL---PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 173 LICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1122 171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
16-217 |
1.84e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.28 E-value: 1.84e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISlHLPVTER------KVGYLFQNLALFP 88
Cdd:COG1136 26 GVSLSIEAGeFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQ-----DIS-SLSERELarlrrrHIGFVFQFFNLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 89 NMNVYENIAFGLKVKKKKKkeqAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:COG1136 100 ELTALENVALPLLLAGVSR---KERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489818851 169 EETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTeEILVMREGRLEK 217
Cdd:COG1136 177 SKTGEEVLELLRELNRELGTTIVMVTHDPELAARAD-RVIRLRDGRIVS 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
27-217 |
2.89e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 159.09 E-value: 2.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSnislHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVK-KK 105
Cdd:PRK10851 32 ALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVS----RLHARDRKVGFVFQHYALFRHMTVFDNIAFGLTVLpRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 106 KKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKD 185
Cdd:PRK10851 106 ERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEE 185
|
170 180 190
....*....|....*....|....*....|..
gi 489818851 186 FHIPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:PRK10851 186 LKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQ 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
27-218 |
4.38e-47 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 154.55 E-value: 4.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnislhLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKK 106
Cdd:cd03293 34 ALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP---------VTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KkeqAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDF 186
Cdd:cd03293 105 K---AEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRET 181
|
170 180 190
....*....|....*....|....*....|....
gi 489818851 187 HIPVIFVTHYASEAEMMTEEILVM--REGRLEKR 218
Cdd:cd03293 182 GKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
16-214 |
4.04e-46 |
|
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: 151.85 E-value: 4.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvteRKVGYLFQN--LALFpNMNV 92
Cdd:cd03225 19 DISLTIKKgEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNpdDQFF-GPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:cd03225 94 EEEVAFGLENLGL---PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 173 LICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:cd03225 171 RELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
25-215 |
7.57e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.75 E-value: 7.57e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpvteRKVGYLFQNLALFPNMNVYENIAF-----G 99
Cdd:COG1131 28 IFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVR-----RRIGYVPQEPALYPDLTVRENLRFfarlyG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 LkvkkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLV 179
Cdd:COG1131 103 L--------PRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELL 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 180 GQMAKDFHIpVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1131 175 RELAAEGKT-VLLSTHYLEEAERLCDRVAIIDKGRI 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
26-215 |
1.08e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.47 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnislhlpVTE--RKVGYLFQNLALFPNMNVYENIAFGLKVK 103
Cdd:COG1116 40 VALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----------VTGpgPDRGVVFQEPALLPWLTVLDNVALGLELR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 104 KKKKkeqAEIQQQVRkmsDYLQISHLlySSVQK-----LSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKL 178
Cdd:COG1116 109 GVPK---AERRERAR---ELLELVGL--AGFEDayphqLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDE 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 489818851 179 VGQMAKDFHIPVIFVTHYASEAEMMTEEILVM--REGRL 215
Cdd:COG1116 181 LLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRI 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
27-215 |
3.68e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.88 E-value: 3.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnislhLPVTE--RKVGYLFQNLALFPNMnVYENIAFGLKVKk 104
Cdd:COG4619 30 AITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA------MPPPEwrRQVAYVPQEPALWGGT-VRDNLPFPFQLR- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 kkkkEQAEIQQQVRKMSDYLQISH-LLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMA 183
Cdd:COG4619 102 ----ERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYL 177
|
170 180 190
....*....|....*....|....*....|..
gi 489818851 184 KDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG4619 178 AEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
16-215 |
5.03e-43 |
|
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: 144.74 E-value: 5.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISlHLPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:COG1127 23 GVSLDVPRgEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK-ELYELRRRIGMLFQGGALFDSLTVFE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKKKkeQAEIQQQVRkmsDYLQISHL-----LYSSvqKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE 169
Cdd:COG1127 102 NVAFPLREHTDLS--EAEIRELVL---EKLELVGLpgaadKMPS--ELSGGMRKRVALARALALDPEILLYDEPTAGLDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 170 ETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1127 175 ITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
28-216 |
1.42e-42 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 147.40 E-value: 1.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddSNISlHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKKk 107
Cdd:PRK09452 45 LLGPSGCGKTTVLRLIAGFETPDSGRIMLDG-----QDIT-HVPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTP- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 108 keQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLIcMKL-VGQMAKDF 186
Cdd:PRK09452 118 --AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQ-MQNeLKALQRKL 194
|
170 180 190
....*....|....*....|....*....|
gi 489818851 187 HIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:PRK09452 195 GITFVFVTHDQEEALTMSDRIVVMRDGRIE 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-214 |
3.21e-42 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.59 E-value: 3.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 1 MLRLqfhKKLPFH----DLNIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNIsLHLPVTER 75
Cdd:COG3840 1 MLRL---DDLTYRygdfPLRFDLTIAAgERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-----DL-TALPPAER 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 76 KVGYLFQNLALFPNMNVYENIAFGLKVKKKKKKEQaeiQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEP 155
Cdd:COG3840 72 PVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 156 KLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:COG3840 149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
28-217 |
4.26e-42 |
|
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: 144.94 E-value: 4.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLHLpvteRKVGYLFQNLALFPNMNVYENIAFGLkvkKKKK 107
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE--DVTNVPPHL----RHINMVFQSYALFPHMTVEENVAFGL---KMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 108 KEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFH 187
Cdd:TIGR01187 72 VPRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180 190
....*....|....*....|....*....|
gi 489818851 188 IPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQ 181
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
25-201 |
4.82e-42 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 141.47 E-value: 4.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSID---GGIIEFDGTPWDdsnislHLPVTERKVGYLFQNLALFPNMNVYENIAFGLK 101
Cdd:COG4136 29 ILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLT------ALPAEQRRIGILFQDDLLFPHLSVGENLAFALP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKKKEQAEIQQqvrkMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:COG4136 103 PTIGRAQRRARVEQ----ALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFE 178
|
170 180
....*....|....*....|
gi 489818851 182 MAKDFHIPVIFVTHYASEAE 201
Cdd:COG4136 179 QIRQRGIPALLVTHDEEDAP 198
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
16-215 |
2.14e-41 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 138.30 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpvteRKVGYLFQNLALFPNMNVYE 94
Cdd:cd03230 18 DISLTVEKGeIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-----RRIGYLPEEPSLYENLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIafglkvkkkkkkeqaeiqqqvrkmsdylqishllyssvqKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:cd03230 93 NL---------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRRE 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 175 CMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03230 134 FWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-215 |
1.42e-40 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 138.45 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 1 MLRLQ-----FHKKLPFHDLNidYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhlpvtE 74
Cdd:COG4555 1 MIEVEnlskkYGKVPALKDVS--FTAKDGeITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 75 RKVGYLFQNLALFPNMNVYENIAFglkVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITE 154
Cdd:COG4555 74 RQIGVLPDERGLYDRLTVRENIRY---FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489818851 155 PKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIpVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKT-VLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
30-215 |
2.17e-40 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 141.32 E-value: 2.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnislhLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKkkkE 109
Cdd:PRK11000 36 GPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND------VPPAERGVGMVFQSYALYPHLSVAENMSFGLKLAGA---K 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 110 QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRlICMKL-VGQMAKDFHI 188
Cdd:PRK11000 107 KEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR-VQMRIeISRLHKRLGR 185
|
170 180
....*....|....*....|....*..
gi 489818851 189 PVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK11000 186 TMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-214 |
3.47e-40 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 140.39 E-value: 3.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 1 MLRLQFHKKLPFHDLNIDYTF-EKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGY 79
Cdd:PRK11144 1 MLELNFKQQLGDLCLTVNLTLpAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 80 LFQNLALFPNMNVYENIAFGLKvkkkkkkeqAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLL 159
Cdd:PRK11144 81 VFQDARLFPHYKVRGNLRYGMA---------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 160 LDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK11144 152 MDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGK 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
16-165 |
3.50e-40 |
|
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: 134.70 E-value: 3.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNIslhlPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:pfam00005 3 NVSLTLNPgEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER----KSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 95 NIAFGLKVKKKKkkeQAEIQQQVRKMSDYLQISHLLYSSVQK----LSGGEKQRVAMARAMITEPKLLLLDEPFN 165
Cdd:pfam00005 79 NLRLGLLLKGLS---KREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
30-215 |
4.82e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.02 E-value: 4.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISL----HLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKK 105
Cdd:COG2884 35 GPSGAGKSTLLKLLYGEERPTSGQVLVNGQ-----DLSRlkrrEIPYLRRRIGVVFQDFRLLPDRTVYENVALPLRVTGK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 106 kkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVgqmaKD 185
Cdd:COG2884 110 ---SRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELL----EE 182
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 186 FH---IPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG2884 183 INrrgTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
16-215 |
5.84e-39 |
|
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: 140.42 E-value: 5.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDdsnislHLPVTE-----RKVGYLFQN--LALF 87
Cdd:COG1123 283 DVSLTLRRGeTLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLT------KLSRRSlrelrRRVQMVFQDpySSLN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 88 PNMNVYENIAFGLKVKKKKKkeQAEIQQQVRKMSDYLQIS-HLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNG 166
Cdd:COG1123 357 PRMTVGDIIAEPLRLHGLLS--RAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSA 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489818851 167 LDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1123 435 LDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
16-216 |
8.77e-39 |
|
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: 133.78 E-value: 8.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsNISLHLPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:cd03261 18 GVDLDVRRgEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISG-LSEAELYRLRRRMGMLFQSGALFDSLTVFE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKKKKEqaEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:cd03261 97 NVAFPLREHTRLSEE--EIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 175 CMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:cd03261 175 IDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIV 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-215 |
1.18e-38 |
|
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: 134.02 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIdyTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISlHLPVTE--RKVG 78
Cdd:COG1120 7 LSVGYGGRPVLDDVSL--SLPPGeVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD-----LA-SLSRRElaRRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 79 YLFQNLALFPNMNVYENIAFGLK-VKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKL 157
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALGRYpHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489818851 158 LLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRI 216
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2-214 |
3.22e-38 |
|
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: 129.67 E-value: 3.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIdyTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvteRKVGYL 80
Cdd:cd00267 5 LSFRYGGRTALDNVSL--TLKAgEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 81 FQnlalfpnmnvyeniafglkvkkkkkkeqaeiqqqvrkmsdylqishllyssvqkLSGGEKQRVAMARAMITEPKLLLL 160
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489818851 161 DEPFNGLDEETRLICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-215 |
7.84e-38 |
|
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: 132.38 E-value: 7.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 29 MGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKKKK 108
Cdd:cd03294 56 MGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRA 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 109 EQAEIQQQVRKMSDYLQISHllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHI 188
Cdd:cd03294 136 EREERAAEALELVGLEGWEH---KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQK 212
|
170 180
....*....|....*....|....*..
gi 489818851 189 PVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03294 213 TIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
16-215 |
2.11e-37 |
|
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: 129.57 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvTERKVGYLFQNLALFPNMNVYE 94
Cdd:cd03262 18 GIDLTVKKgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINE--LRQKVGMVFQQFNLFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKKKKEQAEiqqqvRKMSDYLQ---ISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET 171
Cdd:cd03262 96 NITLAPIKVKGMSKAEAE-----ERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPEL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489818851 172 RLICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03262 171 VGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
16-215 |
2.11e-37 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.56 E-value: 2.11e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGT-PWDDSNISLHLpvTERKVGYLFQNLALFPNMNVY 93
Cdd:COG3638 21 DVSLEIERGeFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdVTALRGRALRR--LRRRIGMIFQQFNLVPRLSVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENI-------------AFGLKVkkkkkkeQAEIQQqVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLL 160
Cdd:COG3638 99 TNVlagrlgrtstwrsLLGLFP-------PEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 161 DEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG3638 171 DEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
30-218 |
4.82e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 129.98 E-value: 4.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnisLHLPVTERKVgyLFQNLALFPNMNVYENIAFGLKVKKKkkkE 109
Cdd:COG4525 40 GASGCGKTTLLNLIAGFLAPSSGEITLDGVP-------VTGPGADRGV--VFQKDALLPWLNVLDNVAFGLRLRGV---P 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 110 QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIP 189
Cdd:COG4525 108 KAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKG 187
|
170 180 190
....*....|....*....|....*....|.
gi 489818851 190 VIFVTHYASEAEMMTEEILVM--REGRLEKR 218
Cdd:COG4525 188 VFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-202 |
5.43e-37 |
|
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: 128.12 E-value: 5.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 5 QFHKKLPFHDLNIdyTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQN 83
Cdd:TIGR03608 7 KFGDKVILDDLNL--TIEKgKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 84 LALFPNMNVYENIAFGLKVKKKKKKEQAEIQQQVRKMsdyLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEP 163
Cdd:TIGR03608 85 FALIENETVEENLDLGLKYKKLSKKEKREKKKEALEK---VGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEP 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 489818851 164 FNGLDEETRLICMKLVGQMAKDFHIpVIFVTHYASEAEM 202
Cdd:TIGR03608 162 TGSLDPKNRDEVLDLLLELNDEGKT-IIIVTHDPEVAKQ 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-215 |
6.56e-37 |
|
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: 128.38 E-value: 6.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 10 LPFHdlnIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDdsnislHLPVTERKVGYLFQNLALFP 88
Cdd:cd03298 13 QPMH---FDLTFAQgEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT------AAPPADRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 89 NMNVYENIAFGLKVKKKKKKEQaeiQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:cd03298 84 HLTVEQNVGLGLSPGLKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 169 EETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03298 161 PALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
25-215 |
2.34e-36 |
|
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: 133.10 E-value: 2.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDG---GIIEFDGTPWDDSNISLHLpvteRKVGYLFQN--LALFPnMNVYENIAFG 99
Cdd:COG1123 34 TVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRG----RRIGMVFQDpmTQLNP-VTVGDQIAEA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 LKVKKKKkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLV 179
Cdd:COG1123 109 LENLGLS---RAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 180 GQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1123 186 RELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
25-215 |
5.04e-36 |
|
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: 126.47 E-value: 5.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhLPVTERKVGYLFQN--LALFPNMNVYENIAFGLKV 102
Cdd:cd03257 33 TLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRL-RKIRRKEIQMVFQDpmSSLNPRMTIGEQIAEPLRI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 KKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:cd03257 112 HGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKL 191
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 183 AKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03257 192 QEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
25-214 |
7.74e-36 |
|
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: 126.14 E-value: 7.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLH-LPVTERKVGYLFQNLALFPNMNVYENIAFG---- 99
Cdd:cd03256 29 FVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGT--DINKLKGKaLRQLRRQIGMIFQQFNLIERLSVLENVLSGrlgr 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 --LKVKKKKKKEQAEIQQqVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMK 177
Cdd:cd03256 107 rsTWRSLFGLFPKEEKQR-ALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMD 185
|
170 180 190
....*....|....*....|....*....|....*..
gi 489818851 178 LVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:cd03256 186 LLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-214 |
1.03e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 125.88 E-value: 1.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 1 MLRLQ-FHKKlpFHDL----NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvTE 74
Cdd:COG1126 1 MIEIEnLHKS--FGDLevlkGISLDVEKgEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINK--LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 75 RKVGYLFQNLALFPNMNVYENIAFGLKVKKKKKKEQAEiqQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITE 154
Cdd:COG1126 77 RKVGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAE--ERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 155 PKLLLLDEPFNGLDEEtrlicmkLVG-------QMAKDfHIPVIFVTHyaseaEM-----MTEEILVMREGR 214
Cdd:COG1126 155 PKVMLFDEPTSALDPE-------LVGevldvmrDLAKE-GMTMVVVTH-----EMgfareVADRVVFMDGGR 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-216 |
2.57e-35 |
|
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: 125.30 E-value: 2.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnisLHLPVTE---RKVGYLFQN--LALFPNMNVYENIAFGLK 101
Cdd:COG1124 35 GLVGESGSGKSTLLRALAGLERPWSGEVTFDGRP-------VTRRRRKafrRRVQMVFQDpyASLHPRHTVDRILAEPLR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKkkkeqAEIQQQVRKMSDYLQI-SHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVG 180
Cdd:COG1124 108 IHGL-----PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLK 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 181 QMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:COG1124 183 DLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-216 |
2.67e-35 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 127.65 E-value: 2.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnislhLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKkk 107
Cdd:PRK11650 35 LVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE------LEPADRDIAMVFQNYALYPHMSVRENMAYGLKIRGM-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 108 kEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEetrlicmKLVGQM---AK 184
Cdd:PRK11650 107 -PKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA-------KLRVQMrleIQ 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 185 DFH----IPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:PRK11650 179 RLHrrlkTTSLYVTHDQVEAMTLADRVVVMNGGVAE 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
16-218 |
3.87e-35 |
|
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: 124.23 E-value: 3.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISL----HLPVTERKVGYLFQNLALFPNM 90
Cdd:cd03258 23 DVSLSVPKgEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGT-----DLTLlsgkELRKARRRIGMIFQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:cd03258 98 TVFENVALPLEIAGV---PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489818851 171 TRLICMKLVGQMAKDFHIPVIFVTHyaseaEM-----MTEEILVMREGRLEKR 218
Cdd:cd03258 175 TTQSILALLRDINRELGLTIVLITH-----EMevvkrICDRVAVMEKGEVVEE 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-215 |
5.86e-35 |
|
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: 123.44 E-value: 5.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYtFEKPVTAMMGASGSGKSTLFQCVSGLKSI-----DGGIIEFDGTP-WDDSNISLHLPvteR 75
Cdd:cd03260 6 LNVYYGDKHALKDISLDI-PKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDiYDLDVDVLELR---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 76 KVGYLFQNLALFPnMNVYENIAFGLKVKKKKKKEQ-AEIQQQV-------RKMSDYLQISHLlyssvqklSGGEKQRVAM 147
Cdd:cd03260 82 RVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEElDERVEEAlrkaalwDEVKDRLHALGL--------SGGQQQRLCL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489818851 148 ARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDfhIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
16-215 |
1.20e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 125.99 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP--VTaMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISlhlpvtERKVGYLFQNLALFPNMNVY 93
Cdd:PRK11432 24 NLNLTIKQGtmVT-LLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ------QRDICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGLKVKKKKkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRL 173
Cdd:PRK11432 97 ENVGYGLKMLGVP---KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 174 ICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK11432 174 SMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKI 215
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-215 |
5.02e-34 |
|
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: 121.39 E-value: 5.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLHLpVTERKVGYLFQNLALFPNMNVYENIAFGL---- 100
Cdd:cd03219 28 IHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE--DITGLPPHE-IARLGIGRTFQIPRLFPELTVLENVMVAAqart 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 101 ---KVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL-DEETRLIcM 176
Cdd:cd03219 105 gsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEEL-A 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 177 KLVGQMaKDFHIPVIFVTH-------YAseaemmtEEILVMREGRL 215
Cdd:cd03219 184 ELIREL-RERGITVLLVEHdmdvvmsLA-------DRVTVLDQGRV 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-201 |
5.27e-34 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 120.66 E-value: 5.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLniDYTFEkP--VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpvteRKVGY 79
Cdd:COG4133 8 LSCRRGERLLFSGL--SFTLA-AgeALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-----RRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 80 LFQNLALFPNMNVYENIAFgLKVKKKKKKEQAEIQQQVrkmsDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLL 159
Cdd:COG4133 80 LGHADGLKPELTVRENLRF-WAALYGLRADREAIDEAL----EAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 160 LDEPFNGLDEETRLICMKLVGQMAKDFHIpVIFVTHYASEAE 201
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELA 195
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
16-214 |
6.43e-34 |
|
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: 119.02 E-value: 6.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNI-SLHlpvteRKVGYLFQNLALFpNMNVY 93
Cdd:cd03228 20 DVSLTIKPGeKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLeSLR-----KNIAYVPQDPFLF-SGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIafglkvkkkkkkeqaeiqqqvrkmsdylqishllyssvqkLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRL 173
Cdd:cd03228 94 ENI----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 174 ICMKLVGQMAKDfhIPVIFVTHYASEAEMMtEEILVMREGR 214
Cdd:cd03228 134 LILEALRALAKG--KTVIVIAHRLSTIRDA-DRIIVLDDGR 171
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
16-215 |
6.57e-34 |
|
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: 121.25 E-value: 6.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLH-LPVTERKVGYLFQNLALFPNMNVY 93
Cdd:TIGR02315 20 NINLNINPgEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGT--DITKLRGKkLRKLRRRIGMIFQHYNLIERLTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENI---AFGLKVKKKKKKEQAEIQQQVRKMS--DYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:TIGR02315 98 ENVlhgRLGYKPTWRSLLGRFSEEDKERALSalERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 169 EETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:TIGR02315 178 PKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-215 |
1.80e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.20 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 14 DLNIDytfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvTERKVGYLFQNLALFPNMNVY 93
Cdd:PRK09493 21 DLNID---QGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL--IRQEAGMVFQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGLKVKKKKKKEQAEiqQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRL 173
Cdd:PRK09493 96 ENVMFGPLRVRGASKEEAE--KQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRH 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 174 ICMKLVGQMAKDFHIPVIfVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK09493 174 EVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRI 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
27-214 |
1.95e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 123.41 E-value: 1.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSnislHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKK 106
Cdd:PRK11607 49 ALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLS----HVPPYQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDF 186
Cdd:PRK11607 123 ---KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERV 199
|
170 180
....*....|....*....|....*...
gi 489818851 187 HIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK11607 200 GVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2-215 |
2.77e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 117.92 E-value: 2.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIdyTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISlHLPVTE--RKVG 78
Cdd:cd03214 5 LSVGYGGRTVLDDLSL--SIEAGeIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKD-----LA-SLSPKElaRKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 79 YLFQNLALfpnmnvyeniafglkvkkkkkkeqaeiqqqvrkmsdyLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLL 158
Cdd:cd03214 77 YVPQALEL-------------------------------------LGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489818851 159 LLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
25-215 |
5.44e-33 |
|
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: 119.37 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISlHLP---VTERKVGYLFQNLALFPNMNVYENIAFG-- 99
Cdd:COG0411 32 IVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR-----DIT-GLPphrIARLGIARTFQNPRLFPELTVLENVLVAah 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 ----------LKVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL-D 168
Cdd:COG0411 106 arlgrgllaaLLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLnP 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489818851 169 EETRLIcMKLVGQMAKDFHIPVIFVTHyaseaEM-----MTEEILVMREGRL 215
Cdd:COG0411 186 EETEEL-AELIRRLRDERGITILLIEH-----DMdlvmgLADRIVVLDFGRV 231
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
30-214 |
5.48e-33 |
|
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: 118.12 E-value: 5.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnisLH---LPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKk 106
Cdd:TIGR02673 35 GPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNR----LRgrqLPLLRRRIGVVFQDFRLLPDRTVYENVALPLEVRGK- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVgqmaKDF 186
Cdd:TIGR02673 110 --KEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLL----KRL 183
|
170 180 190
....*....|....*....|....*....|.
gi 489818851 187 HI---PVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:TIGR02673 184 NKrgtTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
16-195 |
1.12e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.27 E-value: 1.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNislhlpvteRKVGYLFQNLAL---FPnMN 91
Cdd:COG1121 24 DVSLTIPPGeFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR---------RRIGYVPQRAEVdwdFP-IT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 92 VYENIAFGLKVKK-KKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:COG1121 94 VRDVVLMGRYGRRgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180
....*....|....*....|....*
gi 489818851 171 TRLICMKLVGQMAKDfHIPVIFVTH 195
Cdd:COG1121 174 TEEALYELLRELRRE-GKTILVVTH 197
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
7-215 |
4.81e-32 |
|
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: 115.73 E-value: 4.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 7 HKKLPFH-DLNIDytfEKPVTAMMGASGSGKSTLFQCVSGLksidggIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLA 85
Cdd:TIGR01277 10 YEHLPMEfDLNVA---DGEIVAIMGPSGAGKSTLLNLIAGF------IEPASGSIKVNDQSHTGLAPYQRPVSMLFQENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 86 LFPNMNVYENIAFGLKVKKKKKKEQaeiQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFN 165
Cdd:TIGR01277 81 LFAHLTVRQNIGLGLHPGLKLNAEQ---QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489818851 166 GLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
16-216 |
5.03e-32 |
|
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: 116.63 E-value: 5.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTP---WDdsnislhlPVT-ERKVGYLFQNLALFPNM 90
Cdd:cd03295 19 NLNLEIAKgEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDireQD--------PVElRRKIGYVIQQIGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENIAfglKVKKKKKKEQAEIQQQVR---KMSDyLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:cd03295 91 TVEENIA---LVPKLLKWPKEKIRERADellALVG-LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489818851 168 DEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:cd03295 167 DPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-215 |
1.93e-31 |
|
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: 120.71 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnisLHLPVTERKVGYLFQNLALFpNMNVYENIAFGLKVKK 104
Cdd:COG2274 503 RVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQ----IDPASLRRQIGVVLQDVFLF-SGTIRENITLGDPDAT 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKK----KEQAEIQQQVRKMSDYLQisHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVG 180
Cdd:COG2274 578 DEEiieaARLAGLHDFIEALPMGYD--TVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLR 655
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 181 QMAKDfhIPVIFVTHYASEAEmMTEEILVMREGRL 215
Cdd:COG2274 656 RLLKG--RTVIIIAHRLSTIR-LADRIIVLDKGRI 687
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
27-213 |
3.12e-31 |
|
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: 114.10 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGL-KSIDGGIIeFDGTPWDDsnislhlPVTERKVgyLFQNLALFPNMNVYENIAFGLKVKKK 105
Cdd:TIGR01184 15 SLIGHSGCGKSTLLNLISGLaQPTSGGVI-LEGKQITE-------PGPDRMV--VFQNYSLLPWLTVRENIALAVDRVLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 106 KKKEqAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKD 185
Cdd:TIGR01184 85 DLSK-SERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEE 163
|
170 180
....*....|....*....|....*...
gi 489818851 186 FHIPVIFVTHYASEAEMMTEEILVMREG 213
Cdd:TIGR01184 164 HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-217 |
9.08e-31 |
|
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: 114.09 E-value: 9.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDG-TPWDDSNISLHlPVtERKVGYLFQnlalFPNM--- 90
Cdd:TIGR04521 23 DVSLTIEDgEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGrDITAKKKKKLK-DL-RKKVGLVFQ----FPEHqlf 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 --NVYENIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISH-LLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:TIGR04521 97 eeTVYKDIAFGPKNLGL---SEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489818851 168 DEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVL 223
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
16-215 |
1.16e-30 |
|
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: 111.90 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpvteRKVGYLFQNLALFPNMNVYEN 95
Cdd:cd03264 18 GVSLTLGPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-----RRIGYLPQEFGVYPNFTVREF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 96 IAFglkVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLIC 175
Cdd:cd03264 93 LDY---IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRF 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489818851 176 MKLVGQMAKDfHIpVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03264 170 RNLLSELGED-RI-VILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-218 |
4.97e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 111.72 E-value: 4.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 29 MGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnislhlPVTERkvGYLFQNLALFPNMNVYENIAFGLKVKKKKKK 108
Cdd:PRK11248 33 LGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-------PGAER--GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 109 EQAEIQQQVRKMSDYLQISHllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHI 188
Cdd:PRK11248 104 QRLEIAHQMLKKVGLEGAEK---RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGK 180
|
170 180 190
....*....|....*....|....*....|..
gi 489818851 189 PVIFVTHYASEAEMMTEEILVMR--EGRLEKR 218
Cdd:PRK11248 181 QVLLITHDIEEAVFMATELVLLSpgPGRVVER 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2-195 |
8.87e-30 |
|
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: 109.93 E-value: 8.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIdyTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNislhlpvteRKVGYL 80
Cdd:cd03235 5 LTVSYGGHPVLEDVSF--EVKPGeFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKER---------KRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 81 FQNLAL---FPnMNVYENIAFGLKVKKKKKK----EQAEIQQQVRKMsdyLQISHLLYSSVQKLSGGEKQRVAMARAMIT 153
Cdd:cd03235 74 PQRRSIdrdFP-ISVRDVVLMGLYGHKGLFRrlskADKAKVDEALER---VGLSELADRQIGELSGGQQQRVLLARALVQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 154 EPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIpVIFVTH 195
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMT-ILVVTH 190
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
25-215 |
1.22e-29 |
|
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: 109.76 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsniSLHLPV-TERKVGYLFQNLALFPNMNVYENIAF----- 98
Cdd:cd03266 33 VTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD------VVKEPAeARRRLGFVSDSTGLYDRLTARENLEYfagly 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 GLkvkkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKL 178
Cdd:cd03266 107 GL--------KGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178
|
170 180 190
....*....|....*....|....*....|....*..
gi 489818851 179 VGQMaKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03266 179 IRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-215 |
1.28e-29 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 109.94 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISlHLPVTERK---VGYLFQNLALFPNMNVYENIafgLK 101
Cdd:cd03218 28 IVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ-----DIT-KLPMHKRArlgIGYLPQEASIFRKLTVEENI---LA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:cd03218 99 VLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
170 180 190
....*....|....*....|....*....|....
gi 489818851 182 MaKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03218 179 L-KDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
13-215 |
2.85e-29 |
|
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: 108.65 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 13 HDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnisLH---LPVTERKVGYLFQNLALFPN 89
Cdd:cd03292 18 DGINISIS-AGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSD----LRgraIPYLRRKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 90 MNVYENIAFGLKVKKKKKKEqaeIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE 169
Cdd:cd03292 93 RNVYENVAFALEVTGVPPRE---IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489818851 170 ETRLICMKLVgqmaKDFH---IPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03292 170 DTTWEIMNLL----KKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
16-215 |
3.86e-29 |
|
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: 108.21 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:TIGR02211 23 GVSLSIGKgEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQFHHLLPDFTALE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKKKKEQAEIQQqvrKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:TIGR02211 103 NVAMPLLIGKKSVKEAKERAY---EMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 175 CMKLVGQMAKDFHIPVIFVTHYASEAEMMtEEILVMREGRL 215
Cdd:TIGR02211 180 IFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQL 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-215 |
5.59e-29 |
|
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: 107.98 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISLHLPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:cd03263 20 DLSLNVYKgEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY-----SIRTDRKAARQSLGYCPQFDALFDELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAF-----GLkvkkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE 169
Cdd:cd03263 95 HLRFyarlkGL--------PKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 170 ET-RLICMKLVGQMAKDfhiPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03263 167 ASrRAIWDLILEVRKGR---SIILTTHSMDEAEALCDRIAIMSDGKL 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-215 |
7.70e-29 |
|
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: 112.93 E-value: 7.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 12 FHDLNIDYTFEKPV-------------TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnisLHLPVTERKVG 78
Cdd:COG4988 339 LEDVSFSYPGGRPAldglsltippgerVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD----LDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 79 YLFQNLALFPnMNVYENIAFGlkvkkKKKKEQAEIQQQVRK--MSDYLQ-----ISHLLYSSVQKLSGGEKQRVAMARAM 151
Cdd:COG4988 415 WVPQNPYLFA-GTIRENLRLG-----RPDASDEELEAALEAagLDEFVAalpdgLDTPLGEGGRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489818851 152 ITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDfHIpVIFVTHYASEAEMMtEEILVMREGRL 215
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG-RT-VILITHRLALLAQA-DRILVLDDGRI 549
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-195 |
2.07e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 105.58 E-value: 2.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 14 DLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhlpvTE--RKVGYLFQNL--ALFpN 89
Cdd:TIGR01166 10 GLNFAAE-RGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGL----LErrQRVGLVFQDPddQLF-A 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 90 MNVYENIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE 169
Cdd:TIGR01166 84 ADVDQDVAFGPLNLGL---SEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180
....*....|....*....|....*..
gi 489818851 170 E-TRLICMKLVGQMAKDFHipVIFVTH 195
Cdd:TIGR01166 161 AgREQMLAILRRLRAEGMT--VVISTH 185
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
27-216 |
2.21e-28 |
|
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: 106.75 E-value: 2.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnisLHlPVTE--------RKVGYLFQNLALFPNMNVYENIAF 98
Cdd:COG4181 42 AIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD-------LF-ALDEdararlraRHVGFVFQSFQLLPTLTALENVML 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 GLkvkkkkkkE---QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLIC 175
Cdd:COG4181 114 PL--------ElagRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 176 MKLVGQMAKDFHIPVIFVTHYASEAEmMTEEILVMREGRLE 216
Cdd:COG4181 186 IDLLFELNRERGTTLVLVTHDPALAA-RCDRVLRLRAGRLV 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
30-215 |
3.04e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 108.63 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISlHLPVTE-----RKVGYLFQNLALFPNMNVYENIAFGLkvkk 104
Cdd:COG1135 38 GYSGAGKSTLIRCINLLERPTSGSVLVDGV-----DLT-ALSERElraarRKIGMIFQHFNLLSSRTVAENVALPL---- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 kkkkEQA-----EIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD-EETRLIcMKL 178
Cdd:COG1135 108 ----EIAgvpkaEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpETTRSI-LDL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 179 VGQMAKDFHIPVIFVTHyaseaEM-----MTEEILVMREGRL 215
Cdd:COG1135 183 LKDINRELGLTIVLITH-----EMdvvrrICDRVAVLENGRI 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
25-215 |
3.34e-28 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 106.59 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISlHLPVTERK---VGYLFQNLALFPNMNVYENIAFGLK 101
Cdd:TIGR04406 29 IVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQ-----DIT-HLPMHERArlgIGYLPQEASIFRKLTVEENIMAVLE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:TIGR04406 103 IRKDL--DRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKH 180
|
170 180 190
....*....|....*....|....*....|....
gi 489818851 182 MaKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:TIGR04406 181 L-KERGIGVLITDHNVRETLDICDRAYIISDGKV 213
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-216 |
6.58e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 105.67 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 18 DYTFEKPVTAMM---GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:PRK11629 27 NVSFSIGEGEMMaivGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:PRK11629 107 NVAMPLLIGKK---KPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 175 CMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEiLVMREGRLE 216
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQ-LEMRDGRLT 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-217 |
1.49e-27 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 105.20 E-value: 1.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpWDDSNISlHLPVTERKVGYLFQNlalfP-----N 89
Cdd:TIGR04520 20 NVSLSIEKGeFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEE-NLWEIRKKVGMVFQN----PdnqfvG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 90 MNVYENIAFGLkvkkkkkkE-----QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPF 164
Cdd:TIGR04520 93 ATVEDDVAFGL--------EnlgvpREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEAT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489818851 165 NGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAeMMTEEILVMREGRLEK 217
Cdd:TIGR04520 165 SMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVA 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
30-168 |
1.73e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.34 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISlHLPVTERK---VGYLFQNLALFPNMNVYENIafgLKVKKKK 106
Cdd:COG1137 36 GPNGAGKTTTFYMIVGLVKPDSGRIFLDGE-----DIT-HLPMHKRArlgIGYLPQEASIFRKLTVEDNI---LAVLELR 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 107 KKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:COG1137 107 KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVD 168
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-215 |
1.79e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.28 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwDDSNISlhlPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKK 106
Cdd:PRK10771 29 AILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHTTT---PPSRRPVSMLFQENNLFSHLTVAQNIGLGLNPGLKL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KKEQaeiQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDF 186
Cdd:PRK10771 103 NAAQ---REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQER 179
|
170 180
....*....|....*....|....*....
gi 489818851 187 HIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10771 180 QLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-214 |
2.08e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhlpVTERK-VGYLFQNL--ALFpNMNVYENIAFGlk 101
Cdd:PRK13636 34 VTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGL---MKLREsVGMVFQDPdnQLF-SASVYQDVSFG-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 vKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:PRK13636 108 -AVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVE 186
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 182 MAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK13636 187 MQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-195 |
3.58e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 103.96 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYtFEKPVTAMMGASGSGKSTLfqcvsgLKS-------IDG----GIIEFDGTpwddsNI-SLH 69
Cdd:COG1117 17 LNVYYGDKQALKDINLDI-PENKVTALIGPSGCGKSTL------LRClnrmndlIPGarveGEILLDGE-----DIyDPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 70 LPVTE--RKVGYLFQNLALFPnMNVYENIAFGLKVKKKKKkeQAEIQQQVRKmsdYLQISHL-------LYSSVQKLSGG 140
Cdd:COG1117 85 VDVVElrRRVGMVFQKPNPFP-KSIYDNVAYGLRLHGIKS--KSELDEIVEE---SLRKAALwdevkdrLKKSALGLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 141 EKQRVAMARAMITEPKLLLLDEPFNGLD-EETRLICmKLVGQMAKDFHIpvIFVTH 195
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDpISTAKIE-ELILELKKDYTI--VIVTH 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-215 |
4.37e-27 |
|
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: 102.68 E-value: 4.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 6 FHKKLPFHDLNID-YTFEkpVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhlpvteRKVGYLFQNL 84
Cdd:cd03268 10 YGKKRVLDDISLHvKKGE--IYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL------RRIGALIEAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 85 ALFPNMNVYENIafgLKVKKKKKKEQAEIQQQVrkmsDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPF 164
Cdd:cd03268 82 GFYPNLTARENL---RLLARLLGIRKKRIDEVL----DVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 165 NGLD----EETRLICMKLvgqmaKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03268 155 NGLDpdgiKELRELILSL-----RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
26-218 |
9.98e-27 |
|
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: 106.77 E-value: 9.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTP---WDDSNISlhlpvteRKVGYLFQNLALFpNMNVYENIAFG--- 99
Cdd:COG4987 364 VAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlrdLDEDDLR-------RRIAVVPQRPHLF-DTTLRENLRLArpd 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 ---------LkvkkkkkkEQAEIQQQVRKMSDYLQisHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:COG4987 436 atdeelwaaL--------ERVGLGDWLAALPDGLD--TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAA 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489818851 171 TRLICMKLVGQMAKDFhiPVIFVTHYASEAEMMtEEILVMREGRLEKR 218
Cdd:COG4987 506 TEQALLADLLEALAGR--TVLLITHRLAGLERM-DRILVLEDGRIVEQ 550
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
26-216 |
1.23e-26 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 103.63 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLfqcvsgLKSI------DGGIIEFDGTpwddsNISlHLPVTE--RKVGYLFQNLALFPNMNVYENIA 97
Cdd:COG1125 31 TVLVGPSGCGKTTT------LRMInrliepTSGRILIDGE-----DIR-DLDPVElrRRIGYVIQQIGLFPHMTVAENIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 F-----GlkvkkkkkKEQAEIQQQVRKMsdyLQISHLLYSSVQK-----LSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:COG1125 99 TvprllG--------WDKERIRARVDEL---LELVGLDPEEYRDrypheLSGGQQQRVGVARALAADPPILLMDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 168 DEETR------LIcmklvgQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:COG1125 168 DPITReqlqdeLL------RLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIV 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
25-167 |
1.30e-26 |
|
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: 101.74 E-value: 1.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLHLpVTERKVGYLFQNLALFPNMNVYENIAFGLkvkk 104
Cdd:cd03224 28 IVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR--DITGLPPHE-RARAGIGYVPEGRRIFPELTVEENLLLGA---- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 105 kKKKEQAEIQQQVRKMSDYLQIshLLYSSVQK---LSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:cd03224 101 -YARRRAKRKARLERVYELFPR--LKERRKQLagtLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
25-215 |
1.82e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.87 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISLHLPV--TERKVGYLFQNLALFPNMNVYENIAFGLKV 102
Cdd:COG1129 32 VHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP-----VRFRSPRdaQAAGIAIIHQELNLVPNLSVAENIFLGREP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 KKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE-ET-RLicMKLVG 180
Cdd:COG1129 107 RRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTErEVeRL--FRIIR 184
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 181 QMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1129 185 RLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
25-215 |
2.68e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 100.32 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKS--IDGGIIEFDGTPWDDSNISlhlpvteRKVGYLFQNLALFPNMNVYENIAFglkv 102
Cdd:cd03213 37 LTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSFR-------KIIGYVPQDDILHPTLTVRETLMF---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 kkkkkkeQAEIQQqvrkmsdylqishllyssvqkLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:cd03213 106 -------AAKLRG---------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL 157
|
170 180 190
....*....|....*....|....*....|....
gi 489818851 183 AKDfHIPVIFVTHYAS-EAEMMTEEILVMREGRL 215
Cdd:cd03213 158 ADT-GRTIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-215 |
2.89e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 2.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDgtpwdDSNISLhLPVTERK---VGYLFQNLALFPNMNVYENIAFGLK 101
Cdd:PRK10895 31 IVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID-----DEDISL-LPLHARArrgIGYLPQEASIFRRLSVYDNLMAVLQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKKKEQAEiqQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDeETRLICMKLVGQ 181
Cdd:PRK10895 105 IRDDLSAEQRE--DRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD-PISVIDIKRIIE 181
|
170 180 190
....*....|....*....|....*....|....
gi 489818851 182 MAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10895 182 HLRDSGLGVLITDHNVRETLAVCERAYIVSQGHL 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
25-214 |
3.95e-26 |
|
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: 100.05 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSnislhlpvTERKVGYLFQNLALFPNMNVYENIAF-----G 99
Cdd:cd03269 28 IFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA--------ARNRIGYLPEERGLYPKMKVIDQLVYlaqlkG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 LKVkkkkkkeqAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLV 179
Cdd:cd03269 100 LKK--------EEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVI 171
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 180 GQMaKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:cd03269 172 REL-ARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
26-214 |
3.28e-25 |
|
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: 98.62 E-value: 3.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGlksidggiiefDGTPWDDSNISL------HLPVTE--RKVGYLFQNLALF--PNMNVYEN 95
Cdd:COG1119 32 WAILGPNGAGKSTLLSLITG-----------DLPPTYGNDVRLfgerrgGEDVWElrKRIGLVSPALQLRfpRDETVLDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 96 IAFGLKVKKKKKKE-QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:COG1119 101 VLSGFFDSIGLYREpTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGAREL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489818851 175 CMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:COG1119 181 LLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
27-216 |
4.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.35 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpVTERKVGYLFQ--NLALFPNmNVYENIAFGLKVKK 104
Cdd:PRK13637 37 GLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLS--DIRKKVGLVFQypEYQLFEE-TIEKDIAFGPINLG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KkkkEQAEIQQQVRKMSDYLQISHLLYS--SVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:PRK13637 114 L---SEEEIENRVKRAMNIVGLDYEDYKdkSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKEL 190
|
170 180 190
....*....|....*....|....*....|....
gi 489818851 183 AKDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:PRK13637 191 HKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-215 |
1.02e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.51 E-value: 1.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFdGTPWDDSNISLH-----LPVTERK 76
Cdd:PRK11264 9 LVKKFHGQTVLHGIDLEVK-PGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARSLSqqkglIRQLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 77 VGYLFQNLALFPNMNVYENIAFGLKVKKKKKKEQAEiqQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPK 156
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEAT--ARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 157 LLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIfVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-215 |
1.14e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.29 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLksidggiIEF------DGTPWDDSNISLHLPVTE- 74
Cdd:PRK14247 9 LKVSFGQVEVLDGVNLEIP-DNTITALMGPSGSGKSTLLRVFNRL-------IELypearvSGEVYLDGQDIFKMDVIEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 75 -RKVGYLFQNLALFPNMNVYENIAFGLKVKKKKKkEQAEIQQQVR----KMSDYLQISHLLYSSVQKLSGGEKQRVAMAR 149
Cdd:PRK14247 81 rRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVK-SKKELQERVRwaleKAQLWDEVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 150 AMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIpvIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-214 |
1.15e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 98.26 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNIslhlpvteRKVGYLFQNLALFPNMNVYENIAF-----G 99
Cdd:COG4152 29 IFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDR--------RRIGYLPEERGLYPKMKVGEQLVYlarlkG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 LkvkkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLV 179
Cdd:COG4152 101 L--------SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVI 172
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 180 GQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:COG4152 173 RELAAK-GTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
27-215 |
1.20e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 97.44 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvterkvgyLFQNLALFPNMNVYENIAFGLkvkkkk 106
Cdd:PRK11247 42 AVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRL---------MFQDARLLPWKKVIDNVGLGL------ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDF 186
Cdd:PRK11247 107 ---KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQH 183
|
170 180
....*....|....*....|....*....
gi 489818851 187 HIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK11247 184 GFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-215 |
1.68e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.15 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYtFEKPVTAMMGASGSGKSTLFQCVSGLKSID-----GGIIEFDG----TPWDDSnislhlpV 72
Cdd:PRK14239 11 LSVYYNKKKALNSVSLDF-YPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGhniySPRTDT-------V 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 73 TERK-VGYLFQNLALFPnMNVYENIAFGLKVKKKKKKE--QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMAR 149
Cdd:PRK14239 83 DLRKeIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQvlDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489818851 150 AMITEPKLLLLDEPFNGLD-------EETRLicmklvgQMAKDFHIpvIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDpisagkiEETLL-------GLKDDYTM--LLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
28-215 |
2.07e-24 |
|
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: 95.86 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVtERKVGYLFQNLALFPNMNVYENIAFGLKVKKKKk 107
Cdd:TIGR02982 36 LTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL-RRRIGYIFQAHNLLGFLTARQNVQMALELQPNL- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 108 kEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFH 187
Cdd:TIGR02982 114 -SYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQG 192
|
170 180
....*....|....*....|....*...
gi 489818851 188 IPVIFVTHyASEAEMMTEEILVMREGRL 215
Cdd:TIGR02982 193 CTILMVTH-DNRILDVADRILQMEDGKL 219
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
30-199 |
2.93e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 2.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISLHLPVTERK-VGYLFQNLALFPNmNVYENIAFglkvkkkkKK 108
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISPTSGTLLFEGED-----ISTLKPEIYRQqVSYCAQTPTLFGD-TVYDNLIF--------PW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 109 EQAEIQQQVRKMSDYLQ----ISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAK 184
Cdd:PRK10247 106 QIRNQQPDPAIFLDDLErfalPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVR 185
|
170
....*....|....*
gi 489818851 185 DFHIPVIFVTHYASE 199
Cdd:PRK10247 186 EQNIAVLWVTHDKDE 200
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
25-215 |
4.58e-24 |
|
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: 95.13 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGiiefdgtpwdDSNISLHLPVTE-----RKVGYLFQNLALFPNMNVYENIA-- 97
Cdd:cd03265 28 IFGLLGPNGAGKTTTIKMLTTLLKPTSG----------RATVAGHDVVREprevrRRIGIVFQDLSVDDELTGWENLYih 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 ---FGLkvkkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:cd03265 98 arlYGV--------PGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 175 CMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03265 170 VWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-215 |
4.65e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 96.24 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 4 LQFHKKLPFHDLNIDytfEKPVTAMMGASGSGKSTLFQCVSGLKSID---GGIIEFDG-TPWDDSNISLHLPVTERKVGY 79
Cdd:PRK09984 14 FNQHQALHAVDLNIH---HGEMVALLGPSGSGKSTLLRHLSGLITGDksaGSHIELLGrTVQREGRLARDIRKSRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 80 LFQNLALFPNMNVYENIAFG------LKVKKKKKKEQAEIQQQVRKMSDyLQISHLLYSSVQKLSGGEKQRVAMARAMIT 153
Cdd:PRK09984 91 IFQQFNLVNRLSVLENVLIGalgstpFWRTCFSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 154 EPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-195 |
5.31e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 5.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 21 FEKPVTAMMGASGSGKSTLFQCVSGLKSIDG-----GIIEFDGTPWDDSNISLHLpvTERKVGYLFQNLALFPnMNVYEN 95
Cdd:PRK14258 31 YQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVNLNR--LRRQVSMVHPKPNLFP-MSVYDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 96 IAFGLKVKK-KKKKEQAEIQQQVRKMSD-YLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRL 173
Cdd:PRK14258 108 VAYGVKIVGwRPKLEIDDIVESALKDADlWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASM 187
|
170 180
....*....|....*....|..
gi 489818851 174 ICMKLVGQMAKDFHIPVIFVTH 195
Cdd:PRK14258 188 KVESLIQSLRLRSELTMVIVSH 209
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-215 |
7.14e-24 |
|
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: 94.99 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 18 DYTFEKP---VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLHlpVTERKVGYLFQNLALFpNMNVYE 94
Cdd:cd03253 19 DVSFTIPagkKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ--DIREVTLD--SLRRAIGVVPQDTVLF-NDTIGY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKKKKE----QAEIQQQVRKMSDYlqishllYSSV-----QKLSGGEKQRVAMARAMITEPKLLLLDEPFN 165
Cdd:cd03253 94 NIRYGRPDATDEEVIeaakAAQIHDKIMRFPDG-------YDTIvgergLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489818851 166 GLDEETRlicMKLVGQMAKDF-HIPVIFVTHYASEAeMMTEEILVMREGRL 215
Cdd:cd03253 167 ALDTHTE---REIQAALRDVSkGRTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-195 |
1.25e-23 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 95.22 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 12 FHDLNIDYTFEKpVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddSNISL----HLPVTERKVGYLFQNLALF 87
Cdd:PRK11831 23 FDNISLTVPRGK-ITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG-----ENIPAmsrsRLYTVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 88 PNMNVYENIAFGLkvkkkkkKEQAEIQQQVRKMSDYLQI--------SHLLYSsvqKLSGGEKQRVAMARAMITEPKLLL 159
Cdd:PRK11831 97 TDMNVFDNVAYPL-------REHTQLPAPLLHSTVMMKLeavglrgaAKLMPS---ELSGGMARRAALARAIALEPDLIM 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 160 LDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTH 195
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSH 202
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
16-215 |
2.24e-23 |
|
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: 91.89 E-value: 2.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTP---WDDSNISLHlpvterkVGYLFQNLALFPNmN 91
Cdd:cd03246 20 NVSFSIEPgESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADisqWDPNELGDH-------VGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 92 VYENIafglkvkkkkkkeqaeiqqqvrkmsdylqishllyssvqkLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET 171
Cdd:cd03246 92 IAENI----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEG 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489818851 172 RLICMKLVGQMAKDFHIpVIFVTHYASEAEMMtEEILVMREGRL 215
Cdd:cd03246 132 ERALNQAIAALKAAGAT-RIVIAHRPETLASA-DRILVLEDGRV 173
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-215 |
2.38e-23 |
|
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: 93.49 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGL---KSIDGGIIEFDGTPwddsnISLHLpvTERKVGYLFQNLALFPNMNVYENIAFGLK 101
Cdd:cd03234 35 VMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQP-----RKPDQ--FQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKKKEQAEIQQQVRKMS-DYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVG 180
Cdd:cd03234 108 LRLPRKSSDAIRKKRVEDVLlRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLS 187
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 181 QMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03234 188 QLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-215 |
2.49e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 94.48 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGL---KSIDGGIIEFDG------TPWDdsnislhlpvTERKVGYLFQNL-ALFPNMNVYEN 95
Cdd:PRK13640 36 TALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGitltakTVWD----------IREKVGIVFQNPdNQFVGATVGDD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 96 IAFGLKVKKKKKKEQAEIQQQVRK---MSDYLQishllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:PRK13640 106 VAFGLENRAVPRPEMIKIVRDVLAdvgMLDYID------SEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 173 LICMKLVGQMAKDFHIPVIFVTHYASEAEmMTEEILVMREGRL 215
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-215 |
5.83e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.00 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNI-SLHlpvteRKVGYLFQNLALFpNMNVYENIAFGlkvk 103
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLeSLR-----RQIGVVPQDTFLF-SGTIRENIRYG---- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 104 kKKKKEQAEIQQQVRKmsdyLQISHLL------YSSV-----QKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET- 171
Cdd:COG1132 438 -RPDATDEEVEEAAKA----AQAHEFIealpdgYDTVvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETe 512
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489818851 172 RLIcMKLVGQMAKDfhIPVIFVTHYASEAEMMtEEILVMREGRL 215
Cdd:COG1132 513 ALI-QEALERLMKG--RTTIVIAHRLSTIRNA-DRILVLDDGRI 552
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
27-195 |
1.11e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 91.76 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLALFPNMNVYENIAFglkVKKKK 106
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNALENVEL---PALLR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDF 186
Cdd:PRK10584 117 GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREH 196
|
....*....
gi 489818851 187 HIPVIFVTH 195
Cdd:PRK10584 197 GTTLILVTH 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-215 |
1.36e-22 |
|
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: 91.63 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDG-TPWDDSNISLhlpvteRKVGYLF-QNLALFPNMNV 92
Cdd:cd03267 39 GISFTIEKgEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKFL------RRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFglkVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:cd03267 113 IDSFYL---LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 173 LICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
2.38e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 91.33 E-value: 2.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYtfeKP--VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnislhLPVTE--RKV 77
Cdd:COG4559 7 LSVRLGGRTLLDDVSLTL---RPgeLTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAA------WSPWElaRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 78 GYLFQNLAL-FPnMNVYENIAFGLKVKKKKKKEQAEIQQQVRKMSDylqISHLLYSSVQKLSGGEKQRVAMARAMI---- 152
Cdd:COG4559 78 AVLPQHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVG---LAHLAGRSYQTLSGGEQQRVQLARVLAqlwe 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489818851 153 ---TEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDfHIPVIFVTH-------YAseaemmtEEILVMREGRL 215
Cdd:COG4559 154 pvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHdlnlaaqYA-------DRILLLHQGRL 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-215 |
2.60e-22 |
|
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: 90.61 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 18 DYTFE-KP--VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDD-SNISLHlpvteRKVGYLFQNLALFPNmNVY 93
Cdd:cd03248 32 DVSFTlHPgeVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLH-----SKVSLVGQEPVLFAR-SLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGLKVKKKKKKEQAeiQQQVRKMSDYLQISHLLYSSV----QKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE 169
Cdd:cd03248 106 DNIAYGLQSCSFECVKEA--AQKAHAHSFISELASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 170 ETRLICMKLVGQMAKDFHIPVIfvTHYASEAEmMTEEILVMREGRL 215
Cdd:cd03248 184 ESEQQVQQALYDWPERRTVLVI--AHRLSTVE-RADQILVLDGGRI 226
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
16-215 |
5.76e-22 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 89.77 E-value: 5.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNIslhlpvteRKVGYLFQNLALFPNMNVYE 94
Cdd:TIGR03740 18 NISLTVPKnSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDL--------HKIGSLIESPPLYENLTARE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIafgLKVKKKKKKEQAEIQQQVRKMSdylqISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD----EE 170
Cdd:TIGR03740 90 NL---KVHTTLLGLPDSRIDEVLNIVD----LTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDpigiQE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489818851 171 TRLICMKLVGQmakdfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:TIGR03740 163 LRELIRSFPEQ-----GITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
30-202 |
6.71e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.79 E-value: 6.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDG---TPWDDSNISLhlpvTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKk 106
Cdd:PRK11153 38 GASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSEKELRK----ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGT- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkEQAEIQQQVRKMSDYLQISHL--LYSSvqKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD-EETRLIcMKLVGQMA 183
Cdd:PRK11153 113 --PKAEIKARVTELLELVGLSDKadRYPA--QLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSI-LELLKDIN 187
|
170
....*....|....*....
gi 489818851 184 KDFHIPVIFVTHyaseaEM 202
Cdd:PRK11153 188 RELGLTIVLITH-----EM 201
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
25-167 |
8.09e-22 |
|
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: 89.27 E-value: 8.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISlHLP---VTERKVGYLFQNLALFPNMNVYENIAFGLK 101
Cdd:COG0410 31 IVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----IT-GLPphrIARLGIGYVPEGRRIFPSLTVEENLLLGAY 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 102 VKKkkkkEQAEIQQQVRKMSDY---LQisHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:COG0410 105 ARR----DRAEVRADLERVYELfprLK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
16-215 |
8.91e-22 |
|
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: 87.48 E-value: 8.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISLHLPVTERKVGylfqnlalfpnmnvye 94
Cdd:cd03216 18 GVSLSVRRgEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE-----VSFASPRDARRAG---------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 nIAFglkvkkkkkkeqaeiqqqvrkmsdylqishllyssVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD--EETR 172
Cdd:cd03216 77 -IAM-----------------------------------VYQLSVGERQMVEIARALARNARLLILDEPTAALTpaEVER 120
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 173 LIcmKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03216 121 LF--KVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
33-215 |
1.11e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.39 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 33 GSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSN--------ISLhlpVTE-RKvgylfqNLALFPNMNVYENIA------ 97
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSprdairagIAY---VPEdRK------GEGLVLDLSIRENITlasldr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 ---FGLKVkkkkkkeQAEIQQQVRKMSDYLQI-SHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRL 173
Cdd:COG1129 359 lsrGGLLD-------RRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKA 431
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 174 ICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1129 432 EIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
30-215 |
2.75e-21 |
|
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: 86.72 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvtERKVGYL---FQNLALFPNMNVYENIAFGLKvkkkk 106
Cdd:cd03215 33 GLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAI---RAGIAYVpedRKREGLVLDLSVAENIALSSL----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkeqaeiqqqvrkmsdylqishllyssvqkLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDf 186
Cdd:cd03215 105 ------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA- 153
|
170 180
....*....|....*....|....*....
gi 489818851 187 HIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:cd03215 154 GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
25-210 |
3.07e-21 |
|
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: 91.19 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvteRKVGYLFQNLALFPNmNVYENIAFGLKVKK 104
Cdd:TIGR02857 350 RVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWR----DQIAWVPQHPFLFAG-TIAENIRLARPDAS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KkkkeqAEIQQQVRK--MSDYLQ-----ISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMK 177
Cdd:TIGR02857 425 D-----AEIREALERagLDEFVAalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLE 499
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 178 LVGQMAKDfHIpVIFVTHYASEAEMMtEEILVM 210
Cdd:TIGR02857 500 ALRALAQG-RT-VLLVTHRLALAALA-DRIVVL 529
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
16-215 |
4.16e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.51 E-value: 4.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhlpvTERKVGYLFQNL-ALFPNMNVY 93
Cdd:PRK13632 27 NVSFEINEgEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE----IRKKIGIIFQNPdNQFIGATVE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGLKVKKKKKKEQAEIqqqVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRL 173
Cdd:PRK13632 103 DDIAFGLENKKVPPKKMKDI---IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 174 ICMKLVGQMAKDFHIPVIFVTHYASEAeMMTEEILVMREGRL 215
Cdd:PRK13632 180 EIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKL 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
27-215 |
4.29e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 88.32 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISlhlpVTERKVGYLFQNlalfPNMNVY-----ENIAFGlk 101
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR----EVRKFVGLVFQN----PDDQIFsptveQDIAFG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 vKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:PRK13652 104 -PINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLND 182
|
170 180 190
....*....|....*....|....*....|....
gi 489818851 182 MAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK13652 183 LPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-214 |
4.46e-21 |
|
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: 90.51 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLksID-GGIIEFDGTPWDDSNISLHLPVtERKVGYLFQN--LALFPNMNVYENIAFGLKVKKKK 106
Cdd:COG4172 319 GESGSGKSTLGLALLRL--IPsEGEIRFDGQDLDGLSRRALRPL-RRRMQVVFQDpfGSLSPRMTVGQIIAEGLRVHGPG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KKEqAEIQQQVRKMsdyLQISHLLYSSVQK----LSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:COG4172 396 LSA-AERRARVAEA---LEEVGLDPAARHRypheFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL 471
|
170 180 190
....*....|....*....|....*....|..
gi 489818851 183 AKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:COG4172 472 QREHGLAYLFISHDLAVVRALAHRVMVMKDGK 503
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-215 |
4.61e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 4.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSI-------DGGIIEFDGTPWDDSNISLhlpvtERKVGYLFQNLALFPNMNVYENIA 97
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEIydskikvDGKVLYFGKDIFQIDAIKL-----RKEVGMVFQQPNPFPHLSIYDNIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 FGLKVKKKKKKEQAE--IQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLIC 175
Cdd:PRK14246 113 YPLKSHGIKEKREIKkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489818851 176 MKLVGQMAKDfhIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK14246 193 EKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-218 |
4.68e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.54 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQnlalFPNMNVYE-----NIAFGl 100
Cdd:PRK13634 36 VAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQ----FPEHQLFEetvekDICFG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 101 kvKKKKKKEQAEIQQQVRKMSDYLQISH-LLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLV 179
Cdd:PRK13634 111 --PMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMF 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 489818851 180 GQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLEKR 218
Cdd:PRK13634 189 YKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQ 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-215 |
4.70e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.90 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYtfeKP--VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTP---WDDSNISLHLPVterk 76
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTL---RPgeVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPladWSPAELARRRAV---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 77 vgyLFQNLAL-FPnMNVYENIAFGLKVKKKKKKEQAEIQQQVRKMSDylqISHLLYSSVQKLSGGEKQRVAMARAMI--- 152
Cdd:PRK13548 81 ---LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVD---LAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 153 ---TEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-220 |
6.09e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 88.35 E-value: 6.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 22 EKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQnlalFPNMNVYEN-----I 96
Cdd:PRK13641 32 EGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQ----FPEAQLFENtvlkdV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 97 AFGlkVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICM 176
Cdd:PRK13641 108 EFG--PKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMM 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489818851 177 KLVGQMAKDFHIpVIFVTHYASEAEMMTEEILVMREGRLEKRKS 220
Cdd:PRK13641 186 QLFKDYQKAGHT-VILVTHNMDDVAEYADDVLVLEHGKLIKHAS 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-200 |
6.36e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 6.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKS-IDG----GIIEFDGTPWDDSNISlhlPV-TERKVGYLFQNLALFPNmNVYENIAF 98
Cdd:PRK14243 38 ITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLYAPDVD---PVeVRRRIGMVFQKPNPFPK-SIYDNIAY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 GLKVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKL 178
Cdd:PRK14243 114 GARINGYKGDMDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEEL 193
|
170 180
....*....|....*....|..
gi 489818851 179 VGQMAKDFHIpvIFVTHYASEA 200
Cdd:PRK14243 194 MHELKEQYTI--IIVTHNMQQA 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
30-210 |
6.47e-21 |
|
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: 88.57 E-value: 6.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGL---KSIDGGIIEFDGTpwddsNIsLHLPVTE------RKVGYLFQN--LALFPNMNVYENIAF 98
Cdd:COG0444 38 GESGSGKSTLARAILGLlppPGITSGEILFDGE-----DL-LKLSEKElrkirgREIQMIFQDpmTSLNPVMTVGDQIAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 GLKVKKKKKKEQAEiqQQVRKMSDYLQIS----------HllyssvQkLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:COG0444 112 PLRIHGGLSKAEAR--ERAIELLERVGLPdperrldrypH------E-LSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 169 EETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVM 210
Cdd:COG0444 183 VTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-214 |
6.52e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.32 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISLHLPVTERKVGYLFQNLALFPNMNVYENIA-----FGLKV 102
Cdd:PRK13537 38 LLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP-----VPSRARHARQRVGVVPQFDNLDPDFTVRENLLvfgryFGLSA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 kkkkkkeqAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR-LICMKLVGQ 181
Cdd:PRK13537 113 --------AAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARhLMWERLRSL 184
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 182 MAKDFHIpvIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK13537 185 LARGKTI--LLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
16-195 |
6.62e-21 |
|
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: 86.54 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnisLHLPVTERKVGYLFQNL--ALFPNmNV 92
Cdd:cd03226 18 DLSLDLYAgEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP-------IKAKERRKSIGYVMQDVdyQLFTD-SV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGLKVKKKkkkEQAEIQQQVRKMS-DYLQISHllyssVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD-EE 170
Cdd:cd03226 90 REELLLGLKELDA---GNEQAETVLKDLDlYALKERH-----PLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyKN 161
|
170 180
....*....|....*....|....*
gi 489818851 171 TRLICmKLVGQMAKDFHIpVIFVTH 195
Cdd:cd03226 162 MERVG-ELIRELAAQGKA-VIVITH 184
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-171 |
6.72e-21 |
|
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: 87.21 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwdDSNISLHLPVTERKVGYLFQNLALFpNMNVYENIAFGLKVKkk 105
Cdd:cd03249 32 VALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRDLNLRWLRSQIGLVSQEPVLF-DGTIAENIRYGKPDA-- 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489818851 106 kkkEQAEIQQQVRKMSDYLQISHL--LYSSV-----QKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET 171
Cdd:cd03249 105 ---TDEEVEEAAKKANIHDFIMSLpdGYDTLvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
30-195 |
8.02e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 8.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddsNIslhlpvterKVGYLFQNLALFPNMNVYENIAFG---------- 99
Cdd:COG0488 31 GRNGAGKSTLLKILAGELEPDSGEVSIPK------GL---------RIGYLPQEPPLDDDLTVLDTVLDGdaelraleae 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 -------LKVKKKKKKEQAEIQQQVRKMSDY------------LQISH-LLYSSVQKLSGGEKQRVAMARAMITEPKLLL 159
Cdd:COG0488 96 leeleakLAEPDEDLERLAELQEEFEALGGWeaearaeeilsgLGFPEeDLDRPVSELSGGWRRRVALARALLSEPDLLL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 160 LDEPFNGLDEETRLicmKLVGQMaKDFHIPVIFVTH 195
Cdd:COG0488 176 LDEPTNHLDLESIE---WLEEFL-KNYPGTVLVVSH 207
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-215 |
8.06e-21 |
|
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: 86.49 E-value: 8.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNIS-LHLPVTERKVGYLFQNLALFpNMNVYENIAFGLKVKKK 105
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT-----DIRqLDPADLRRNIGYVPQDVTLF-YGTLRDNITLGAPLADD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 106 KKKEQAE----IQQQVRK--MSDYLQIShllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRlicMKLV 179
Cdd:cd03245 108 ERILRAAelagVTDFVNKhpNGLDLQIG----ERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE---ERLK 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 489818851 180 GQMAKDF-HIPVIFVTHYASEAEmMTEEILVMREGRL 215
Cdd:cd03245 181 ERLRQLLgDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-217 |
8.55e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 90.17 E-value: 8.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSN-ISLHlpvteRKVGYLFQNLALFpNMNVYENIAFGLKVK 103
Cdd:TIGR00958 509 VVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDhHYLH-----RQVALVGQEPVLF-SGSVRENIAYGLTDT 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 104 kkkkkEQAEIQQQVRKMSDYLQISHLL--YSSV-----QKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEEtrliCM 176
Cdd:TIGR00958 583 -----PDEEIMAAAKAANAHDFIMEFPngYDTEvgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE----CE 653
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 177 KLVGQMAKDFHIPVIFVTHYASEAEmMTEEILVMREGRLEK 217
Cdd:TIGR00958 654 QLLQESRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVE 693
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-218 |
9.26e-21 |
|
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: 86.52 E-value: 9.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLHlpVTERKVGYLFQNLALFpNMNVYE 94
Cdd:cd03251 20 DISLDIPAgETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH--DVRDYTLA--SLRRQIGLVSQDVFLF-NDTVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKKKKE----QAEIQQQVRKMSDYlqishllYSSV-----QKLSGGEKQRVAMARAMITEPKLLLLDEPFN 165
Cdd:cd03251 95 NIAYGRPGATREEVEeaarAANAHEFIMELPEG-------YDTVigergVKLSGGQRQRIAIARALLKDPPILILDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489818851 166 GLDEET-RLICMKLVGQMAkdfHIPVIFVTHYASEAEmMTEEILVMREGRLEKR 218
Cdd:cd03251 168 ALDTESeRLVQAALERLMK---NRTTFVIAHRLSTIE-NADRIVVLEDGKIVER 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-215 |
9.50e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.37 E-value: 9.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 15 LNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpVTERKVGYLFQNlalfPNMNVY- 93
Cdd:PRK13638 20 LNLDFS-LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLL--ALRQQVATVFQD----PEQQIFy 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ----ENIAFGLKVKKKKkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE 169
Cdd:PRK13638 93 tdidSDIAFSLRNLGVP---EAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489818851 170 ETRL----ICMKLVGQMAKdfhipVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK13638 170 AGRTqmiaIIRRIVAQGNH-----VIISSHDIDLIYEISDAVYVLRQGQI 214
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
30-168 |
1.42e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLksIDG-GIIEFDGTPWDDsnislhLPVTE--RKVGYLFQNLALFPNMNVYENIAFGLKVKKKk 106
Cdd:COG4138 29 GPNGAGKSTLLARMAGL--LPGqGEILLNGRPLSD------WSAAElaRHRAYLSQQQSPPFAMPVFQYLALHQPAGAS- 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 107 kkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMIT-------EPKLLLLDEPFNGLD 168
Cdd:COG4138 100 ---SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-215 |
1.55e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.93 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWD--DSNISLHLpvterKVGYLFQNLALFPNMNV 92
Cdd:COG3845 23 DVSLTVRPgEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirSPRDAIAL-----GIGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGLKVKKKKKKEQAEIQQQVRKMSD-Y-LQIShlLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL-DE 169
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARARIRELSErYgLDVD--PDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 170 ET-RLicMKLVGQMAKDFHiPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG3845 176 EAdEL--FEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-215 |
1.69e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.99 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 6 FHKKLPFHDL---NIDYTF-EKPVTAMMGASGSGKSTLFQCVSGLKSIDGG--IIEFDGTPWDDSNISlHLPVTERKVGY 79
Cdd:PRK13645 16 YAKKTPFEFKalnNTSLTFkKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtIVGDYAIPANLKKIK-EVKRLRKEIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 80 LFQnlalFPNMNVYE-----NIAFGlkvKKKKKKEQAEIQQQVRKMSDYLQISH-LLYSSVQKLSGGEKQRVAMARAMIT 153
Cdd:PRK13645 95 VFQ----FPEYQLFQetiekDIAFG---PVNLGENKQEAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 154 EPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-215 |
1.80e-20 |
|
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: 86.40 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKPVT-AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVtERKVGYLFQNL--ALFPNMNV 92
Cdd:TIGR02769 29 NVSLSIEEGETvGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAF-RRDVQLVFQDSpsAVNPRMTV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGLKVKkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQK----LSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:TIGR02769 108 RQIIGEPLRHL-----TSLDESEQKARIAELLDMVGLRSEDADKlprqLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 169 EETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-215 |
2.75e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 86.22 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNislhlpVTE--RKVGYLFQNL-ALFPNMNVYENIAFGLKVK 103
Cdd:PRK13635 37 AIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET------VWDvrRQVGMVFQNPdNQFVGATVQDDVAFGLENI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 104 KKKKKEQAE-IQQQVRK--MSDYLQishllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVG 180
Cdd:PRK13635 111 GVPREEMVErVDQALRQvgMEDFLN------REPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVR 184
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 181 QMAKDFHIPVIFVTHYASEAeMMTEEILVMREGRL 215
Cdd:PRK13635 185 QLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-215 |
4.27e-20 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 85.06 E-value: 4.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 13 HDLNIDYtFEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGII-----EFDGTPWDDSNISLHLpvtERKVGYLFQNLALF 87
Cdd:COG4161 19 FDINLEC-PSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghQFDFSQKPSEKAIRLL---RQKVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 88 PNMNVYENIAFGLKVKKKKKKEQAeiQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:COG4161 95 PHLTVMENLIEAPCKVLGLSKEQA--REKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489818851 168 DEETRLICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG4161 173 DPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
22-215 |
4.51e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.40 E-value: 4.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 22 EKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLALFPNMNVYENIAFGLK 101
Cdd:PRK10070 53 EGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGME 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKKKEQAEiqqqvrKMSDYLQ---ISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKL 178
Cdd:PRK10070 133 LAGINAEERRE------KALDALRqvgLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180 190
....*....|....*....|....*....|....*..
gi 489818851 179 VGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10070 207 LVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
28-215 |
4.73e-20 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 85.07 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCV-------SGLKSIDGGIIEFDGTPwDDSNISLhlpvTERKVGYLFQNLALFPNMNVYENIAFGL 100
Cdd:PRK11124 33 LLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTP-SDKAIRE----LRRNVGMVFQQYNLWPHLTVQQNLIEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 101 KVKKKKKKEQAeiQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVG 180
Cdd:PRK11124 108 CRVLGLSKDQA--LARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIR 185
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 181 QMAkDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK11124 186 ELA-ETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
25-195 |
5.22e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.82 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsnislhlpvteRKVGYLFQNLAL---FPnMNVYENIAFGL- 100
Cdd:NF040873 20 LTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------------ARVAYVPQRSEVpdsLP-LTVRDLVAMGRw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 101 KVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVG 180
Cdd:NF040873 84 ARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLA 163
|
170
....*....|....*
gi 489818851 181 QMAKDfHIPVIFVTH 195
Cdd:NF040873 164 EEHAR-GATVVVVTH 177
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
27-216 |
1.11e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.78 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDG------TPWDdsnislhlpvTERKVGYLFQNL-ALFPNMNVYENIAFG 99
Cdd:PRK13650 37 SIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteeNVWD----------IRHKIGMVFQNPdNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 LKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLV 179
Cdd:PRK13650 107 LENKGI---PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTI 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 489818851 180 GQMAKDFHIPVIFVTHYASEAEmMTEEILVMREGRLE 216
Cdd:PRK13650 184 KGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVE 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-214 |
1.36e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 22 EKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWddSNISLHLpVTERKVGYLFQNLALFPNMNVYENIAF--- 98
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPGHQ-IARMGVVRTFQHVRLFREMTVIENLLVaqh 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 ---------GLKVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD- 168
Cdd:PRK11300 107 qqlktglfsGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNp 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 169 EETRLIcMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK11300 187 KETKEL-DELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
27-216 |
1.53e-19 |
|
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: 81.98 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISLHLPVTERKVGYLFQNLALFpNMNVYENIAfglkvkkkk 106
Cdd:cd03247 32 ALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVP-----VSDLEKALSSLISVLNQRPYLF-DTTLRNNLG--------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkeqaeiqqqvrkmsdylqishllyssvQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDf 186
Cdd:cd03247 97 ----------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD- 147
|
170 180 190
....*....|....*....|....*....|
gi 489818851 187 hIPVIFVTHYASEAEMMtEEILVMREGRLE 216
Cdd:cd03247 148 -KTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
16-213 |
1.68e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.73 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKPVT-AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvteRKVGYLFQ--NLALFPNMNV 92
Cdd:COG4167 31 PVSFTLEAGQTlAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRC----KHIRMIFQdpNTSLNPRLNI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGLKVKKKKKKEQAEIQ-----QQVRKMSDYLQIshllYssVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:COG4167 107 GQILEEPLRLNTDLTAEEREERifatlRLVGLLPEHANF----Y--PHMLSSGQKQRVALARALILQPKIIIADEALAAL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 168 DEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREG 213
Cdd:COG4167 181 DMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQG 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-214 |
1.82e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 83.60 E-value: 1.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 1 MLRLQ-----FHKKLP-----FHDLNI---DYTFekpVTaMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNIS 67
Cdd:COG1101 1 MLELKnlsktFNPGTVnekraLDGLNLtieEGDF---VT-VIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK-----DVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 68 lHLPVTER--KVGYLFQNLAL--FPNMNVYENIA--------FGLKVKKKKKkEQAEIQQQVRKMSdyLQISHLLYSSVQ 135
Cdd:COG1101 72 -KLPEYKRakYIGRVFQDPMMgtAPSMTIEENLAlayrrgkrRGLRRGLTKK-RRELFRELLATLG--LGLENRLDTKVG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 136 KLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:COG1101 148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
25-215 |
2.20e-19 |
|
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: 83.34 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNIsLHLPVTERKV------GYLFQNLALFPNMNVYENIAF 98
Cdd:TIGR02323 31 VLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELEL-YQLSEAERRRlmrtewGFVHQNPRDGLRMRVSAGANI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 GLKVKKKKKKEQAEIQQQVRKMSDYLQISH-LLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMK 177
Cdd:TIGR02323 110 GERLMAIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLD 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 489818851 178 LVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:TIGR02323 190 LLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-217 |
3.62e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 83.26 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISlhlpVTERKVGYLFQNLA-LFPNMNVYENIAFGLKVKK 104
Cdd:PRK13648 38 TSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE----KLRKHIGIVFQNPDnQFVGSIVKYDVAFGLENHA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKKKEQAEIQQQVRKMSDYLQISHllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAK 184
Cdd:PRK13648 114 VPYDEMHRRVSEALKQVDMLERAD---YEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKS 190
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 185 DFHIPVIFVTHYASEAeMMTEEILVMREGRLEK 217
Cdd:PRK13648 191 EHNITIISITHDLSEA-MEADHVIVMNKGTVYK 222
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
28-215 |
5.23e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.84 E-value: 5.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNI-SLHLPVTERKVGYLFQNLALFPNMNVYENIAFGLKVKKKK 106
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DITRLkNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KKEqaeIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKdF 186
Cdd:PRK10908 111 GDD---IRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNR-V 186
|
170 180
....*....|....*....|....*....
gi 489818851 187 HIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10908 187 GVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-213 |
6.23e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 17 IDYT-FEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWddSNISlhlPVTERKVG-YLF-QNLALFPNMNVY 93
Cdd:PRK15439 30 IDFTlHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC--ARLT---PAKAHQLGiYLVpQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGLkvkkkkkkeqAEIQQQVRKMSDYLQI--SHL-LYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE- 169
Cdd:PRK15439 105 ENILFGL----------PKRQASMQKMKQLLAAlgCQLdLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPa 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 170 ETRlicmKLVGQMAK--DFHIPVIFVTHYASEAEMMTEEILVMREG 213
Cdd:PRK15439 175 ETE----RLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
28-213 |
1.46e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTlfqcvSGLKSI----DGGIIEFDGTPWDDSNISLHLPVtERKVGYLFQ--NLALFPNMNVYENIAFGLK 101
Cdd:PRK15134 317 LVGESGSGKST-----TGLALLrlinSQGEIWFDGQPLHNLNRRQLLPV-RHRIQVVFQdpNSSLNPRLNVLQIIEEGLR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:PRK15134 391 VHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS 470
|
170 180 190
....*....|....*....|....*....|..
gi 489818851 182 MAKDFHIPVIFVTHYASEAEMMTEEILVMREG 213
Cdd:PRK15134 471 LQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
28-195 |
1.54e-18 |
|
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: 83.45 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSidggiiEFDGTPWDDSNIslhlpvterKVGYLFQNLALFPNMNVYENIAFGLKVKKKK- 106
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDK------DFNGEARPQPGI---------KVGYLPQEPQLDPTKTVRENVEEGVAEIKDAl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 --------------------KKEQAEIQQQV---------RKMSdylQISHLLY-----SSVQKLSGGEKQRVAMARAMI 152
Cdd:TIGR03719 101 drfneisakyaepdadfdklAAEQAELQEIIdaadawdldSQLE---IAMDALRcppwdADVTKLSGGERRRVALCRLLL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 153 TEPKLLLLDEPFNGLDEETrlicMKLVGQMAKDFHIPVIFVTH 195
Cdd:TIGR03719 178 SKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTH 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-214 |
1.91e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 82.19 E-value: 1.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISLHLPVTERKVGYLFQNLALFPNMNVYEN-IAFGlkvkKKK 106
Cdd:PRK13536 72 LLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-----VPARARLARARIGVVPQFDNLDLEFTVRENlLVFG----RYF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR-LICMKLVGQMAKD 185
Cdd:PRK13536 143 GMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARhLIWERLRSLLARG 222
|
170 180
....*....|....*....|....*....
gi 489818851 186 FHIpvIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK13536 223 KTI--LLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-220 |
1.97e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.29 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISlhlpVTERKVGYLFQNL-ALFPNMNVYENIAFGLKVKKK 105
Cdd:PRK13642 37 SIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW----NLRRKIGMVFQNPdNQFVGATVEDDVAFGMENQGI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 106 KKKEQaeiqqqVRKMSDYLQISHLLYSSVQ---KLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:PRK13642 113 PREEM------IKRVDEALLAVNMLDFKTRepaRLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEI 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 489818851 183 AKDFHIPVIFVTHYASEAEmMTEEILVMREGRLEKRKS 220
Cdd:PRK13642 187 KEKYQLTVLSITHDLDEAA-SSDRILVMKAGEIIKEAA 223
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
27-215 |
2.26e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlPVTERKVGYLFQNL--ALFPNMNVYENIAFGLKVKK 104
Cdd:PRK10419 42 ALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQR-KAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKkkEQAEIQQQVRKMsdyLQISHLLYSSVQK----LSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVG 180
Cdd:PRK10419 121 SL--DKAERLARASEM---LRAVDLDDSVLDKrppqLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLK 195
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 181 QMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10419 196 KLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
25-218 |
5.31e-18 |
|
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: 81.69 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnisLHLPVTERKVGYLFQNLALFpNMNVYENIAFGLKVKK 104
Cdd:TIGR02203 360 TVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD----YTLASLRRQVALVSQDVVLF-NDTIANNIAYGRTEQA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKK-----KEQAEIQQQVRKMSDYLQIShlLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET-RLIcmkl 178
Cdd:TIGR02203 435 DRAeieraLAAAYAQDFVDKLPLGLDTP--IGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESeRLV---- 508
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 179 vgQMAKDFHIP---VIFVTHYASEAEmMTEEILVMREGRLEKR 218
Cdd:TIGR02203 509 --QAALERLMQgrtTLVIAHRLSTIE-KADRIVVMDDGRIVER 548
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-216 |
5.46e-18 |
|
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: 81.72 E-value: 5.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTP---WDDSNISLHlpvterkVGYLFQNLALFPNmNVYENIA-FGl 100
Cdd:COG4618 360 VLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADlsqWDREELGRH-------IGYLPQDVELFDG-TIAENIArFG- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 101 kvkkkkkkeQAEIQQQVR--------KMsdylqISHL-------LYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFN 165
Cdd:COG4618 431 ---------DADPEKVVAaaklagvhEM-----ILRLpdgydtrIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 166 GLDEE-----TRLIcmklvgQMAKDFHIPVIFVTHYASeAEMMTEEILVMREGRLE 216
Cdd:COG4618 497 NLDDEgeaalAAAI------RALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQ 545
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
16-215 |
5.89e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.13 E-value: 5.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpWDDSNISlHLPVTERKVGYLFQNlalfPNMN--- 91
Cdd:PRK13633 28 DVNLEVKKgEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEE-NLWDIRNKAGMVFQN----PDNQiva 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 92 --VYENIAFGlkvKKKKKKEQAEIQQQVR------KMSDYLQIS-HLLyssvqklSGGEKQRVAMARAMITEPKLLLLDE 162
Cdd:PRK13633 101 tiVEEDVAFG---PENLGIPPEEIRERVDeslkkvGMYEYRRHApHLL-------SGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489818851 163 PFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAeMMTEEILVMREGRL 215
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
13-215 |
6.10e-18 |
|
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: 81.71 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 13 HDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDdsNISLHlpVTERKVGYLFQNLALFPNmNV 92
Cdd:TIGR01193 491 SDISLTIK-MNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK--DIDRH--TLRQFINYLPQEPYIFSG-SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGLKVKKKKKK-----EQAEIQQQVRKMSDYLQIShlLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:TIGR01193 565 LENLLLGAKENVSQDEiwaacEIAEIKDDIENMPLGYQTE--LSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489818851 168 DEETRlicMKLVGQMAKDFHIPVIFVTHYASEAEmMTEEILVMREGRL 215
Cdd:TIGR01193 643 DTITE---KKIVNNLLNLQDKTIIFVAHRLSVAK-QSDKIIVLDHGKI 686
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-215 |
7.46e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.12 E-value: 7.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 22 EKPVTAMMGASGSGKSTLFQCVSGL------KSIDGGIIEFDGTPWDDSNISLHLpvtERKVGYLFQNLALFPNMNVYEN 95
Cdd:PRK14267 29 QNGVFALMGPSGCGKSTLLRTFNRLlelneeARVEGEVRLFGRNIYSPDVDPIEV---RREVGMVFQYPNPFPHLTIYDN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 96 IAFGLKVKKKKKKeQAEIQQQVR----KMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET 171
Cdd:PRK14267 106 VAIGVKLNGLVKS-KKELDERVEwalkKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVG 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489818851 172 RLICMKLVGQMAKDFHIpvIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK14267 185 TAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-208 |
8.59e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 8.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddsnislhlpvtERKVGYLFQNLALFPNMNvyenIAFGLKVKKKKK 107
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------------KLRIGYVPQKLYLDTTLP----LTVNRFLRLRPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 108 KEQAEIQQQVRKmsdyLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFH 187
Cdd:PRK09544 96 TKKEDILPALKR----VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELD 171
|
170 180
....*....|....*....|.
gi 489818851 188 IPVIFVTHYASEAEMMTEEIL 208
Cdd:PRK09544 172 CAVLMVSHDLHLVMAKTDEVL 192
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-214 |
1.48e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 78.43 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 12 FHDLNID-YTFEkpVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNIsLHLPVTERKV------GYLFQNL 84
Cdd:PRK11701 22 CRDVSFDlYPGE--VLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDL-YALSEAERRRllrtewGFVHQHP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 85 ALFPNMNVYE--NI-----AFGlkvkkkkKKEQAEIQQQVrkmSDYLQISHLLYSSVQKL----SGGEKQRVAMARAMIT 153
Cdd:PRK11701 99 RDGLRMQVSAggNIgerlmAVG-------ARHYGDIRATA---GDWLERVEIDAARIDDLpttfSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489818851 154 EPKLLLLDEPFNGLD--EETRLicMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK11701 169 HPRLVFMDEPTGGLDvsVQARL--LDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-215 |
1.52e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.02 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQnlalFPNMNVYE-----NIAFGl 100
Cdd:PRK13649 36 TAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQ----FPESQLFEetvlkDVAFG- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 101 kvKKKKKKEQAEIQQQVRKMSDYLQISHLLYS-SVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLV 179
Cdd:PRK13649 111 --PQNFGVSQEEAEALAREKLALVGISESLFEkNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLF 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 180 GQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK13649 189 KKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-216 |
1.83e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFdGTpwddsNIslhlpvterKVGYLFQNLALF-PNMNVY 93
Cdd:COG0488 333 DLSLRIDRGdRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TV---------KIGYFDQHQEELdPDKTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAfglkvkkkKKKEQAEiQQQVRkmsDYLQisHLL------YSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:COG0488 398 DELR--------DGAPGGT-EQEVR---GYLG--RFLfsgddaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489818851 168 DEETRlicmKLVGQMAKDFHIPVIFVTH--YASEAemMTEEILVMREGRLE 216
Cdd:COG0488 464 DIETL----EALEEALDDFPGTVLLVSHdrYFLDR--VATRILEFEDGGVR 508
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-215 |
1.84e-17 |
|
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: 77.91 E-value: 1.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddSNISLHLPVT-ERKVGYLFQNLALFpNMNVYENIAFGLKVK 103
Cdd:cd03252 30 VVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG-----HDLALADPAWlRRQVGVVLQENVLF-NRSIRDNIALADPGM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 104 KKKKKEQ----AEIQQQVRKMSD-YLQIshlLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKL 178
Cdd:cd03252 104 SMERVIEaaklAGAHDFISELPEgYDTI---VGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 489818851 179 VGQMAKDFhiPVIFVTHYASeAEMMTEEILVMREGRL 215
Cdd:cd03252 181 MHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRI 214
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-215 |
2.22e-17 |
|
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: 80.44 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 15 LNIDYtFEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddSNISLHLPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:TIGR01257 949 LNITF-YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-----KDIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFglkVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:TIGR01257 1023 HILF---YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 175 CMKLVGQMAKDFHIpvIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:TIGR01257 1100 IWDLLLKYRSGRTI--IMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-214 |
3.22e-17 |
|
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: 79.48 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLK---SIDGGIIeFDGTPWDDSNISlhlpVTERK-VGYLFQNLALFPNM 90
Cdd:TIGR02633 19 GIDLEVRPgECVGLCGENGAGKSTLMKILSGVYphgTWDGEIY-WSGSPLKASNIR----DTERAgIVIIHQELTLVPEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENIAFGLKVKKK-KKKEQAEIQQQVRKMSDYLQISHLLYS-SVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:TIGR02633 94 SVAENIFLGNEITLPgGRMAYNAMYLRAKNLLRELQLDADNVTrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 169 EETRLICMKLVGQMaKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:TIGR02633 174 EKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-214 |
3.32e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 79.59 E-value: 3.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGL---KSIDGGIIeFDGTPWDDSNISlhlpVTERK-VGYLFQNLALFPNM 90
Cdd:PRK13549 23 NVSLKVRAgEIVSLCGENGAGKSTLMKVLSGVyphGTYEGEII-FEGEELQASNIR----DTERAgIAIIHQELALVKEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENIAFGLKVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE- 169
Cdd:PRK13549 98 SVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTEs 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489818851 170 ETRlICMKLVGQMaKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK13549 178 ETA-VLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-217 |
6.27e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.04 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhLPVtERKVGYLFQNL--ALFPNmNV 92
Cdd:PRK13639 20 GINFKAEKgEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSL-LEV-RKTVGIVFQNPddQLFAP-TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGlkvKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:PRK13639 97 EEDVAFG---PLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489818851 173 LICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:PRK13639 174 SQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIK 217
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-215 |
8.50e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 77.08 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 15 LNIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQnlalFPNMNVY 93
Cdd:PRK13643 23 FDIDLEVKKgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 E-----NIAFGLKVKKKKKKEQAEIQQQVRKMSDYLQisHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:PRK13643 99 EetvlkDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 169 EETRLICMKLVGQMAKDFHIpVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQT-VVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
25-215 |
1.22e-16 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 76.66 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddsnislHLPVTE-----RKVGYLFQNLALFPNMNVYENIA-- 97
Cdd:TIGR01188 21 VFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG----------YDVVREprkvrRSIGIVPQYASVDEDLTGRENLEmm 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 ---FGLkvkkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:TIGR01188 91 grlYGL--------PKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 175 CMKLVGQMAKDFHIpVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:TIGR01188 163 IWDYIRALKEEGVT-ILLTTHYMEEADKLCDRIAIIDHGRI 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
16-217 |
1.32e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.81 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGII---EFDGTPWDDSNISLHLPVTE---------RKVGYLFQ 82
Cdd:PRK13631 44 NISYTFEKnKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgDIYIGDKKNNHELITNPYSKkiknfkelrRRVSMVFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 83 nlalFPNMNVYE-----NIAFGLKVKKKKKKEQAEiqqqvrKMSDYLQISHLLYSSVQK----LSGGEKQRVAMARAMIT 153
Cdd:PRK13631 124 ----FPEYQLFKdtiekDIMFGPVALGVKKSEAKK------LAKFYLNKMGLDDSYLERspfgLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489818851 154 EPKLLLLDEPFNGLDEETRLICMKLVGQmAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILK 256
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-168 |
1.86e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIeFDGTP---WDDSNISLHlpvteRkvGYLFQNLALFPNMNVYENIAFGLKVKKKK 106
Cdd:PRK03695 29 GPNGAGKSTLLARMAGLLPGSGSIQ-FAGQPleaWSAAELARH-----R--AYLSQQQTPPFAMPVFQYLTLHQPDKTRT 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 107 kkeqAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMA-------RAMITEPKLLLLDEPFNGLD 168
Cdd:PRK03695 101 ----EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLD 165
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
26-172 |
1.95e-16 |
|
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: 77.40 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhlpvTERKVGYLFQNLALFpNMNVYENIAFGlkVKKK 105
Cdd:TIGR02868 364 VAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE----VRRRVSVCAQDAHLF-DTTVRENLRLA--RPDA 436
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 106 KKKEQAEIQQQVRkMSDYLQ-----ISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:TIGR02868 437 TDEELWAALERVG-LADWLRalpdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
30-168 |
2.12e-16 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 76.31 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISlHLPVTE-----RKVGYLFQN--LALFPNMNVYENIAFGLKV 102
Cdd:COG4608 51 GESGCGKSTLGRLLLRLEEPTSGEILFDGQ-----DIT-GLSGRElrplrRRMQMVFQDpyASLNPRMTVGDIIAEPLRI 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 KKKKkkEQAEIQQQVRKMsdyLQISHLLYSSVQK----LSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:COG4608 125 HGLA--SKAERRERVAEL---LELVGLRPEHADRypheFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-214 |
2.44e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.10 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKS--IDGGIIEFDGTpwddsNIsLHLPVTERK---VGYLFQNLALFPN 89
Cdd:COG0396 18 GVNLTIKPgEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGE-----DI-LELSPDERAragIFLAFQYPVEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 90 MNVYENIAFGLKVKKKKKKEQAEIQQQVRKMSDYLQISH-LLYSSV-QKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:COG0396 92 VSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEdFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 168 DEETrlicMKLVGQMAKDFHIP---VIFVTHYaseaemmtEEIL---------VMREGR 214
Cdd:COG0396 172 DIDA----LRIVAEGVNKLRSPdrgILIITHY--------QRILdyikpdfvhVLVDGR 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-215 |
3.88e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 75.20 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKPVT-AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQnlalFPNMNVYE 94
Cdd:PRK13646 25 DVNTEFEQGKYyAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 N-----IAFGLKVKKKKKKEQAEiqQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE 169
Cdd:PRK13646 101 DtvereIIFGPKNFKMNLDEVKN--YAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 170 ETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK13646 179 QSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
25-217 |
4.34e-16 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddSNISL------HLPVTERK--------VGYLFQNLALFPNM 90
Cdd:PRK10619 33 VISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG-----QTINLvrdkdgQLKVADKNqlrllrtrLTMVFQHFNLWSHM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENI------AFGLkvkkkkkkEQAEIQQQVRKMSDYLQISHllySSVQK----LSGGEKQRVAMARAMITEPKLLLL 160
Cdd:PRK10619 108 TVLENVmeapiqVLGL--------SKQEARERAVKYLAKVGIDE---RAQGKypvhLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489818851 161 DEPFNGLDEETRLICMKLVGQMAKDFHIPVIfVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-217 |
4.43e-16 |
|
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: 76.38 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKS---IDGGII---------------EFDGTPWDDSNISLHLPVTE-- 74
Cdd:TIGR03269 18 NISFTIEEgEVLGILGRSGAGKSVLMHVLRGMDQyepTSGRIIyhvalcekcgyverpSKVGEPCPVCGGTLEPEEVDfw 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 75 -----------RKVGYLFQ-NLALFPNMNVYENIafgLKVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEK 142
Cdd:TIGR03269 98 nlsdklrrrirKRIAIMLQrTFALYGDDTVLDNV---LEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 143 QRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKE 249
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
26-214 |
5.10e-16 |
|
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: 76.01 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDD-SNISLHlpvteRKVGYLFQNLALFpNMNVYENIAFGlkvkk 104
Cdd:COG5265 387 VAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLR-----AAIGIVPQDTVLF-NDTIAYNIAYG----- 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKKKEQAEIQQQVRKMsdylQISHLLYSSVQ-----------KLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET-R 172
Cdd:COG5265 456 RPDASEEEVEAAARAA----QIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTeR 531
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 173 LI--CMKLVGQmakdfHIPVIFVTHYAS---EAemmtEEILVMREGR 214
Cdd:COG5265 532 AIqaALREVAR-----GRTTLVIAHRLStivDA----DEILVLEAGR 569
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-195 |
1.04e-15 |
|
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: 70.94 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNID-YTFEKpvTAMMGASGSGKSTLfqcvsgLKSIDGGIIEFDGTPWDDSNIslhlpvterKVGYL 80
Cdd:cd03221 6 LSKTYGGKLLLKDISLTiNPGDR--IGLVGRNGAGKSTL------LKLIAGELEPDEGIVTWGSTV---------KIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 81 FQnlalfpnmnvyeniafglkvkkkkkkeqaeiqqqvrkmsdylqishllyssvqkLSGGEKQRVAMARAMITEPKLLLL 160
Cdd:cd03221 69 EQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 161 DEPFNGLDEETRlicmKLVGQMAKDFHIPVIFVTH 195
Cdd:cd03221 95 DEPTNHLDLESI----EALEEALKEYPGTVILVSH 125
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-215 |
1.17e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.12 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYTFEKpVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTP-WDDSNISLhlpvtERKVGYL 80
Cdd:PRK11231 8 LTVGYGTKRILNDLSLSLPTGK-ITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPiSMLSSRQL-----ARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 81 FQNLALFPNMNVYENIAFGLKVKKKK-----KKEQAEIQQQVRKMsdylQISHLLYSSVQKLSGGEKQRVAMARAMITEP 155
Cdd:PRK11231 82 PQHHLTPEGITVRELVAYGRSPWLSLwgrlsAEDNARVNQAMEQT----RINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 156 KLLLLDEPFNGLDEETRLICMKLVGQMaKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMREL-NTQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-218 |
1.32e-15 |
|
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: 72.17 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKS--IDGGIIEFDGTpwddsNIsLHLPVTERK---VGYLFQNLALFPn 89
Cdd:cd03217 18 GVNLTIKKgEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGE-----DI-TDLPPEERArlgIFLAFQYPPEIP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 90 mnvyeniafGLkvkkkkkkeqaeiqqqvrKMSDYLQishllysSVQK-LSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:cd03217 91 ---------GV------------------KNADFLR-------YVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489818851 169 EETrlicMKLVGQMAKDFHIP---VIFVTHYASEAEMMTEE-ILVMREGRLEKR 218
Cdd:cd03217 137 IDA----LRLVAEVINKLREEgksVLIITHYQRLLDYIKPDrVHVLYDGRIVKS 186
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-171 |
1.50e-15 |
|
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: 72.64 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 7 HKKLPFHDLNIDYtfeKP--VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDD-SNISLHlpvteRKVGYLFQN 83
Cdd:cd03254 14 EKKPVLKDINFSI---KPgeTVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLR-----SMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 84 LALFPNmNVYENIAFGlkvKKKKKKEQAEIQQQVRKMSDYlqISHL---LYSSV----QKLSGGEKQRVAMARAMITEPK 156
Cdd:cd03254 86 TFLFSG-TIMENIRLG---RPNATDEEVIEAAKEAGAHDF--IMKLpngYDTVLgengGNLSQGERQLLAIARAMLRDPK 159
|
170
....*....|....*
gi 489818851 157 LLLLDEPFNGLDEET 171
Cdd:cd03254 160 ILILDEATSNIDTET 174
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-215 |
2.14e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSidggiiEFDGTPWDDSNISLHLPVTE--RKVGY 79
Cdd:PRK10253 13 LTLGYGKYTVAENLTVEIP-DGHFTAIIGPNGCGKSTLLRTLSRLMT------PAHGHVWLDGEHIQHYASKEvaRRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 80 LFQNLALFPNMNVYENIAFGLKVKKKKKKE-QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLL 158
Cdd:PRK10253 86 LAQNATTPGDITVQELVARGRYPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489818851 159 LLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
28-195 |
2.30e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 70.65 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFdgtPWDDSniSLHLPvterKVGYLFQ-NLAlfpnmnvyeniafglkvkkkk 106
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWGSGRIGM---PEGED--LLFLP----QRPYLPLgTLR--------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 kkEQaeiqqqvrkmsdylqishLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRlicmKLVGQMAKDF 186
Cdd:cd03223 82 --EQ------------------LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE----DRLYQLLKEL 137
|
....*....
gi 489818851 187 HIPVIFVTH 195
Cdd:cd03223 138 GITVISVGH 146
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
13-215 |
3.28e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 13 HDLNIDYTFEKpVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTP---WDDSNISlhlpvteRKVGYLFQNLALFPN 89
Cdd:PRK10575 28 HPLSLTFPAGK-VTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPlesWSSKAFA-------RKVAYLPQQLPAAEG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 90 MNVYENIAFGLKVKKKKKKE-QAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:PRK10575 100 MTVRELVAIGRYPWHGALGRfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489818851 169 EETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEM 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-220 |
4.77e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 71.74 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 22 EKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpvtERKVGYLFQN--LALFPNMNVYENIAFG 99
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYR----SQRIRMIFQDpsTSLNPRQRISQILDFP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 LKVKKKKKKEQAE--IQQQVRKMSdyLQISHLLYSSvQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMK 177
Cdd:PRK15112 114 LRLNTDLEPEQREkqIIETLRQVG--LLPDHASYYP-HMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 178 LVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLEKRKS 220
Cdd:PRK15112 191 LMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
30-172 |
4.95e-15 |
|
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: 70.93 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLfqcvsgLKSI------DGG--IIEFDGTPWDDSNISLH--LPVTERKVGYLFQNLALFPNMNVYENIAFG 99
Cdd:COG4778 44 GPSGAGKSTL------LKCIygnylpDSGsiLVRHDGGWVDLAQASPReiLALRRRTIGYVSQFLRVIPRVSALDVVAEP 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489818851 100 LKVKKKkkkEQAEIQQQVRKMSDYLQI-SHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:COG4778 118 LLERGV---DREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANR 188
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
30-214 |
5.02e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 72.43 E-value: 5.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDG--------TPWDDsnislhlpvTERKVGYLFQN-LA-LFPNMNVYENIAFG 99
Cdd:PRK15079 54 GESGCGKSTFARAIIGLVKATDGEVAWLGkdllgmkdDEWRA---------VRSDIQMIFQDpLAsLNPRMTIGEIIAEP 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 LKVKKKKKKEQaEIQQQVRKMSDYLQI-SHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKL 178
Cdd:PRK15079 125 LRTYHPKLSRQ-EVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNL 203
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 179 VGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK15079 204 LQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-215 |
5.64e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 23 KPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTE--RKVGYLFQNLALFPnMNVYENIAFGL 100
Cdd:PRK14271 47 RAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEfrRRVGMLFQRPNPFP-MSIMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 101 KVKKKKKKEQAEIQQQVR--KMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKL 178
Cdd:PRK14271 126 RAHKLVPRKEFRGVAQARltEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190
....*....|....*....|....*....|....*..
gi 489818851 179 VGQMAKdfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK14271 206 IRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
26-183 |
1.03e-14 |
|
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: 69.58 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKsiDGGIIE----FDGTPWDDSnislhlpvTERKVGYLFQNLALFPNMNVYENIAFglk 101
Cdd:cd03232 36 TALMGESGAGKTTLLDVLAGRK--TAGVITgeilINGRPLDKN--------FQRSTGYVEQQDVHSPNLTVREALRF--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 vkkkkkkeqaeiqqqvrkmSDYLqishllyssvQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:cd03232 103 -------------------SALL----------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
..
gi 489818851 182 MA 183
Cdd:cd03232 154 LA 155
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-217 |
2.73e-14 |
|
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: 70.99 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYT-FEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFD-GTPWDDsnislhlpVTE----------RKVGYLFQN 83
Cdd:TIGR03269 302 NVSLEvKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVD--------MTKpgpdgrgrakRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 84 LALFPNMNVYENI--AFGLKVKKKKKKEQAEIQQQVRKMSDYLQIShLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLD 161
Cdd:TIGR03269 374 YDLYPHRTVLDNLteAIGLELPDELARMKAVITLKMVGFDEEKAEE-ILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 162 EPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-215 |
7.64e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 7.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGlkSIDG---GIIEFDGTPWDDSN--------ISLhLPVTERKVGylfqnlaLFPNMNVYENIA- 97
Cdd:PRK13549 295 GLVGAGRTELVQCLFG--AYPGrweGEIFIDGKPVKIRNpqqaiaqgIAM-VPEDRKRDG-------IVPVMGVGKNITl 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 -----FGLKVKKKKKKEQAEIQQQVRKMSdyLQISHLLYSsVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:PRK13549 365 aaldrFTGGSRIDDAAELKTILESIQRLK--VKTASPELA-IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 173 LICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK13549 442 YEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
25-167 |
8.71e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.98 E-value: 8.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDG---TPWDDSNIslhlpvTERKVGYLFQNLALFPNMNVYENIAFGlk 101
Cdd:PRK11614 33 IVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGkdiTDWQTAKI------MREAVAIVPEGRRVFSRMTVEENLAMG-- 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 102 vkkKKKKEQAEIQQQVRKMSDYLqiSHLLYSSVQK---LSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:PRK11614 105 ---GFFAERDQFQERIKWVYELF--PRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-214 |
1.02e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.52 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGL---KSIDGGIIEFDGTPWDDsnislhlpvTERKVGYLFQNLALFPNMNVYENIAF-GL 100
Cdd:PLN03211 96 ILAVLGPSGSGKSTLLNALAGRiqgNNFTGTILANNRKPTKQ---------ILKRTGFVTQDDILYPHLTVRETLVFcSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 101 KVKKKKKKEQAEIQQQVRKMSDY----LQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICM 176
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESVISELgltkCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190
....*....|....*....|....*....|....*...
gi 489818851 177 KLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGR 284
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
27-215 |
1.07e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.08 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTP---WDDSNISLHLPVTERKVgYLF-----QNLAL-FPNMNvyenia 97
Cdd:PRK11160 370 ALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiadYSEAALRQAISVVSQRV-HLFsatlrDNLLLaAPNAS------ 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 fglkvkkkkkKEQ-AEIQQQVrKMSDYLQISHLLYSSV----QKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET- 171
Cdd:PRK11160 443 ----------DEAlIEVLQQV-GLEKLLEDDKGLNAWLgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETe 511
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489818851 172 RLIcMKLVGQMAKDfhIPVIFVTHYASEAEMMtEEILVMREGRL 215
Cdd:PRK11160 512 RQI-LELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQI 551
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-171 |
1.40e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.81 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 6 FHKKLPFHDLnidyTFEKP---VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnislhlpvterKVGYLFQ 82
Cdd:TIGR03719 332 FGDKLLIDDL----SFKLPpggIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---------------KLAYVDQ 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 83 NL-ALFPNMNVYENIAFGLKvkkkkkkeqaEIQQQVRKMSDYLQISHLLYSS------VQKLSGGEKQRVAMARAMITEP 155
Cdd:TIGR03719 393 SRdALDPNKTVWEEISGGLD----------IIKLGKREIPSRAYVGRFNFKGsdqqkkVGQLSGGERNRVHLAKTLKSGG 462
|
170
....*....|....*.
gi 489818851 156 KLLLLDEPFNGLDEET 171
Cdd:TIGR03719 463 NVLLLDEPTNDLDVET 478
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-213 |
1.72e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 23 KP--VTAMMGASGSGKSTLFQCVSGLKS---IDGGIIEFDGTPWDDSnislhlpvTERKVGYLFQNLALFPNMNVYENIA 97
Cdd:TIGR00956 787 KPgtLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSS--------FQRSIGYVQQQDLHLPTSTVRESLR 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 FGLKVKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSV----QKLSGGEKQRVAMARAMITEPKLLL-LDEPFNGLDEETR 172
Cdd:TIGR00956 859 FSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTA 938
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 173 LICMKLVGQMAKdfHIPVIFVTHYASEAEMMTE--EILVMREG 213
Cdd:TIGR00956 939 WSICKLMRKLAD--HGQAILCTIHQPSAILFEEfdRLLLLQKG 979
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-214 |
1.80e-13 |
|
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: 66.34 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKP-VTAMMGASGSGKSTLFQCVSG-LKSIDGgiiefdgtpwddsniSLHLPvteRKVGYLFQNlALFPNMNVY 93
Cdd:cd03250 23 DINLEVPKGeLVAIVGPVGSGKSSLLSALLGeLEKLSG---------------SVSVP---GSIAYVSQE-PWIQNGTIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGlkvkkkkkkeqAEIQQQvrkmsdylqishlLYSSVQK-------------------------LSGGEKQRVAMA 148
Cdd:cd03250 84 ENILFG-----------KPFDEE-------------RYEKVIKacalepdleilpdgdlteigekginLSGGQKQRISLA 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 149 RAMITEPKLLLLDEPFNGLDEET-RLICMKLVGQMAKDfHIPVIFVTH---YASEAEMmteeILVMREGR 214
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVgRHIFENCILGLLLN-NKTRILVTHqlqLLPHADQ----IVVLDNGR 204
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-215 |
1.81e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.70 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISlHLPVTERKVGYLFQNLAL-FPNMNVY 93
Cdd:PRK13644 20 NINLVIKKgEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGI--DTGDFS-KLQGIRKLVGIVFQNPETqFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGlkvKKKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRL 173
Cdd:PRK13644 97 EDLAFG---PENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 174 ICMKLVGQMAKDFHIpVIFVTHYASEAEmMTEEILVMREGRL 215
Cdd:PRK13644 174 AVLERIKKLHEKGKT-IVYITHNLEELH-DADRIIVMDRGKI 213
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-195 |
2.64e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 68.22 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSidggiiEFDGTPWDDSNIslhlpvterKVGYLFQNLALFPNMNVYENIAFGLKVKKKKKK- 108
Cdd:PRK11819 40 GLNGAGKSTLLRIMAGVDK------EFEGEARPAPGI---------KVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 109 --------------------EQAEIQQQV---------RKMS-----------DylqishllySSVQKLSGGEKQRVAMA 148
Cdd:PRK11819 105 fneiyaayaepdadfdalaaEQGELQEIIdaadawdldSQLEiamdalrcppwD---------AKVTKLSGGERRRVALC 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489818851 149 RAMITEPKLLLLDEPFNGLDEETrlicmklVG---QMAKDFHIPVIFVTH 195
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAES-------VAwleQFLHDYPGTVVAVTH 218
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-214 |
3.38e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvtERKVGYLFQNLALFPNMNVYENIAFGLKVKK 104
Cdd:PRK10982 26 IHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAL---ENGISMVHQELNLVLQRSVMDNMWLGRYPTK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMaK 184
Cdd:PRK10982 103 GMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-K 181
|
170 180 190
....*....|....*....|....*....|
gi 489818851 185 DFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK10982 182 ERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
29-214 |
3.55e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 65.75 E-value: 3.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 29 MGASGSGKSTLFQCVSGL----KSIDgGIIEFDGTPWDDSNISLHlpvteRKVGYLFQNLALFPNMNVYENIAFGLKVkk 104
Cdd:cd03233 39 LGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYKEFAEKYP-----GEIIYVSEEDVHFPTLTVRETLDFALRC-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 kkkkeqaeiqqqvrKMSDYlqishllyssVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAK 184
Cdd:cd03233 111 --------------KGNEF----------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAD 166
|
170 180 190
....*....|....*....|....*....|.
gi 489818851 185 DFHIPVIFVTHYAS-EAEMMTEEILVMREGR 214
Cdd:cd03233 167 VLKTTTFVSLYQASdEIYDLFDKVLVLYEGR 197
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
29-195 |
4.78e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 29 MGASGSGKSTLFQCVSGLksidggiiefdgtpWDDSNISLHLPVTER----------KVGYLFQNLAlFPNmnvyeniaf 98
Cdd:COG4178 395 TGPSGSGKSTLLRAIAGL--------------WPYGSGRIARPAGARvlflpqrpylPLGTLREALL-YPA--------- 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 glkvkKKKKKEQAEIQQQVRKmsdyLQISHL---LYSSV---QKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:COG4178 451 -----TAEAFSDAELREALEA----VGLGHLaerLDEEAdwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
170 180
....*....|....*....|...
gi 489818851 173 LICMKLVGQMAKDfhIPVIFVTH 195
Cdd:COG4178 522 AALYQLLREELPG--TTVISVGH 542
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-215 |
5.06e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.18 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSG-------LKsIDGgiIEFDgtpwddsniSLHLPVTERKVGYLFQNLALFPNmNVYENIAF 98
Cdd:PRK11174 379 IALVGPSGAGKTSLLNALLGflpyqgsLK-ING--IELR---------ELDPESWRKHLSWVGQNPQLPHG-TLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 GlkvkkKKKKEQAEIQQQVRK--MSDYL-QISHLLYSSVQK----LSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET 171
Cdd:PRK11174 446 G-----NPDASDEQLQQALENawVSEFLpLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489818851 172 RLICMKLVGQMAKdfHIPVIFVTHYASEAEMMtEEILVMREGRL 215
Cdd:PRK11174 521 EQLVMQALNAASR--RQTTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
14-176 |
5.55e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 5.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 14 DLNIDY---------TFEKPVTAMM---GASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddSNISLHLPVTERKVGYLF 81
Cdd:PRK13540 6 ELDFDYhdqpllqqiSFHLPAGGLLhlkGSNGAGKTTLLKLIAGLLNPEKGEILFER-----QSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 82 QNLALFPNMNVYENIAFGLKVKKKKKkeqaEIQQQVRKMSdylqISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLD 161
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSPGAV----GITELCRLFS----LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
170
....*....|....*
gi 489818851 162 EPFNGLDEETRLICM 176
Cdd:PRK13540 153 EPLVALDELSLLTII 167
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-168 |
5.88e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 66.99 E-value: 5.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSID---GGIIEFDGTPWDDSNISlhlpvteRKVGYLFQNLALFPNMNVYENIAFG---- 99
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMR-------AISAYVQQDDLFIPTLTVREHLMFQahlr 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 100 LKVKKKKKKEQAEIQQQVRKMSdYLQISHLLYSS---VQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:TIGR00955 128 MPRRVTKKEKRERVDEVLQALG-LRKCANTRIGVpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-217 |
7.34e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.26 E-value: 7.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 6 FHKKLPFH----DlNIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEF-----------DGTPWDDSNISLH 69
Cdd:PRK13651 12 FNKKLPTElkalD-NVSVEINQgEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkktKEKEKVLEKLVIQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 70 LPVTE---------RKVGYLFQ--NLALFPNmNVYENIAFGlkvKKKKKKEQAEIQQQVRKmsdYLQISHLLYSSVQK-- 136
Cdd:PRK13651 91 KTRFKkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFG---PVSMGVSKEEAKKRAAK---YIELVGLDESYLQRsp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 137 --LSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIpVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK13651 164 feLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLEWTKRTIFFKDGK 242
|
...
gi 489818851 215 LEK 217
Cdd:PRK13651 243 IIK 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-215 |
7.39e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.86 E-value: 7.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLpvtERKVGYLFQNLALFPNMNVYENIAFGLKVKK 104
Cdd:PRK11288 32 VHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAL---AAGVAIIYQELHLVPEMTVAENLYLGQLPHK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKKKEQAEIQQQVRkmsdyLQISHL-----LYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD--EETRLicMK 177
Cdd:PRK11288 109 GGIVNRRLLNYEAR-----EQLEHLgvdidPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSarEIEQL--FR 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 489818851 178 LVGQMAKDFHIpVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK11288 182 VIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-168 |
7.62e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 7.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNI--SLHlpvterkvgYLFQNLALFPNMNVYENIAF--GLK 101
Cdd:PRK13539 31 LVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeACH---------YLGHRNAMKPALTVAENLEFwaAFL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489818851 102 VKKKKKKEQAeiqqqvrkmSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:PRK13539 102 GGEELDIAAA---------LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
16-218 |
8.51e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.58 E-value: 8.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEKPVT-AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNislhLPVTERKVGYLFQNLALFpNMNVYE 94
Cdd:PRK11176 361 NINFKIPAGKTvALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT----LASLRNQVALVSQNVHLF-NDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGlkvkKKKKKEQAEIQQQVR---------KMSDYLQIshLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFN 165
Cdd:PRK11176 436 NIAYA----RTEQYSREQIEEAARmayamdfinKMDNGLDT--VIGENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489818851 166 GLDEETRLICMKLVGQMAKDFHIPVIfvTHYASEAEmMTEEILVMREGRLEKR 218
Cdd:PRK11176 510 ALDTESERAIQAALDELQKNRTSLVI--AHRLSTIE-KADEILVVEDGEIVER 559
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-215 |
8.96e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 65.88 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDG-TPWDD-----SNISL----------HLPVTErkvgylfqNLALfpNMNVY 93
Cdd:COG4586 55 GPNGAGKSTTIKMLTGILVPTSGEVRVLGyVPFKRrkefaRRIGVvfgqrsqlwwDLPAID--------SFRL--LKAIY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 EniafglkvkkkkkKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD----E 169
Cdd:COG4586 125 R-------------IPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDvvskE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489818851 170 ETRlicmKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG4586 192 AIR----EFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-182 |
9.27e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.67 E-value: 9.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 18 DYTFEKP---VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDS---NISLHLPVTErKVGYLFQNLAL-FPNM 90
Cdd:PRK15056 25 DASFTVPggsIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqkNLVAYVPQSE-EVDWSFPVLVEdVVMM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENIAFglkvkkkKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:PRK15056 104 GRYGHMGW-------LRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176
|
170
....*....|..
gi 489818851 171 TRLICMKLVGQM 182
Cdd:PRK15056 177 TEARIISLLREL 188
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-215 |
1.57e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.90 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLALFPNMNVYENIAFglkVKKKK 106
Cdd:PRK10535 38 AIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREHFGFIFQRYHLLSHLTAAQNVEV---PAVYA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDF 186
Cdd:PRK10535 115 GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRG 194
|
170 180 190
....*....|....*....|....*....|..
gi 489818851 187 HIpVIFVTH---YASEAEMMTEeilvMREGRL 215
Cdd:PRK10535 195 HT-VIIVTHdpqVAAQAERVIE----IRDGEI 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
27-215 |
2.03e-12 |
|
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: 65.48 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGL----KSIDGGIIEFDGTpwddsNIsLHLPVTE------RKVGYLFQN--LALFPNMNVYE 94
Cdd:COG4172 40 ALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQ-----DL-LGLSERElrrirgNRIAMIFQEpmTSLNPLHTIGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKVKKKKKKEQAE-----------IQQQVRKMSDYlqiSHllyssvqKLSGGEKQRVAMARAMITEPKLLLLDEP 163
Cdd:COG4172 114 QIAEVLRLHRGLSGAAARaralellervgIPDPERRLDAY---PH-------QLSGGQRQRVMIAMALANEPDLLIADEP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 164 FNGLDEETRLICMKLVGQMAKDFHIPVIFVTH-------YAseaemmtEEILVMREGRL 215
Cdd:COG4172 184 TTALDVTVQAQILDLLKDLQRELGMALLLITHdlgvvrrFA-------DRVAVMRQGEI 235
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-214 |
2.19e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 64.99 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNISLHLPVTE----RKVGYLFQNLalFPNMNVYENIAFGLKV 102
Cdd:PRK11308 45 AVVGESGCGKSTLARLLTMIETPTGGELYYQGQ-----DLLKADPEAQkllrQKIQIVFQNP--YGSLNPRKKVGQILEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 KKKKKKE--QAEIQQQVRKMSD--------YLQISHLLyssvqklSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:PRK11308 118 PLLINTSlsAAERREKALAMMAkvglrpehYDRYPHMF-------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 489818851 173 LICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK11308 191 AQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGR 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
30-215 |
2.21e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.19 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwDDSNISLHLPVTERKVGYLFQNL---ALFPNMNVYENIA--------- 97
Cdd:PRK09700 296 GLVGSGRTELMNCLFGVDKRAGGEIRLNG---KDISPRSPLDAVKKGMAYITESRrdnGFFPNFSIAQNMAisrslkdgg 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 FGLKVKKKKKKEQAEIQQQVRKMsdyLQIS-HLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICM 176
Cdd:PRK09700 373 YKGAMGLFHEVDEQRTAENQREL---LALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY 449
|
170 180 190
....*....|....*....|....*....|....*....
gi 489818851 177 KLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK09700 450 KVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
12-171 |
2.51e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.37 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 12 FHDLNIDY----------TFE-KP--VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsNI-SLHLPVTERKV 77
Cdd:PRK13657 337 FDDVSFSYdnsrqgvedvSFEaKPgqTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT-----DIrTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 78 GYLFQNLALFpNMNVYENIAFGLK-VKKKKKKEQAEIQQQvrkmSDYLQISHLLYSSV-----QKLSGGEKQRVAMARAM 151
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDNIRVGRPdATDEEMRAAAERAQA----HDFIERKPDGYDTVvgergRQLSGGERQRLAIARAL 486
|
170 180
....*....|....*....|
gi 489818851 152 ITEPKLLLLDEPFNGLDEET 171
Cdd:PRK13657 487 LKDPPILILDEATSALDVET 506
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
109-214 |
2.52e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 109 EQAEIQQQVRKMSDYlqiSHllyssvqKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHI 188
Cdd:PRK15134 139 DRVGIRQAAKRLTDY---PH-------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNM 208
|
90 100
....*....|....*....|....*.
gi 489818851 189 PVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK15134 209 GLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
82-195 |
2.68e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.44 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 82 QNLALFpNMNVYENIAFGlkvkkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQK-----------LSGGEKQRVAMARA 150
Cdd:PTZ00265 1303 QEPMLF-NMSIYENIKFG---------KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARA 1372
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489818851 151 MITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTH 195
Cdd:PTZ00265 1373 LLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
11-213 |
3.71e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 11 PFHDL-NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNislHLPVTERKVGYLFQNLALFP 88
Cdd:PRK09700 17 PVHALkSVNLTVYPgEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD---HKLAAQLGIGIIYQELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 89 NMNVYENIAFGLKVKKKK----KKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPF 164
Cdd:PRK09700 94 ELTVLENLYIGRHLTKKVcgvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489818851 165 NGL-DEETRLICMkLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREG 213
Cdd:PRK09700 174 SSLtNKEVDYLFL-IMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
30-214 |
4.14e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKS-TLFQCVSGLKS--IDGGIIEFDGtpwddSNIsLHLPVTE------RKVGYLFQN--LALFPNMNVYENIAF 98
Cdd:PRK09473 49 GESGSGKSqTAFALMGLLAAngRIGGSATFNG-----REI-LNLPEKElnklraEQISMIFQDpmTSLNPYMRVGEQLME 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 GLKVKKKKKKEQAeIQQQVRkMSDYLQISHL-----LYSsvQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRL 173
Cdd:PRK09473 123 VLMLHKGMSKAEA-FEESVR-MLDAVKMPEArkrmkMYP--HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489818851 174 ICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK09473 199 QIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
2-177 |
4.68e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 62.58 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFhDLNIDYtFEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDgtpwdDSNIS-LHLPVterkVGYL 80
Cdd:PRK13541 7 LQFNIEQKNLF-DLSITF-LPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYK-----NCNINnIAKPY----CTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 81 FQNLALFPNMNVYENIAFGLKVKKKKKKEQAEIQqqvrkmsdYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLL 160
Cdd:PRK13541 76 GHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIH--------YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180
....*....|....*....|..
gi 489818851 161 DEPFNGLDEETR-----LICMK 177
Cdd:PRK13541 148 DEVETNLSKENRdllnnLIVMK 169
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-216 |
5.02e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.46 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGlkSIDG---GIIEFDGTPWDDSN--------ISLhLPVTERKVGylfqnlaLFPNMNVYENI-- 96
Cdd:TIGR02633 293 GLVGAGRTELVQALFG--AYPGkfeGNVFINGKPVDIRNpaqairagIAM-VPEDRKRHG-------IVPILGVGKNItl 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 97 ----AFGLKVKKKKKKEQ----AEIQQ-QVRKMSDYLQIShllyssvqKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:TIGR02633 363 svlkSFCFKMRIDAAAELqiigSAIQRlKVKTASPFLPIG--------RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489818851 168 DEETRLICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
30-195 |
6.59e-12 |
|
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: 62.13 E-value: 6.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpvteRKVGYLFQNLALFPNMNVYENIAFGLKVKKKKKKE 109
Cdd:cd03231 33 GPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIA-----RGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 110 QAEIQQQVRKMSDylqishllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETrliCMKLVGQMAKdfHIP 189
Cdd:cd03231 108 EALARVGLNGFED---------RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG---VARFAEAMAG--HCA 173
|
170
....*....|
gi 489818851 190 ----VIFVTH 195
Cdd:cd03231 174 rggmVVLTTH 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-215 |
9.32e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 9.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVtERKVGYLFQN--LALFPNMNVYENIAFGLKVKK 104
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAL-RRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHG 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKKKEQAEiqqqvRKMSDYLQISHLL----YSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVG 180
Cdd:PRK10261 433 LLPGKAAA-----ARVAWLLERVGLLpehaWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 181 QMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
137-215 |
1.59e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.59e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 137 LSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-213 |
1.67e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWD-----DSNislhlpvtERKVGYLFQNLALFPNMNVYENI--- 96
Cdd:PRK10762 32 VMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkSSQ--------EAGIGIIHQELNLIPQLTIAENIflg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 97 -----AFGlkvkkkkKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGL-DEE 170
Cdd:PRK10762 104 refvnRFG-------RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 171 TRLIcMKLVGQMaKDFHIPVIFVTHYASEAEMMTEEILVMREG 213
Cdd:PRK10762 177 TESL-FRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-216 |
3.32e-11 |
|
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: 60.62 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnislhlpvterkVGYLFQNLALFPNMNVYENIAF-----GLK 101
Cdd:cd03220 52 GLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV----------------SSLLGLGGGFNPELTGRENIYLngrllGLS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 vkkkkkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:cd03220 116 --------RKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE 187
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 182 MAKDFHIpVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:cd03220 188 LLKQGKT-VILVSHDPSSIKRLCDRALVLEKGKIR 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
30-171 |
4.07e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsnislhlpVterKVGYLFQNL-ALFPNMNVYENIAFGLkvkkkkkk 108
Cdd:PRK11819 357 GPNGAGKSTLFKMITGQEQPDSGTIKIGET------------V---KLAYVDQSRdALDPNKTVWEEISGGL-------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 109 eqaeiqqqvrkmsDYLQISHLLYSS-----------------VQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET 171
Cdd:PRK11819 414 -------------DIIKVGNREIPSrayvgrfnfkggdqqkkVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-214 |
4.62e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.90 E-value: 4.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 26 TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLhlpvTERKVGYLFQNL--ALFpNMNVYENIAFGlkvK 103
Cdd:PRK13647 34 TALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW----VRSKVGLVFQDPddQVF-SSTVWDDVAFG---P 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 104 KKKKKEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMA 183
Cdd:PRK13647 106 VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLH 185
|
170 180 190
....*....|....*....|....*....|.
gi 489818851 184 KDFHIpVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK13647 186 NQGKT-VIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
25-196 |
4.70e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 60.35 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKS--IDGGIIEFDGtpwddSNIsLHLPVTER-KVG-YL-FQNLALFPNMNVYENIAFG 99
Cdd:TIGR01978 28 IHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKG-----QDL-LELEPDERaRAGlFLaFQYPEEIPGVSNLEFLRSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 100 LKVKKKKKKEQ----AEIQQQVRKMSDYLQIS-HLLYSSVQK-LSGGEKQRVAMARAMITEPKLLLLDEPFNGLD-EETR 172
Cdd:TIGR01978 102 LNARRSARGEEpldlLDFEKLLKEKLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLDiDALK 181
|
170 180
....*....|....*....|....
gi 489818851 173 LICmKLVGQMaKDFHIPVIFVTHY 196
Cdd:TIGR01978 182 IVA-EGINRL-REPDRSFLIITHY 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
14-215 |
4.74e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 61.40 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 14 DLNIDytfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDdsniSLHLPVTERKVGYLFQNLALFPNMNVY 93
Cdd:PRK09536 23 DLSVR---EGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVE----ALSARAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGLKVKKKKKKEQAEIQQQ-VRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETR 172
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489818851 173 LICMKLVGQMAKDFHIpVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK09536 176 VRTLELVRRLVDDGKT-AVAAIHDLDLAARYCDELVLLADGRV 217
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
30-168 |
6.58e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 6.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDdsnislHLPVTER---KVGYL---FQNLALFPNMNVYENIAFGLKVK 103
Cdd:COG3845 291 GVAGNGQSELAEALAGLRPPASGSIRLDGEDIT------GLSPRERrrlGVAYIpedRLGRGLVPDMSVAENLILGRYRR 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 104 KKKKK----EQAEIQQQVRKMSDYLQI-SHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:COG3845 365 PPFSRggflDRKAIRAFAEELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
30-218 |
8.00e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.88 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDsnisLHLPVTERKVGYLFQNLALFPNmNVYENIAFGlkvkkKKKKE 109
Cdd:PRK10789 348 GPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK----LQLDSWRSRLAVVSQTPFLFSD-TVANNIALG-----RPDAT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 110 QAEIQQQVRKMS---DYLQISHLLYSSVQK----LSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:PRK10789 418 QQEIEHVARLASvhdDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
170 180 190
....*....|....*....|....*....|....*.
gi 489818851 183 AKdfHIPVIFVTHYASeAEMMTEEILVMREGRLEKR 218
Cdd:PRK10789 498 GE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQR 530
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
113-184 |
8.19e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 8.19e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489818851 113 IQQQVRK------MSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAK 184
Cdd:PRK10938 106 IQDEVKDparceqLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQ 183
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-214 |
1.32e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.25 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDL--NIDYTFEKPVT-AMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSN---ISLH------ 69
Cdd:PRK10261 18 LNIAFMQEQQKIAAvrNLSFSLQRGETlAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvIELSeqsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 70 -LPVTERKVGYLFQN--LALFPNMNVYENIAFGLKVKKKKKKEQAeiQQQVRKMSDYLQI--SHLLYSSV-QKLSGGEKQ 143
Cdd:PRK10261 98 mRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEA--MVEAKRMLDQVRIpeAQTILSRYpHQLSGGMRQ 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489818851 144 RVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-209 |
1.40e-10 |
|
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: 58.96 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsnislhlpvterKVGYLFQNLALFPNMNVYENIAFGLKVKK 104
Cdd:cd03237 27 VIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD----------------TVSYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKKKEQAEIQQQvrkmsdyLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAK 184
Cdd:cd03237 91 THPYFKTEIAKP-------LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAE 163
|
170 180
....*....|....*....|....*
gi 489818851 185 DFHIPVIFVTHYASEAEMMTEEILV 209
Cdd:cd03237 164 NNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-195 |
1.44e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 60.18 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEfdgtpwddsnislhlpvTERKVGYLFQNLALFPNMNVYENIAFGLKVKK 104
Cdd:COG1245 368 VLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-----------------EDLKISYKPQYISPDYDGTVEEFLRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 KKKKEQAEIqqqVRKmsdyLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAK 184
Cdd:COG1245 431 GSSYYKTEI---IKP----LGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAE 503
|
170
....*....|.
gi 489818851 185 DFHIPVIFVTH 195
Cdd:COG1245 504 NRGKTAMVVDH 514
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-198 |
1.68e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.04 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 12 FHDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGL-KSIDGGIIEFDGTPWDDSNislhLPVTERKVGYLFQNLALFPNm 90
Cdd:PTZ00265 401 YKDLNFTLT-EGKTYAFVGESGCGKSTILKLIERLyDPTEGDIIINDSHNLKDIN----LKWWRSKIGVVSQDPLLFSN- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENIAFGLKVKKKKKKEQAEIQQ------------------------------------QVRKM------SDYLQISH 128
Cdd:PTZ00265 475 SIKNNIKYSLYSLKDLEALSNYYNEdgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNyqtikdSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 129 -----------------LLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVI 191
Cdd:PTZ00265 555 kvlihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
....*..
gi 489818851 192 FVTHYAS 198
Cdd:PTZ00265 635 IIAHRLS 641
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
30-170 |
2.13e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISlhlpvteRKVGYLFQNLALFPNMNVYENIAFGLKVKKKKKKE 109
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS-------RFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQ 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489818851 110 QAEIQQQVRKMSDYLQishllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:PRK13543 117 MPGSALAIVGLAGYED------TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
133-215 |
3.18e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.98 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 133 SVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMRE 212
Cdd:NF000106 141 AAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDR 219
|
...
gi 489818851 213 GRL 215
Cdd:NF000106 220 GRV 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
133-215 |
5.88e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.14 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 133 SVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMRE 212
Cdd:PRK15439 400 AARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQ 478
|
...
gi 489818851 213 GRL 215
Cdd:PRK15439 479 GEI 481
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
30-195 |
9.46e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 9.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDgtpwddsnislhlpvTERKVGYLFQNLALFPNMNVYENIAFGLKvkkkkkkE 109
Cdd:PRK11147 36 GRNGAGKSTLMKILNGEVLLDDGRIIYE---------------QDLIVARLQQDPPRNVEGTVYDFVAEGIE-------E 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 110 QAEiqqqvrKMSDYLQISHLL-----------YSSVQK-------------------------------LSGGEKQRVAM 147
Cdd:PRK11147 94 QAE------YLKRYHDISHLVetdpseknlneLAKLQEqldhhnlwqlenrinevlaqlgldpdaalssLSGGWLRKAAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489818851 148 ARAMITEPKLLLLDEPFNGLDEETrlicMKLVGQMAKDFHIPVIFVTH 195
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISH 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
25-195 |
1.17e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.12 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSG--LKSIDGGIIEFDGTPWDdsnislhlpvterkvgylfqnlalfPNMNVYENIAfglkv 102
Cdd:COG2401 58 IVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFG-------------------------REASLIDAIG----- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 KKKKKKEQAEIQQQVrKMSDylqiSHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:COG2401 108 RKGDFKDAVELLNAV-GLSD----AVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL 182
|
170
....*....|...
gi 489818851 183 AKDFHIPVIFVTH 195
Cdd:COG2401 183 ARRAGITLVVATH 195
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
124-213 |
4.24e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 124 LQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMM 203
Cdd:PRK13409 441 LQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYI 520
|
90 100
....*....|....*....|....*.
gi 489818851 204 TEEILV----------------MREG 213
Cdd:PRK13409 521 SDRLMVfegepgkhghasgpmdMREG 546
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-214 |
4.84e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.49 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 7 HKKLPFHDLNIDYTfEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDdsniSLHLPVTERKVGYLFQNLAL 86
Cdd:PRK10790 352 DDNLVLQNINLSVP-SRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS----SLSHSVLRQGVAMVQQDPVV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 87 FPNmNVYENIAFGLKVKKKK---KKEQAEIQQQVRKMSDylQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEP 163
Cdd:PRK10790 427 LAD-TFLANVTLGRDISEEQvwqALETVQLAELARSLPD--GLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489818851 164 FNGLDEETRLICMKLVGQMAKdfHIPVIFVTHYAS---EAemmtEEILVMREGR 214
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLStivEA----DTILVLHRGQ 551
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
3-168 |
7.68e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 3 RLQFHKKLPFHDLNIDYTFEKpVTAMMGASGSGKSTLFQCVSGlksidggiiEFD---GTPWddsnislhlpvTERKVGY 79
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGK-LTVVLGATGSGKSTLLQSLLS---------QFEiseGRVW-----------AERSIAY 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 80 LFQNlALFPNMNVYENIAFglkvkkKKKKEQAEIQQQVRKM---SDYLQISHLLYSSVQK----LSGGEKQRVAMARAMI 152
Cdd:PTZ00243 726 VPQQ-AWIMNATVRGNILF------FDEEDAARLADAVRVSqleADLAQLGGGLETEIGEkgvnLSGGQKARVSLARAVY 798
|
170
....*....|....*.
gi 489818851 153 TEPKLLLLDEPFNGLD 168
Cdd:PTZ00243 799 ANRDVYLLDDPLSALD 814
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
135-200 |
8.23e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 8.23e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 135 QKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEA 200
Cdd:PRK10938 400 HSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-195 |
8.28e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 8.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSG-LKSIDGgiiefdgtpwddsniSLHLPvTERKVGYLFQNLA-LFPNMNVYENIAFGlkvkk 104
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLMLGqLQADSG---------------RIHCG-TKLEVAYFDQHRAeLDPEKTVMDNLAEG----- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 kkkKEQAEIQQQVRKMSDYLQisHLLYSS------VQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETrlicMKL 178
Cdd:PRK11147 408 ---KQEVMVNGRPRHVLGYLQ--DFLFHPkramtpVKALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET----LEL 478
|
170
....*....|....*..
gi 489818851 179 VGQMAKDFHIPVIFVTH 195
Cdd:PRK11147 479 LEELLDSYQGTVLLVSH 495
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
115-198 |
8.70e-09 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.75 E-value: 8.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 115 QQVRKMSDYLQISHLL-----YSSVQK----LSGGEKQRVAMARAMITEPKLLLLDEPFNGL--DEETRLIcmklvgQMA 183
Cdd:TIGR00954 552 KDLEQILDNVQLTHILereggWSAVQDwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVsvDVEGYMY------RLC 625
|
90
....*....|....*
gi 489818851 184 KDFHIPVIFVTHYAS 198
Cdd:TIGR00954 626 REFGITLFSVSHRKS 640
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-179 |
1.22e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSidGGIIEfdgtpwDDSNISLHLPVTE---RKVGYLFQNLALFPNMNVYENIAFGLK 101
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAGRKT--GGYIE------GDIRISGFPKKQEtfaRISGYCEQNDIHSPQVTVRESLIYSAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKKKEQAEIQQQVRKMSDYLQISHLLYS-----SVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICM 176
Cdd:PLN03140 980 LRLPKEVSKEEKMMFVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
...
gi 489818851 177 KLV 179
Cdd:PLN03140 1060 RTV 1062
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-216 |
1.50e-08 |
|
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: 54.25 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGiiefDGTPWDDSNISlhlpvterKVGYLFQNLALFPNMNVYENIAFGLKVKKKK 106
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSG----DATVAGKSILT--------NISDVHQNMGYCPQFDAIDDLLTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KKEQAEIQQQVRKMSDYlQISHL---LYSS--VQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQ 181
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVANW-SIQSLglsLYADrlAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVS 2115
|
170 180 190
....*....|....*....|....*....|....*
gi 489818851 182 MAKDFHiPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:TIGR01257 2116 IIREGR-AVVLTSHSMEECEALCTRLAIMVKGAFQ 2149
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
28-220 |
1.54e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.15 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIiEFDGTPWDdsniSLHLPVTERKVGYLFQNLALFP-----NMNVYENIAfglKV 102
Cdd:TIGR01271 1250 LLGRTGSGKSTLLSALLRLLSTEGEI-QIDGVSWN----SVTLQTWRKAFGVIPQKVFIFSgtfrkNLDPYEQWS---DE 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 KKKKKKEQAEIQQQVRKMSDYLQIshLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:TIGR01271 1322 EIWKVAEEVGLKSVIEQFPDKLDF--VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS 1399
|
170 180 190
....*....|....*....|....*....|....*...
gi 489818851 183 AKDfhIPVIFVTHYAsEAEMMTEEILVMREGRLEKRKS 220
Cdd:TIGR01271 1400 FSN--CTVILSEHRV-EALLECQQFLVIEGSSVKQYDS 1434
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-214 |
1.62e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 2 LRLQFHKKLPFHDlniDYTFE--KPVTAMM---------GASGSGKSTLFQCVS----GLKSIDGGIIEFDGTPWDDsnI 66
Cdd:TIGR00956 58 LTRGFRKLKKFRD---TKTFDilKPMDGLIkpgeltvvlGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEE--I 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 67 SLHLPvteRKVGYLFQNLALFPNMNVYENIAF-GLKVKKKKKKEQAEIQQQVRKMSDY----LQISHLLYSSV-----QK 136
Cdd:TIGR00956 133 KKHYR---GDVVYNAETDVHFPHLTVGETLDFaARCKTPQNRPDGVSREEYAKHIADVymatYGLSHTRNTKVgndfvRG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 137 LSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAkDFHIPVIFVTHY--ASEAEMMTEEILVMREGR 214
Cdd:TIGR00956 210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSA-NILDTTPLVAIYqcSQDAYELFDKVIVLYEGY 288
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
11-214 |
1.74e-08 |
|
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: 52.61 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 11 PFHDLNIdYTFEKPVTAMMGASGSGKSTLFQCVS----GLKSIDGgiiefDGTPWDDS---------NISLHLPVTERKv 77
Cdd:cd03240 11 SFHERSE-IEFFSPLTLIVGQNGAGKTTIIEALKyaltGELPPNS-----KGGAHDPKliregevraQVKLAFENANGK- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 78 gylfqNLALFPNMNVYENIAFglkvkkkkkKEQAEIQQqvrkmsdylqishLLYSSVQKLSGGEKQ------RVAMARAM 151
Cdd:cd03240 84 -----KYTITRSLAILENVIF---------CHQGESNW-------------PLLDMRGRCSGGEKVlasliiRLALAETF 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 152 ITEPKLLLLDEPFNGLDEETR---LIcmKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGR 214
Cdd:cd03240 137 GSNCGILALDEPTTNLDEENIeesLA--EIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGR 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
30-168 |
1.74e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIE-FDGtpwdDSNISLHLPVTERKVGYLFQNLA--LFPNMNVYENIAF-----GLk 101
Cdd:NF033858 34 GPDGVGKSSLLSLIAGARKIQQGRVEvLGG----DMADARHRRAVCPRIAYMPQGLGknLYPTLSVFENLDFfgrlfGQ- 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489818851 102 vkkkkkkEQAEIQQQvrkmsdylqISHLLYSS---------VQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:NF033858 109 -------DAAERRRR---------IDELLRATglapfadrpAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
28-171 |
2.72e-08 |
|
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: 52.03 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLHlpVTERKVGYLFQNLALFP-----NMNVYEniafglkv 102
Cdd:cd03369 39 IVGRTGAGKSTLILALFRFLEAEEGKIEIDGI--DISTIPLE--DLRSSLTIIPQDPTLFSgtirsNLDPFD-------- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489818851 103 kkkkkkEQAEIQqqvrkMSDYLQIShllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET 171
Cdd:cd03369 107 ------EYSDEE-----IYGALRVS----EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-210 |
3.00e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGiiEFDGTP-WDD-----SNISLHLPVTERKVGYLF-----QNLALFPNM--- 90
Cdd:cd03236 28 VLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPdWDEildefRGSELQNYFTKLLEGDVKvivkpQYVDLIPKAvkg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 91 NVYENIafglkvkkkkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:cd03236 106 KVGELL------------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489818851 171 TRLICMKLVGQMAKDFHiPVIFVTHYASEAEMMTEEILVM 210
Cdd:cd03236 174 QRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
27-195 |
3.47e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 52.97 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKSIDGGIIEfdgtpWDDSNislhlpvterKVGYLFQNLAL-FPN-MNVYENIAfglkvkk 104
Cdd:PRK15064 349 AIIGENGVGKTTLLRTLVGELEPDSGTVK-----WSENA----------NIGYYAQDHAYdFENdLTLFDWMS------- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 kKKKEQAEIQQQVRKMsdylqISHLLYS------SVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEET--RLicm 176
Cdd:PRK15064 407 -QWRQEGDDEQAVRGT-----LGRLLFSqddikkSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESieSL--- 477
|
170 180
....*....|....*....|
gi 489818851 177 klvgQMA-KDFHIPVIFVTH 195
Cdd:PRK15064 478 ----NMAlEKYEGTLIFVSH 493
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
30-201 |
3.64e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.20 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISlhlpvTERKVGYLFQNLALFPNMNVYENIA-----FGLkvkk 104
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIA-----TRRRVGYMSQAFSLYGELTVRQNLElharlFHL---- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 105 kkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAK 184
Cdd:NF033858 370 ----PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSR 445
|
170
....*....|....*...
gi 489818851 185 DFHIpVIFV-THYASEAE 201
Cdd:NF033858 446 EDGV-TIFIsTHFMNEAE 462
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
29-215 |
3.72e-08 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.01 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 29 MGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwddsnislhlpvterKVGYLFQ-NLALFPNMNVYENIAF-----GLKv 102
Cdd:COG1134 58 IGRNGAGKSTLLKLIAGILEPTSGRVEVNG-----------------RVSALLElGAGFHPELTGRENIYLngrllGLS- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 kkkkkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:COG1134 120 -------RKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL 192
|
170 180 190
....*....|....*....|....*....|...
gi 489818851 183 AKDFHIpVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:COG1134 193 RESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
29-168 |
6.01e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 6.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 29 MGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHlpvteRKVGYLFQNLALFPNMNVYENIAFGLKVKKKKKK 108
Cdd:PRK13538 33 EGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYH-----QDLLYLGHQPGIKTELTALENLRFYQRLHGPGDD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 109 EQaeIQQQVRKM--SDYLQIShllyssVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:PRK13538 108 EA--LWEALAQVglAGFEDVP------VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
28-220 |
8.53e-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: 51.39 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIiEFDGTPWDdsniSLHLPVTERKVGYLFQNLALFP-----NMNVYENIAfglKV 102
Cdd:cd03289 35 LLGRTGSGKSTLLSAFLRLLNTEGDI-QIDGVSWN----SVPLQKWRKAFGVIPQKVFIFSgtfrkNLDPYGKWS---DE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 103 KKKKKKEQAEIQQQVRKMSDylQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQM 182
Cdd:cd03289 107 EIWKVAEEVGLKSVIEQFPG--QLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQA 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 489818851 183 akdFHIPVIFVTHYASEAEMMTEEILVMREGRLEKRKS 220
Cdd:cd03289 185 ---FADCTVILSEHRIEAMLECQRFLVIEENKVRQYDS 219
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
30-215 |
9.26e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDG------TPWDDSNISLHLPVTERKVGYLFQNL-----ALFPNMNVYENiAF 98
Cdd:PRK10982 281 GLVGAKRTDIVETLFGIREKSAGTITLHGkkinnhNANEAINHGFALVTEERRSTGIYAYLdigfnSLISNIRNYKN-KV 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 99 GLKvkkkkkkEQAEIQQQVRKMSDYLQI---SHllYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLIC 175
Cdd:PRK10982 360 GLL-------DNSRMKSDTQWVIDSMRVktpGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEI 430
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489818851 176 MKLVGQMAKDfHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10982 431 YQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-213 |
1.64e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 50.02 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLALFpNMNVYENIAFGL---K 101
Cdd:cd03290 29 LTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLL-NATVEENITFGSpfnK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 VKKKKKKEQAEIQQQVRKM--SDYLQISHLLYSsvqkLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKL- 178
Cdd:cd03290 108 QRYKAVTDACSLQPDIDLLpfGDQTEIGERGIN----LSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQEg 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 489818851 179 VGQMAKDFHIPVIFVTH---YASEAEMmteeILVMREG 213
Cdd:cd03290 184 ILKFLQDDKRTLVLVTHklqYLPHADW----IIAMKDG 217
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
30-215 |
2.17e-07 |
|
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: 49.80 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWddSNISLHL-----------PVTERkvGYLFQNLALFpnmNVY--ENI 96
Cdd:cd03244 37 GRTGSGKSSLLLALFRLVELSSGSILIDGVDI--SKIGLHDlrsrisiipqdPVLFS--GTIRSNLDPF---GEYsdEEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 97 AFGLkvkkkkkkEQAEIQQQVRKMSDYLQisHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICM 176
Cdd:cd03244 110 WQAL--------ERVGLKEFVESLPGGLD--TVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQ 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 489818851 177 KLVgqMAKDFHIPVIFVTHYAsEAEMMTEEILVMREGRL 215
Cdd:cd03244 180 KTI--REAFKDCTVLTIAHRL-DTIIDSDRILVLDKGRV 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
122-195 |
3.22e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 3.22e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489818851 122 DYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDfhIPVIFVTH 195
Cdd:PRK13409 198 ERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEG--KYVLVVEH 269
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-168 |
3.74e-07 |
|
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: 49.47 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERkvgylfqnlalfpnmnvyE 94
Cdd:cd03291 55 NINLKIEKgEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIK------------------E 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489818851 95 NIAFGLKVKK---KKKKEQAEIQQQVRKMSDylQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:cd03291 117 NIIFGVSYDEyryKSVVKACQLEEDITKFPE--KDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-215 |
4.02e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 4.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 30 GASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddsnISLHLPVTERKVGYLF-----QNLALFPNMNVYENIA------- 97
Cdd:PRK11288 286 GLVGAGRSELMKLLYGATRRTAGQVYLDGKP-----IDIRSPRDAIRAGIMLcpedrKAEGIIPVHSVADNINisarrhh 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 98 --FGLKVKKKKKKEQAEiqQQVRKM-----SDYLQIshllyssvQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:PRK11288 361 lrAGCLINNRWEAENAD--RFIRSLniktpSREQLI--------MNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVG 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489818851 171 TRLICMKLVGQMAKDfHIPVIFVThyaSE-AEMM--TEEILVMREGRL 215
Cdd:PRK11288 431 AKHEIYNVIYELAAQ-GVAVLFVS---SDlPEVLgvADRIVVMREGRI 474
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
118-195 |
4.88e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.40 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 118 RKMSDY----LQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDfHIPVIFV 193
Cdd:COG1245 190 RGKLDElaekLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVV 268
|
..
gi 489818851 194 TH 195
Cdd:COG1245 269 EH 270
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-217 |
1.36e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 20 TFEKP---VTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwddsnislhlpvterkVGYLFQNlALFPNMNVYENI 96
Cdd:TIGR00957 658 TFSIPegaLVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-----------------VAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 97 AFGLKVkkkkkkeQAEIQQQVRKMSDYLQISHLLYSSVQ--------KLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:TIGR00957 720 LFGKAL-------NEKYYQQVLEACALLPDLEILPSGDRteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489818851 169 EET-RLICMKLVGQMAKDFHIPVIFVTHYASEAEmMTEEILVMREGRLEK 217
Cdd:TIGR00957 793 AHVgKHIFEHVIGPEGVLKNKTRILVTHGISYLP-QVDVIIVMSGGKISE 841
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-215 |
2.23e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 12 FHDLNIDYTFEKPVtAMMGASGSGKSTLfqcvsgLKSIDGGIIEFDGTPWDDSNISLHLPVTERKVGYLFQNLALFPNMN 91
Cdd:PLN03073 525 FKNLNFGIDLDSRI-AMVGPNGIGKSTI------LKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMR 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 92 VYENIAfglkvkkkkkkeqaeiQQQVRKMSDYLQIS-HLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDee 170
Cdd:PLN03073 598 CFPGVP----------------EQKLRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD-- 659
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489818851 171 trLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PLN03073 660 --LDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-170 |
2.29e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGL---KSIDGGIIeFDGTPWDDSNISLhlpvTERK-VGYLFQNLALFPNMNVYENI------ 96
Cdd:NF040905 31 ALCGENGAGKSTLMKVLSGVyphGSYEGEIL-FDGEVCRFKDIRD----SEALgIVIIHQELALIPYLSIAENIflgner 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489818851 97 -AFGLKVKKKKKKEQAEIQQQVRkmsdyLQISHLlySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEE 170
Cdd:NF040905 106 aKRGVIDWNETNRRARELLAKVG-----LDESPD--TLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEE 173
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
138-168 |
2.50e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 2.50e-06
10 20 30
....*....|....*....|....*....|.
gi 489818851 138 SGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
130-178 |
3.33e-06 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 44.15 E-value: 3.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 130 LYSSVQKLSGGEKQR---VAMARAMI----------TEPKLLLLDEPFNGLDEETRLICMKL 178
Cdd:pfam13558 26 TYRRSGGLSGGEKQLlayLPLAAALAaqygsaegrpPAPRLVFLDEAFAKLDEENIRTALEL 87
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
6-217 |
5.82e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 6 FHKKLPFHDLN-IDYT-FEKPVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGtpwDDSNISLhlpvterkvgylfqN 83
Cdd:PRK13546 31 KHKNKTFFALDdISLKaYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---EVSVIAI--------------S 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 84 LALFPNMNVYENIAFGLKVKKKkkkEQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEP 163
Cdd:PRK13546 94 AGLSGQLTGIENIEFKMLCMGF---KRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489818851 164 FNGLDEETRLICMKLVGQMaKDFHIPVIFVTHYASEAEMMTEEILVMREGRLEK 217
Cdd:PRK13546 171 LSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-168 |
7.09e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 46.44 E-value: 7.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPWDDSNISLHLPVTERkvgylfqnlalfpnmnvyE 94
Cdd:TIGR01271 444 NISFKLEKgQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIK------------------D 505
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489818851 95 NIAFGLKVKK---KKKKEQAEIQQQVRKMSDYLQIshLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:TIGR01271 506 NIIFGLSYDEyryTSVIKACQLEEDIALFPEKDKT--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
131-215 |
7.90e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 131 YSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDeetrlicmklVGqmAKdFHI------------PVIFVThyas 198
Cdd:NF040905 399 FQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID----------VG--AK-YEIytiinelaaegkGVIVIS---- 461
|
90 100
....*....|....*....|..
gi 489818851 199 eAEM-----MTEEILVMREGRL 215
Cdd:NF040905 462 -SELpellgMCDRIYVMNEGRI 482
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
136-209 |
8.93e-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: 44.49 E-value: 8.93e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489818851 136 KLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILV 209
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
130-207 |
9.12e-06 |
|
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: 44.27 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 130 LYSSVQKLSGGEKQRVAMARAM----ITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIpVIFVTHYASEAEMMTE 205
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLPELAELADK 149
|
..
gi 489818851 206 EI 207
Cdd:cd03227 150 LI 151
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
136-215 |
9.67e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.50 E-value: 9.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 136 KLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
129-215 |
1.71e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 129 LLYSSVQKLSGGEKQRVAMARAM---------ITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASE 199
Cdd:PRK13547 138 LVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNL 217
|
90
....*....|....*.
gi 489818851 200 AEMMTEEILVMREGRL 215
Cdd:PRK13547 218 AARHADRIAMLADGAI 233
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
27-217 |
2.11e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 27 AMMGASGSGKSTLFQCVSGLKS--IDGGIIEFDGtpwddSNIsLHLPVTER-KVG-YL-FQNLALFPNMNvyeNIAFglk 101
Cdd:CHL00131 37 AIMGPNGSGKSTLSKVIAGHPAykILEGDILFKG-----ESI-LDLEPEERaHLGiFLaFQYPIEIPGVS---NADF--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 102 vkKKKKKEQAEIQQQVRKMS--DYLQI-----------SHLLYSSVQK-LSGGEKQRVAMARAMITEPKLLLLDEPFNGL 167
Cdd:CHL00131 105 --LRLAYNSKRKFQGLPELDplEFLEIineklklvgmdPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAILDETDSGL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489818851 168 D-EETRLICMKLVGQMAKDFHIpvIFVTHYASEAEMMTEE-ILVMREGRLEK 217
Cdd:CHL00131 183 DiDALKIIAEGINKLMTSENSI--ILITHYQRLLDYIKPDyVHVMQNGKIIK 232
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
112-216 |
2.96e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 112 EIQQQVRkmsDYL--------QIShllySSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRlicmKLVGQMA 183
Cdd:PRK10636 405 ELEQKLR---DYLggfgfqgdKVT----EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR----QALTEAL 473
|
90 100 110
....*....|....*....|....*....|...
gi 489818851 184 KDFHIPVIFVTHYASEAEMMTEEILVMREGRLE 216
Cdd:PRK10636 474 IDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVE 506
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-168 |
4.81e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 43.81 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 18 DYTFEKPV---TAMMGASGSGKSTLFQCVSGlksidggiiefDGTPWDDSNIslhlpVTERKVGYLFQNLALFpNMNVYE 94
Cdd:PLN03232 635 DINLEIPVgslVAIVGGTGEGKTSLISAMLG-----------ELSHAETSSV-----VIRGSVAYVPQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489818851 95 NIAFGLKVKKKKKKEQAEIQQQVRKMSdyLQISHLLYSSVQK---LSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:PLN03232 698 NILFGSDFESERYWRAIDVTALQHDLD--LLPGRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-168 |
6.74e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.19 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDytFEKPV---TAMMGASGSGKSTLFQCVSG-LKSIDGGIIEFDGTpwddsnislhlpvterkVGYLFQNLALFpNMN 91
Cdd:PLN03130 635 NIN--LDVPVgslVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-----------------VAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 92 VYENIAFGLKVKKKKKKEQAEIQQQVRKMS-----DYLQISHllySSVQkLSGGEKQRVAMARAMITEPKLLLLDEPFNG 166
Cdd:PLN03130 695 VRDNILFGSPFDPERYERAIDVTALQHDLDllpggDLTEIGE---RGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
..
gi 489818851 167 LD 168
Cdd:PLN03130 771 LD 772
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
22-195 |
8.68e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 42.59 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 22 EKPVTAMMGASGSGKSTLFQCVSGLKSiDGGIIEFDGTPWDDSNIsLHLPVTERK------VGYLFQNLA--LFPNMNVY 93
Cdd:COG4170 32 EGEIRGLVGESGSGKSLIAKAICGITK-DNWHVTADRFRWNGIDL-LKLSPRERRkiigreIAMIFQEPSscLDPSAKIG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 94 ENIAFGLKVKKKK---------KKEQAE-------IQQQVRKMSDYlqiSHllyssvqKLSGGEKQRVAMARAMITEPKL 157
Cdd:COG4170 110 DQLIEAIPSWTFKgkwwqrfkwRKKRAIellhrvgIKDHKDIMNSY---PH-------ELTEGECQKVMIAMAIANQPRL 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 489818851 158 LLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTH 195
Cdd:COG4170 180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISH 217
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
135-177 |
9.49e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 9.49e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 489818851 135 QKLSGGEKQRVAMARAMITEPK--LLLLDEPFNGLDEETRLICMK 177
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
28-168 |
2.71e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 41.31 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGLKSIDGGIIEFDGT---PW-DDSNISLHLPVTE------RKVGYLFQNLALFPNMNVYENIA 97
Cdd:PRK10636 32 LVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlAWvNQETPALPQPALEyvidgdREYRQLEAQLHDANERNDGHAIA 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489818851 98 fgLKVKKKKKKEQAEIQQQVRKMSDYLQISH-LLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLD 168
Cdd:PRK10636 112 --TIHGKLDAIDAWTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
28-215 |
2.76e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.11 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 28 MMGASGSGKSTLFQCVSGL-KSIDGGIIeFDGTPWDDSNislhlPVTERKvgyLFQnlALFPNMNVYENIAFGlkVKKKK 106
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLyQPQSGEIL-LDGKPVTAEQ-----PEDYRK---LFS--AVFTDFHLFDQLLGP--EGKPA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 107 KKEQAEIQQQVRKMSDYLQISHLLYSSVqKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDF 186
Cdd:PRK10522 421 NPALVEKWLERLKMAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEM 499
|
170 180 190
....*....|....*....|....*....|..
gi 489818851 187 HIPVIFVTH---YASEAemmtEEILVMREGRL 215
Cdd:PRK10522 500 GKTIFAISHddhYFIHA----DRLLEMRNGQL 527
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-195 |
3.61e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489818851 137 LSGGEKQ------RVAMARAMITEPKLLLLDEPFNGLDEETRlicMKLVGQMAKDFH-IP-VIFVTH 195
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERR---RKLVDIMERYLRkIPqVIIVSH 852
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
136-205 |
5.05e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.17 E-value: 5.05e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 136 KLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFHIPVIFVTHyasEAEMMTE 205
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISH---DLQMLSQ 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-215 |
6.55e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 39.68 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKStlFQCVSGLKSIDGGI------IEFDGTPWDDSNislhlpVTERKVGYLFQNlalfPN--MNVYENI 96
Cdd:PRK10418 31 VLALVGGSGSGKS--LTCAAALGILPAGVrqtagrVLLDGKPVAPCA------LRGRKIATIMQN----PRsaFNPLHTM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 97 AfglkvkkkkkKEQAEIQQQVRKMSDYLQISHLLYS-------SVQKL-----SGGEKQRVAMARAMITEPKLLLLDEPF 164
Cdd:PRK10418 99 H----------THARETCLALGKPADDATLTAALEAvglenaaRVLKLypfemSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489818851 165 NGLDEETRLICMKLVGQMAKDFHIPVIFVTHYASEAEMMTEEILVMREGRL 215
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
25-196 |
7.18e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 39.39 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLK--SIDGGIIEFDG------TPWDDSN----ISLHLPVTERKVGYLFqnlalFPNMNV 92
Cdd:PRK09580 29 VHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGkdllelSPEDRAGegifMAFQYPVEIPGVSNQF-----FLQTAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 93 YENIAFGLKVKKKKKKEQAEIQQQVR--KMSDylqisHLLYSSVQ-KLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDE 169
Cdd:PRK09580 104 NAVRSYRGQEPLDRFDFQDLMEEKIAllKMPE-----DLLTRSVNvGFSGGEKKRNDILQMAVLEPELCILDESDSGLDI 178
|
170 180
....*....|....*....|....*..
gi 489818851 170 ETRLICMKLVGQMaKDFHIPVIFVTHY 196
Cdd:PRK09580 179 DALKIVADGVNSL-RDGKRSFIIVTHY 204
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
11-43 |
8.09e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.02 E-value: 8.09e-04
10 20 30
....*....|....*....|....*....|...
gi 489818851 11 PFHDLNIDytFEKPVTAMMGASGSGKSTLFQCV 43
Cdd:pfam13476 8 SFRDQTID--FSKGLTLITGPNGSGKTTILDAI 38
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
21-195 |
1.54e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.45 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 21 FEKPVTAMMGASGSGKSTLFQCVS-GL----KSIDGGIIEFDGTPWDDSNISLHLPVTERKvgYL-------FQNLALFP 88
Cdd:COG0419 21 FDDGLNLIVGPNGAGKSTILEAIRyALygkaRSRSKLRSDLINVGSEEASVELEFEHGGKR--YRierrqgeFAEFLEAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 89 NMNVYENIA--FGLKVKKKKKKEQAEIQQQVRKMSDYLQISHLL----------YSSVQKLSGGEKQRVAMARAMitepk 156
Cdd:COG0419 99 PSERKEALKrlLGLEIYEELKERLKELEEALESALEELAELQKLkqeilaqlsgLDPIETLSGGERLRLALADLL----- 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 489818851 157 LLLLDepFNGLDEETRLICMKLVGQMAkdfhipviFVTH 195
Cdd:COG0419 174 SLILD--FGSLDEERLERLLDALEELA--------IITH 202
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
134-196 |
2.48e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 38.34 E-value: 2.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489818851 134 VQKLSGGEKQ------RVAMARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFH-IP-VIFVTHY 196
Cdd:PRK01156 799 IDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdIPqVIMISHH 869
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
140-171 |
3.06e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 37.95 E-value: 3.06e-03
10 20 30
....*....|....*....|....*....|..
gi 489818851 140 GEKQRVAMARAMITEPKLLLLDEPFNGLDEET 171
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINT 190
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
76-167 |
3.50e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 76 KVGYLFQNLALFPNMNVYENIAFGLkvkkkkkkEQAEIQQQVRKMS----DYLQISHLLYSsvqkLSGGEKQRVAMARAM 151
Cdd:PRK00635 757 EVRYKGKNIADILEMTAYEAEKFFL--------DEPSIHEKIHALCslglDYLPLGRPLSS----LSGGEIQRLKLAYEL 824
|
90
....*....|....*....
gi 489818851 152 IT---EPKLLLLDEPFNGL 167
Cdd:PRK00635 825 LApskKPTLYVLDEPTTGL 843
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-199 |
4.85e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 37.56 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 16 NIDYTFEK-PVTAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTPwddSNISLHLPVTERKVGylFQNLALfpnmnvyE 94
Cdd:PRK13545 42 NISFEVPEgEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA---ALIAISSGLNGQLTG--IENIEL-------K 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 95 NIAFGLKvkkkkkkeQAEIQQQVRKMSDYLQISHLLYSSVQKLSGGEKQRVAMARAMITEPKLLLLDEPFNGLDEETRLI 174
Cdd:PRK13545 110 GLMMGLT--------KEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|....*
gi 489818851 175 CMKLVGQMaKDFHIPVIFVTHYASE 199
Cdd:PRK13545 182 CLDKMNEF-KEQGKTIFFISHSLSQ 205
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-215 |
6.63e-03 |
|
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: 36.81 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 9 KLPFHDLNIDY-TFEKPV-------------TAMMGASGSGKSTLFQCVSGLKSIDGGIIEFDGTpwDDSNISLHlpVTE 74
Cdd:cd03288 19 EIKIHDLCVRYeNNLKPVlkhvkayikpgqkVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGI--DISKLPLH--TLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489818851 75 RKVGYLFQNLALFPNmnvyeNIAFGLKVKKK-------KKKEQAEIQQQVRKMSDYLQIshLLYSSVQKLSGGEKQRVAM 147
Cdd:cd03288 95 SRLSIILQDPILFSG-----SIRFNLDPECKctddrlwEALEIAQLKNMVKSLPGGLDA--VVTEGGENFSVGQRQLFCL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489818851 148 ARAMITEPKLLLLDEPFNGLDEETRLICMKLVGQMAKDFhiPVIFVTHYASEAeMMTEEILVMREGRL 215
Cdd:cd03288 168 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTI-LDADLVLVLSRGIL 232
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
25-94 |
7.86e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 36.60 E-value: 7.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489818851 25 VTAMMGASGSGKSTLFQCVSGLKSIDGGIIE---FDGTPWDDSNISLHLPVTERKVGYLFQNLALFPNMNVYE 94
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGltdERSRNGGIGGIPSLLNGIDPKEPIEFEISEFLEDGVRYR 73
|
|
| |
