|
Name |
Accession |
Description |
Interval |
E-value |
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-190 |
1.77e-64 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 198.35 E-value: 1.77e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF-NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRY 79
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNMTVKENLS---AITKLTRRDL-YLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVI 155
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAlplRVTGKSRKEIrRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 503446380 156 ADEPLRYLSEDYRIKVIRLFKYLNQdKGITFLIAT 190
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINR-RGTTVLIAT 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-193 |
4.17e-37 |
|
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: 128.29 E-value: 4.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSF-NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYL 80
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLS---AITKLTRRDLYLS-EEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIA 156
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAfalEVTGVPPREIRKRvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 503446380 157 DEPLRYLSEDYRIKVIRLFKYLNQdKGITFLIATLAS 193
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAK 196
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-190 |
8.16e-35 |
|
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: 122.60 E-value: 8.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSF----NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLR 77
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 78 R-YLGIIFEDIRLISNMTVKEN----LSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFP 152
Cdd:cd03255 81 RrHIGFVFQSFNLLPDLTALENvelpLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 503446380 153 LVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVT 198
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-190 |
5.43e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 117.84 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF----NKRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILL 75
Cdd:COG1136 4 LLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGP-SGsGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LRR-YLGIIFEDIRLISNMTVKEN------LSAITKLTRRDLylSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVI 148
Cdd:COG1136 83 LRRrHIGFVFQFFNLLPELTALENvalpllLAGVSRKERRER--ARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503446380 149 YNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVT 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-190 |
3.14e-26 |
|
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: 100.02 E-value: 3.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRYLG 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-----DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLSAITKLTRRDlylSEEI-------FDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLV 154
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVP---KDEIdervrevAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 503446380 155 IADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVT 188
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-190 |
6.09e-26 |
|
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: 99.93 E-value: 6.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgillLRRYL 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----ARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENL---SAITKLTRRDLYLS-EEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIA 156
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIryfAELYGLFDEELKKRiEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190
....*....|....*....|....*....|....
gi 503446380 157 DEPLRYLSEDYRIKVIRLFKYLNQDkGITFLIAT 190
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKE-GKTVLFSS 189
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-190 |
1.97e-25 |
|
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: 97.98 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgilLLRRYLG 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKEN------LSAITKLTRRDlyLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVI 155
Cdd:cd03259 76 MVFQDYALFPHLTVAENiafglkLRGVPKAEIRA--RVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 503446380 156 ADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03259 154 LDEPLSALDAKLREELREELKELQRELGITTIYVT 188
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-159 |
8.55e-25 |
|
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: 96.80 E-value: 8.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYLG 81
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKEN----LSAITKLTRRDLY-LSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIA 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENvafpLREHTRLSEEEIReIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
...
gi 503446380 157 DEP 159
Cdd:cd03261 161 DEP 163
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-159 |
5.29e-24 |
|
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: 95.05 E-value: 5.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRY 79
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGG-SGsGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNMTVKEN----LSAITKLTRRDLY-LSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLV 154
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENvafpLREHTDLSEAEIReLVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
....*
gi 503446380 155 IADEP 159
Cdd:COG1127 164 LYDEP 168
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-190 |
5.52e-24 |
|
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: 94.57 E-value: 5.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF----NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLL 76
Cdd:cd03258 1 MIELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 77 RRYLGIIFEDIRLISNMTVKENLS---AITKLTRRDLYL-SEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFP 152
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAlplEIAGVPKAEIEErVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 503446380 153 LVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLIT 198
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-190 |
1.49e-23 |
|
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: 92.25 E-value: 1.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgILLLRRYLG 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLSaitkltrrdlylseeifdmlsighlldkYPheLSISEQSLINIARGVIYNFPLVIADEPLR 161
Cdd:cd03229 80 MVFQDFALFPHLTVLENIA----------------------------LG--LSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180
....*....|....*....|....*....
gi 503446380 162 YLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLGITVVLVT 158
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-190 |
3.58e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 92.43 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgillLRRYL 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGP-NGaGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE----VRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLSAITKLTRRDLYLS----EEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIA 156
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEAreriDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190
....*....|....*....|....*....|....
gi 503446380 157 DEPLRYLSEDYRIKVIRLFKYLNqDKGITFLIAT 190
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELA-AEGKTVLLST 188
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-190 |
2.66e-22 |
|
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: 89.90 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDlNYSGILLLRRYLG 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLS-AITKLTRRD----LYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIA 156
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITlAPIKVKGMSkaeaEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190
....*....|....*....|....*....|....
gi 503446380 157 DEPLRYLSEDYRIKVIRLFKYLNQDkGITFLIAT 190
Cdd:cd03262 160 DEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVT 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-190 |
2.84e-22 |
|
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: 90.26 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF----NKRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILL 75
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGE-SGsGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LRRYLGIIFEDIRLISN--MTVK----ENLSAITKLTRRDLYLSEEIFDMLSIG---HLLDKYPHELSISEQSLINIARG 146
Cdd:cd03257 80 RRKEIQMVFQDPMSSLNprMTIGeqiaEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503446380 147 VIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFIT 203
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-190 |
4.02e-22 |
|
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: 90.05 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNK-RTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgILLLRRYL 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQD---PVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLSAITKLT-----RRDLYLSEEIFDM-LSIGHLLDKYPHELSISEQSLINIARGVIYNFPLV 154
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLkwpkeKIRERADELLALVgLDPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 503446380 155 IADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVT 193
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-190 |
2.51e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.77 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANrinQI--ILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDL--Nysgill 75
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPG---EFvaLLGPSGcGKTTLLRMIAGFETPDSGRILLDGRDVTGLppE------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 lRRYLGIIFEDIRLISNMTVKEN----LSA--ITKLTRRDlyLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIY 149
Cdd:COG3842 76 -KRNVGMVFQDYALFPHLTVAENvafgLRMrgVPKAEIRA--RVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503446380 150 NFPLVIADEPLRYLseDY--RIKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG3842 153 EPRVLLLDEPLSAL--DAklREEMREELRRLQRELGITFIYVT 193
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-190 |
4.98e-21 |
|
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: 85.53 E-value: 4.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgillLRRYLG 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE----VKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLsaitkltrrdlylseeifdmlsighlldkyphELSISEQSLINIARGVIYNFPLVIADEPLR 161
Cdd:cd03230 77 YLPEEPSLYENLTVRENL--------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180
....*....|....*....|....*....
gi 503446380 162 YLSEDYRIKVIRLFKYLNqDKGITFLIAT 190
Cdd:cd03230 125 GLDPESRREFWELLRELK-KEGKTILLSS 152
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-190 |
5.19e-21 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.07 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDlNYSGILLLRRYL 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLS----AITKLTRRDLY-LSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVI 155
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMfgplRVRGASKEEAEkQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190
....*....|....*....|....*....|....*
gi 503446380 156 ADEPLRYLSEDYRIKVIRLFKYLnQDKGITFLIAT 190
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVT 193
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-190 |
5.85e-21 |
|
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: 86.91 E-value: 5.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLnysgiLLLRRYLG 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLS---AITKLTRRDLYLS-EEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIAD 157
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAfglRLKKLPKAEIKERvAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190
....*....|....*....|....*....|...
gi 503446380 158 EPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELGITFVFVT 188
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-190 |
8.84e-21 |
|
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: 86.40 E-value: 8.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF----NKRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDfnvSDLNYSGILL 75
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGE-SGsGKSTLLRALAGLERPWSGEVTFDG---RPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LRRYLGIIFEDIRLISN--MTVKENLS---AITKLTRRDlylsEEIFDMLSI----GHLLDKYPHELSISEQSLINIARG 146
Cdd:COG1124 77 FRRRVQMVFQDPYASLHprHTVDRILAeplRIHGLPDRE----ERIAELLEQvglpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 503446380 147 VIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVS 196
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-159 |
3.92e-20 |
|
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: 82.70 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 17 FSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRvfdFNVSDLNYSGILLLRRYLGIIFEDIRLISNMTV 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGP-NGaGKSTLLKLIAGLLSPTEGTIL---LDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503446380 96 KENLsaitKLTRRDLYLS--------EEIFDMLSIGHLLD----KYPHELSISEQSLINIARGVIYNFPLVIADEP 159
Cdd:pfam00005 77 RENL----RLGLLLKGLSkrekdaraEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-188 |
1.21e-19 |
|
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: 83.39 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 3 EFIDVVKSF-NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYLG 81
Cdd:cd03256 2 EVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKEN-----LSAITKL-------TRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIY 149
Cdd:cd03256 82 MIFQQFNLIERLSVLENvlsgrLGRRSTWrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 503446380 150 NFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLI 188
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIV 200
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-190 |
3.13e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.84 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF-NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRY 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNMTVKENLS---AITKLTRRDlyLSEEIFDMLSIGHLLDK---YPHELSISEQSLINIARGVIYNFPL 153
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAiplIIAGASGDD--IRRRVSAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 503446380 154 VIADEPLRYLSEDYRIKVIRLFKYLNQdKGITFLIAT 190
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMAT 194
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-189 |
8.32e-19 |
|
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: 80.34 E-value: 8.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLnysgILLLRRyLGIIFE 85
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN----IEALRR-IGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 DIRLISNMTVKENLSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSE 165
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180
....*....|....*....|....
gi 503446380 166 DyRIKVIRLFKYLNQDKGITFLIA 189
Cdd:cd03268 160 D-GIKELRELILSLRDQGITVLIS 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-190 |
1.11e-18 |
|
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: 83.41 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKR-----TVFSNLSFRIAANRInqI-ILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGI 73
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGET--LgLVGESGsGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 74 LLLRRYLGIIFEDIR--LISNMTVKENLS----AITKLTRRDlyLSEEIFDMLSI----GHLLDKYPHELSISEQSLINI 143
Cdd:COG1123 338 RELRRRVQMVFQDPYssLNPRMTVGDIIAeplrLHGLLSRAE--RRERVAELLERvglpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503446380 144 ARGVIYNFPLVIADEP---LrylseDYRI--KVIRLFKYLNQDKGITFLIAT 190
Cdd:COG1123 416 ARALALEPKLLILDEPtsaL-----DVSVqaQILNLLRDLQRELGLTYLFIS 462
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
32-190 |
1.28e-18 |
|
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: 80.46 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 32 IILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRYLGIIFEDIRLISNMTVKENLSAITKLTRRDLY 111
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 112 LSE----EIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFL 187
Cdd:cd03299 105 EIErkvlEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVL 184
|
...
gi 503446380 188 IAT 190
Cdd:cd03299 185 HVT 187
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-190 |
2.21e-18 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 81.66 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINqIILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRY 79
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFL-VLLGPSGcGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-----DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNMTVKENLSaiTKLTRRDLYLSE------EIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPL 153
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIA--FPLKLRKVPKAEidrrvrEAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKV 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 503446380 154 VIADEPLRYLseDY--RIKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG3839 155 FLLDEPLSNL--DAklRVEMRAEIKRLHRRLGTTTIYVT 191
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-190 |
1.30e-17 |
|
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: 77.86 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKR----TVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILL 75
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGA-SGsGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LR-RYLGIIFEDIRLISNMTVKEN------LSAITKLTRRdlylSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVI 148
Cdd:COG4181 87 LRaRHVGFVFQSFQLLPTLTALENvmlpleLAGRRDARAR----ARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503446380 149 YNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVT 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-163 |
2.68e-17 |
|
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: 76.64 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF--NKRTVFS--NLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSdlnySGILLL 76
Cdd:cd03266 1 MITADALTKRFrdVKKTVQAvdGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 77 RRYLGIIFEDIRLISNMTVKENL---SAITKLTRRDLYLS-EEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFP 152
Cdd:cd03266 77 RRRLGFVSDSTGLYDRLTARENLeyfAGLYGLKGDELTARlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170
....*....|.
gi 503446380 153 LVIADEPLRYL 163
Cdd:cd03266 157 VLLLDEPTTGL 167
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-190 |
5.40e-17 |
|
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: 75.16 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDfnvsdlnysgilllrrylgiife 85
Cdd:cd03214 4 NLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG----------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 diRLISNMTVKEnlsaitkLTRRDLYLSEeIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSE 165
Cdd:cd03214 61 --KDLASLSPKE-------LARKIAYVPQ-ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180
....*....|....*....|....*
gi 503446380 166 DYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03214 131 AHQIELLELLRRLARERGKTVVMVL 155
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-190 |
8.63e-17 |
|
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: 73.82 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 3 EFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgILLLRRYLGI 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 83 IFedirlisnmtvkenlsaitkltrrdlylseeifdmlsighlldkyphELSISEQSLINIARGVIYNFPLVIADEPLRY 162
Cdd:cd00267 78 VP-----------------------------------------------QLSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180
....*....|....*....|....*...
gi 503446380 163 LSEDYRIKVIRLFKYLNQdKGITFLIAT 190
Cdd:cd00267 111 LDPASRERLLELLRELAE-EGRTVIIVT 137
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-190 |
1.77e-16 |
|
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: 74.43 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 13 KRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgILLLRRYLGIIFEDIRL-I 90
Cdd:cd03225 13 ARPALDDISLTIKKGEFVLIVGP-NGsGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKVGLVFQNPDDqF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 91 SNMTVKENLSaitkLTRRDLYLSEE--------IFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRY 162
Cdd:cd03225 89 FGPTVEEEVA----FGLENLGLPEEeieerveeALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180
....*....|....*....|....*...
gi 503446380 163 LSEDYRIKVIRLFKYLNQdKGITFLIAT 190
Cdd:cd03225 165 LDPAGRRELLELLKKLKA-EGKTIIIVT 191
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-181 |
2.76e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 75.89 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRYLG 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR-----DRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLS-AITKLTRRDLYLSEEI-------FDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPL 153
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAfGLTVLPRRERPNAAAIkakvtqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180
....*....|....*....|....*...
gi 503446380 154 VIADEPLRYLSEDYRIKVIRLFKYLNQD 181
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEE 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-163 |
4.55e-16 |
|
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: 73.27 E-value: 4.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSF----NKRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgilll 76
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGP-SGcGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 77 rRYLGIIFEDIRLISNMTVKENLS---AITKLTRRDLY-LSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFP 152
Cdd:cd03293 73 -PDRGYVFQQDALLPWLTVLDNVAlglELQGVPKAEAReRAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170
....*....|.
gi 503446380 153 LVIADEPLRYL 163
Cdd:cd03293 152 VLLLDEPFSAL 162
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-190 |
6.58e-16 |
|
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: 73.53 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgilLLRRYLG 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-----VQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLSAITKLTRRDLYLSE--------EIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPL 153
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEaeirakvhELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 503446380 154 VIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVT 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-190 |
8.88e-16 |
|
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: 74.94 E-value: 8.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFS--NLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPD---SGFVRVFDFNVSDLNysgILL 75
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS---EAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LRRYLGIIFEDIRLISNM-TVKENLS---AITKLTRRDLY-LSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYN 150
Cdd:COG1123 81 RGRRIGMVFQDPMTQLNPvTVGDQIAealENLGLSRAEARaRVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503446380 151 FPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLIT 200
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
6-188 |
1.10e-15 |
|
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: 72.47 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGIllLRRYLGIIFE 85
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--ARLGIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 DIRLISNMTVKENLSAITKLTRRDLYLS--------------EEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNF 151
Cdd:cd03219 83 IPRLFPELTVLENVMVAAQARTGSGLLLararreereareraEELLERVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 503446380 152 PLVIADEPLRYLSEDYRIKVIRLFKYLNqDKGITFLI 188
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELR-ERGITVLL 198
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-190 |
2.71e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.06 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRYLG 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLSAITKLTRRDlylSEEI----FDMLSIGHL---LDKYPHELSISEQSLINIARGVIyNFPLV 154
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAFGLRMQKTP---AAEItprvMEALRMVQLeefAQRKPHQLSGGQQQRVAIARAVV-NKPKV 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 503446380 155 -IADEPLRYLseDYRI-KVIRL-FKYLNQDKGITFLIAT 190
Cdd:PRK09452 166 lLLDESLSAL--DYKLrKQMQNeLKALQRKLGITFVFVT 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-159 |
3.42e-15 |
|
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: 70.77 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGIlllrrylG 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRI-------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLSAITKL---TRRD-LYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIAD 157
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLAQLkglKKEEaRRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
..
gi 503446380 158 EP 159
Cdd:cd03269 154 EP 155
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
15-190 |
5.00e-15 |
|
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: 71.37 E-value: 5.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 15 TVFSNLSFRIAANRiNQIILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYLGIIFEDI------ 87
Cdd:TIGR02769 25 PVLTNVSLSIEEGE-TVGLLGRSGcGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVFQDSpsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 88 RLISNMTVKENLSAITKLTR-RDLYLSEEIFDMLSI-GHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSE 165
Cdd:TIGR02769 104 RMTVRQIIGEPLRHLTSLDEsEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
|
170 180
....*....|....*....|....*
gi 503446380 166 DYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:TIGR02769 184 VLQAVILELLRKLQQAFGTAYLFIT 208
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
6-190 |
1.03e-14 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 71.22 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRYLGIIFE 85
Cdd:TIGR03265 9 NIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ-----KRDYGIVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 DIRLISNMTVKEN----LSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLR 161
Cdd:TIGR03265 84 SYALFPNLTVADNiaygLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLS 163
|
170 180
....*....|....*....|....*....
gi 503446380 162 YLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:TIGR03265 164 ALDARVREHLRTEIRQLQRRLGVTTIMVT 192
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-134 |
2.06e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKR----TVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILL 75
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGY-SGaGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503446380 76 LRRYLGIIFEDIRLISNMTVKEN------LSAITKLTRRdlylsEEIFDMLSIGHLLDK---YPHELS 134
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENvalpleIAGVPKAEIR-----KRVAELLELVGLSDKadaYPSQLS 142
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
14-190 |
5.11e-14 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 68.56 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 14 RTVFSNLSFRIAANRiNQIILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYLGIIFED------ 86
Cdd:PRK10419 25 QTVLNNVSLSLKSGE-TVALLGRSGcGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsisavn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 87 ----IRLIsnmtVKENLSAITKLTRRD-LYLSEEIFDMLSIG-HLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPL 160
Cdd:PRK10419 104 prktVREI----IREPLRHLLSLDKAErLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190
....*....|....*....|....*....|
gi 503446380 161 RYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFIT 209
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-201 |
6.18e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 6.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgiLLLRRYL 80
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLSAITKLTRRDLYL-----------SEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIY 149
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKVCGVniidwremrvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503446380 150 NFPLVIADEPLRYLSE---DYRIKVIRLFKylNQDKGITFLIATLASIDD--DFYTV 201
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNkevDYLFLIMNQLR--KEGTAIVYISHKLAEIRRicDRYTV 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-159 |
8.52e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 68.70 E-value: 8.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSdlnySGILLLRRYLG 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP----ARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLSAITKLTRRDLYLSEEIF-DMLSIGHL---LDKYPHELSISEQSLINIARGVIYNFPLVIAD 157
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIpSLLEFARLeskADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
..
gi 503446380 158 EP 159
Cdd:PRK13536 198 EP 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-190 |
9.97e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 67.09 E-value: 9.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVfsNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRYL 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-----ERPV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKEN----LSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIA 156
Cdd:COG3840 74 SMLFQENNLFPHLTVAQNiglgLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190
....*....|....*....|....*....|....
gi 503446380 157 DEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELCRERGLTVLMVT 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
16-190 |
1.03e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.98 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 16 VFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRR-YLGIIFEDIRLISNMT 94
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRReHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 95 VKENL------SAITKLTRRDlyLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYR 168
Cdd:PRK10535 103 AAQNVevpavyAGLERKQRLL--RAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180
|
170 180
....*....|....*....|..
gi 503446380 169 IKVIRLFKYLnQDKGITFLIAT 190
Cdd:PRK10535 181 EEVMAILHQL-RDRGHTVIIVT 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-190 |
1.28e-13 |
|
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: 67.01 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSdlnySGILLLRRYLGIIFE 85
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 DIRLISNMTVKENLSAITKL--------TRRdlylSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIAD 157
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLygvpgaerRER----IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190
....*....|....*....|....*....|...
gi 503446380 158 EPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTT 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-187 |
1.62e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIIlpqsG----GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYS----- 71
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALL----GengaGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 72 GIlllrrylGIIFEDIRLISNMTVKENL---SAITK---LTRRDLY-LSEEIFDMLSIGHLLDKYPHELSISEQSLINIA 144
Cdd:COG1129 80 GI-------AIIHQELNLVPNLSVAENIflgREPRRgglIDWRAMRrRARELLARLGLDIDPDTPVGDLSVAQQQLVEIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503446380 145 RGVIYNFPLVIADEPLRYLSEDyriKVIRLFKYLNQ--DKGITFL 187
Cdd:COG1129 153 RALSRDARVLILDEPTASLTER---EVERLFRIIRRlkAQGVAII 194
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-172 |
1.72e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.08 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNV-SDLNYSG----ILL 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQqkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LRRYLGIIFEDIRLISNMTVKENL---SAITKLTRRD--LYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYN 150
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIiegPVIVKGEPKEeaTARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 503446380 151 FPLVIADEP---------------LRYLSEDYRIKVI 172
Cdd:PRK11264 163 PEVILFDEPtsaldpelvgevlntIRQLAQEKRTMVI 199
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
10-181 |
2.06e-13 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 67.71 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 10 SFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFdfnVSDLNYSGILLLRRYLGIIFEDIRL 89
Cdd:TIGR03258 14 AYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGLTGRIA---IADRDLTHAPPHKRGLALLFQNYAL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 90 ISNMTVKENLSAITKLTRRDLYL-SEEIFDMLSIGHLLD---KYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSE 165
Cdd:TIGR03258 91 FPHLKVEDNVAFGLRAQKMPKADiAERVADALKLVGLGDaaaHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDA 170
|
170
....*....|....*.
gi 503446380 166 DYRIKVIRLFKYLNQD 181
Cdd:TIGR03258 171 NIRANMREEIAALHEE 186
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-190 |
3.11e-13 |
|
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: 66.26 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGF-VRVFDF-----NVSDLnysgil 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGErrggeDVWEL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 75 llRRYLGI----IFEDIRliSNMTVKEN-LSAIT-------KLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLIN 142
Cdd:COG1119 77 --RKRIGLvspaLQLRFP--RDETVLDVvLSGFFdsiglyrEPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503446380 143 IARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVT 200
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-60 |
4.33e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.07 E-value: 4.33e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRV 60
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-190 |
5.63e-13 |
|
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: 64.82 E-value: 5.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 20 LSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRYLGIIFEDIRLISNMTVKEN- 98
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQENNLFAHLTVEQNv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 99 ---LSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLF 175
Cdd:cd03298 92 glgLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170
....*....|....*
gi 503446380 176 KYLNQDKGITFLIAT 190
Cdd:cd03298 172 LDLHAETKMTVLMVT 186
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-60 |
6.28e-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: 66.50 E-value: 6.28e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRV 60
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
37-189 |
6.50e-13 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.91 E-value: 6.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 37 SG-GKSTIIRMIYGAEKPDSGFVRvFD-FNVSDLNYSGILLLRRYLGIIFEDIR--LISNMTVKENLSA---I-TKLTRR 108
Cdd:COG4608 53 SGcGKSTLGRLLLRLEEPTSGEIL-FDgQDITGLSGRELRPLRRRMQMVFQDPYasLNPRMTVGDIIAEplrIhGLASKA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 109 DLylSEEIFDMLS-IG----HLlDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLseDYRIK--VIRLFKYLNQD 181
Cdd:COG4608 132 ER--RERVAELLElVGlrpeHA-DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL--DVSIQaqVLNLLEDLQDE 206
|
....*....
gi 503446380 182 KGITFL-IA 189
Cdd:COG4608 207 LGLTYLfIS 215
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-145 |
6.94e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 65.98 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF----NKRTVFSNLSFRIAANRINQIIlPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILL 75
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVI-GASGaGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503446380 76 LRRYLGIIFEDIRLISNMTVKENLSAITKLTRRDlylSEEI-------FDMLSIGHLLDKYPHELSISEQSLINIAR 145
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTP---KAEIkarvtelLELVGLSDKADRYPAQLSGGQKQRVAIAR 153
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-159 |
8.88e-13 |
|
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: 64.49 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGilllRRYLGIIF- 84
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 85 -EDIRLISNMTVKENLSAI----TKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEP 159
Cdd:cd03218 81 pQEASIFRKLTVEENILAVleirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-159 |
1.31e-12 |
|
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: 64.06 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNK--RTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSdlnySGILLLRRY 79
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNMTVKENL---SAITKLTRRDLYL-SEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVI 155
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLrfyARLKGLPKSEIKEeVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
....
gi 503446380 156 ADEP 159
Cdd:cd03263 157 LDEP 160
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-190 |
1.77e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.22 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 5 IDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSG----------FVRVFDFNVSDLNYSGIL 74
Cdd:PRK10619 9 IDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGsivvngqtinLVRDKDGQLKVADKNQLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 75 LLRRYLGIIFEDIRLISNMTVKEN----------LSAITKLTRRDLYLSEEIFDMLSIGhlldKYPHELSISEQSLINIA 144
Cdd:PRK10619 89 LLRTRLTMVFQHFNLWSHMTVLENvmeapiqvlgLSKQEARERAVKYLAKVGIDERAQG----KYPVHLSGGQQQRVSIA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503446380 145 RGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDkGITFLIAT 190
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVT 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-190 |
2.01e-12 |
|
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: 63.32 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 3 EFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDlnysgillLRRYLGI 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK--------ERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 83 I--FEDIRLISNMTVKE--------NLSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFP 152
Cdd:cd03235 73 VpqRRSIDRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPD 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 503446380 153 LVIADEPLRYLSEDYRIKVIRLFKYLNQdKGITFLIAT 190
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVT 189
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
35-190 |
4.01e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.11 E-value: 4.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 35 PQSGGKSTIIRMIYGAEKPDSGFVRV----FDFNvSDLNYSGILLLRRYLGIIFEDIRLISNMTVKENLsaiTKLTRRDL 110
Cdd:PRK11124 36 PSGAGKSSLLRVLNLLEMPRSGTLNIagnhFDFS-KTPSDKAIRELRRNVGMVFQQYNLWPHLTVQQNL---IEAPCRVL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 111 YLSE--------EIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLnQDK 182
Cdd:PRK11124 112 GLSKdqalaraeKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AET 190
|
....*...
gi 503446380 183 GITFLIAT 190
Cdd:PRK11124 191 GITQVIVT 198
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
6-159 |
4.97e-12 |
|
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: 63.05 E-value: 4.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRInQIILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRR-YLGII 83
Cdd:cd03294 29 EILKKTGQTVGVNDVSLDVREGEI-FVIMGLSGsGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 84 FEDIRLISNMTVKEN------LSAITKLTRRDlyLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIAD 157
Cdd:cd03294 108 FQSFALLPHRTVLENvafgleVQGVPRAEREE--RAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
..
gi 503446380 158 EP 159
Cdd:cd03294 186 EA 187
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
37-160 |
5.07e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 63.74 E-value: 5.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 37 SG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDlNYSGILLL--RRYLGIIFEDIRLISNMTVKENLSAITKLTRRDLYLS 113
Cdd:PRK11144 33 SGaGKTSLINAISGLTRPQKGRIVLNGRVLFD-AEKGICLPpeKRRIGYVFQDARLFPHYKVRGNLRYGMAKSMVAQFDK 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 503446380 114 eeIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPL 160
Cdd:PRK11144 112 --IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
16-190 |
5.47e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.53 E-value: 5.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 16 VFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLR-RYLGIIFEDIRLISNMT 94
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRnQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 95 VKENLSA---ITKLTRRDLylSEEIFDMLS---IGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYR 168
Cdd:PRK11629 104 ALENVAMpllIGKKKPAEI--NSRALEMLAavgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNA 181
|
170 180
....*....|....*....|..
gi 503446380 169 IKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK11629 182 DSIFQLLGELNRLQGTAFLVVT 203
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-168 |
1.39e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVrVFDfnvsDLNYSGILLLRRYL 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-MLD----GVDLSHVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLS---AITKLTRRDlyLSEEIFDMLSIGHLLD---KYPHELSISEQSLINIARGVIYNFPLV 154
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAfglKQDKLPKAE--IASRVNEMLGLVHMQEfakRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170
....*....|....
gi 503446380 155 IADEPLRYLSEDYR 168
Cdd:PRK11607 172 LLDEPMGALDKKLR 185
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-174 |
2.66e-11 |
|
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: 60.53 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFN-------KRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRV-FDFNVSDL--- 68
Cdd:COG4778 4 LLEVENLSKTFTlhlqggkRLPVLDGVSFSVAAGECVALTGP-SGaGKSTLLKCIYGNYLPDSGSILVrHDGGWVDLaqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 69 NYSGILLLRRY-LGIIFEDIRLISNMT----VKENL-----SAITKLTRrdlylSEEIFDMLSI-GHLLDKYPHELSISE 137
Cdd:COG4778 83 SPREILALRRRtIGYVSQFLRVIPRVSaldvVAEPLlergvDREEARAR-----ARELLARLNLpERLWDLPPATFSGGE 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 503446380 138 QSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRL 174
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVEL 194
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-190 |
3.34e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 61.27 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGfvRVFdFNVSDLNYSGIllLRRYLG 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEG--QIF-IDGEDVTHRSI--QQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLSAITKLTRRDlylSEEI-------FDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLV 154
Cdd:PRK11432 82 MVFQSYALFPHMSLGENVGYGLKMLGVP---KEERkqrvkeaLELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 503446380 155 IADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVT 194
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-189 |
3.45e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 61.52 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSF-NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGillLRRYL 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS---LRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLIsNMTVKENLSaITKLTRRDlylsEEIFDMLSIGHLLD---KYPH-----------ELSISEQSLINIARG 146
Cdd:PRK13657 412 AVVFQDAGLF-NRSIEDNIR-VGRPDATD----EEMRAAAERAQAHDfieRKPDgydtvvgergrQLSGGERQRLAIARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503446380 147 VIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKgITFLIA 189
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMKGR-TTFIIA 527
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-198 |
3.92e-11 |
|
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: 61.36 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 19 NLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSG--FVRVFDFNVsDLNYSGILL---LRRYLGIIFEDIRLISNM 93
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEWV-DMTKPGPDGrgrAKRYIGILHQEYDLYPHR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 94 TVKENLS-AITKLTRRDLYLSEEIFDMLSIG-------HLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSE 165
Cdd:TIGR03269 381 TVLDNLTeAIGLELPDELARMKAVITLKMVGfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDP 460
|
170 180 190
....*....|....*....|....*....|...
gi 503446380 166 DYRIKVIRLFKYLNQDKGITFLIatlASIDDDF 198
Cdd:TIGR03269 461 ITKVDVTHSILKAREEMEQTFII---VSHDMDF 490
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-190 |
9.28e-11 |
|
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: 59.27 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 4 FIDVVKSFNKR-----TVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFnvsdLNYSGILLLRR 78
Cdd:cd03267 19 LIGSLKSLFKRkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 79 YLGIIF-EDIRLISNMTVKENLS---AITKLT----RRDLylsEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYN 150
Cdd:cd03267 95 RIGVVFgQKTQLWWDLPVIDSFYllaAIYDLPparfKKRL---DELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503446380 151 FPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTS 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-188 |
1.09e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.14 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGilLLRRYLGIIFE 85
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 DIRLISNMTVKENLSAITKLtRRDLYL------SEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEP 159
Cdd:PRK10895 86 EASIFRRLSVYDNLMAVLQI-RDDLSAeqredrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180
....*....|....*....|....*....
gi 503446380 160 LRYLSEDYRIKVIRLFKYLnQDKGITFLI 188
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHL-RDSGLGVLI 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-179 |
1.91e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 59.27 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRRYLG 81
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-----ERGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISNMTVKENLSAITKLTRRDlylSEEI-------FDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLV 154
Cdd:PRK11000 79 MVFQSYALYPHLSVAENMSFGLKLAGAK---KEEInqrvnqvAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
|
170 180
....*....|....*....|....*....
gi 503446380 155 IADEPLRYLSE----DYRIKVIRLFKYLN 179
Cdd:PRK11000 156 LLDEPLSNLDAalrvQMRIEISRLHKRLG 184
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-160 |
2.31e-10 |
|
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: 57.50 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 14 RTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRvfdfnvsdLNYSGillLRRYLGIIFEDIRLISNM 93
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL--------LNGGP---LDFQRDSIARGLLYLGHA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503446380 94 T-VKENLSAITKLT-RRDLYLSEEIFDMLS---IGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPL 160
Cdd:cd03231 82 PgIKTTLSVLENLRfWHADHSDEQVEEALArvgLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-159 |
2.58e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 58.58 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGIlllrRYL 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRI----GYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GiifEDIRLISNMTVKENLSAITKLtrRDLYLSE------EIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLV 154
Cdd:COG4152 77 P---EERGLYPKMKVGEQLVYLARL--KGLSKAEakrradEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
....*
gi 503446380 155 IADEP 159
Cdd:COG4152 152 ILDEP 156
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-190 |
2.73e-10 |
|
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: 57.60 E-value: 2.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFN--KRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilLLRRY 79
Cdd:cd03245 3 IEFRNVSFSYPnqEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPA---DLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNmTVKENLsaitklTRRDLYLSEE----IFDMLSIGHLLDKYPH--ELSISEQ---------SLINIA 144
Cdd:cd03245 80 IGYVPQDVTLFYG-TLRDNI------TLGAPLADDErilrAAELAGVTDFVNKHPNglDLQIGERgrglsggqrQAVALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503446380 145 RGVIYNFPLVIADEP---LRYLSEDYRIKviRLFKYLnqdKGITFLIAT 190
Cdd:cd03245 153 RALLNDPPILLLDEPtsaMDMNSEERLKE--RLRQLL---GDKTLIIIT 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-159 |
1.08e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.65 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 12 NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRvfdFNVSDLNYSGILLLRRYLGiiFEDIrLIS 91
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK---LDGGDIDDPDVAEACHYLG--HRNA-MKP 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503446380 92 NMTVKENLS---AITKLTRRDLYLSEEIFDMLSIGHLLDKYpheLSISEQSLINIARGVIYNFPLVIADEP 159
Cdd:PRK13539 87 ALTVAENLEfwaAFLGGEELDIAAALEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEP 154
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-190 |
1.12e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.30 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFS--NLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGIlllRR 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFTlkDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL---RK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 79 YLGIIFE--DIRLISNmTVK-------ENLSAITKLTRRDLYLSEEIFDMLSIGhllDKYPHELSISEQSLINIARGVIY 149
Cdd:PRK13648 84 HIGIVFQnpDNQFVGS-IVKydvafglENHAVPYDEMHRRVSEALKQVDMLERA---DYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503446380 150 NFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISIT 200
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-158 |
1.82e-09 |
|
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: 55.31 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFN-KRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilLLRRYL 80
Cdd:cd03254 3 IEFENVNFSYDeKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK---SLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNmTVKENLSAITKLTRRDLYlsEEIFDMLSIGHLLDKYP-----------HELSISEQSLINIARGVIY 149
Cdd:cd03254 80 GVVLQDTFLFSG-TIMENIRLGRPNATDEEV--IEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLR 156
|
....*....
gi 503446380 150 NFPLVIADE 158
Cdd:cd03254 157 DPKILILDE 165
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
33-159 |
1.95e-09 |
|
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: 55.55 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 33 ILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGIlllrrylgIIFEDIRLISNMTVKENLSAITKLTRRDLY 111
Cdd:TIGR01184 16 LIGHSGcGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVRENIALAVDRVLPDLS 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 503446380 112 LSE------EIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEP 159
Cdd:TIGR01184 88 KSErraiveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEP 141
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-187 |
2.18e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.74 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 36 QSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYLGIIFEDI------RLISNMTVKENLSAITKLT-- 106
Cdd:PRK11308 49 ESGcGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNPygslnpRKKVGQILEEPLLINTSLSaa 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 107 -RRdlylsEEIFDMLS-IG----HLlDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQ 180
Cdd:PRK11308 129 eRR-----EKALAMMAkVGlrpeHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
....*..
gi 503446380 181 DKGITFL 187
Cdd:PRK11308 203 ELGLSYV 209
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-195 |
2.56e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 9 KSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIR----MIYGAEKPDSgFVRVFDFNVS-------DLNYSgilllR 77
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGS-HIELLGRTVQregrlarDIRKS-----R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 78 RYLGIIFEDIRLISNMTVKENL------------SAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIAR 145
Cdd:PRK09984 86 ANTGYIFQQFNLVNRLSVLENVligalgstpfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503446380 146 GVIYNFPLVIADEPLRYLS-EDYRIkVIRLFKYLNQDKGITfLIATLASID 195
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDpESARI-VMDTLRDINQNDGIT-VVVTLHQVD 214
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-196 |
5.37e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 54.20 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 20 LSFRIAANRINQI-ILPQSG-GKSTIIRMIYGAEKPDSGFVRVfdfNVSDLNYSGIllLRRYLGIIFEDIRLISNMTVKE 97
Cdd:PRK10771 16 MRFDLTVERGERVaILGPSGaGKSTLLNLIAGFLTPASGSLTL---NGQDHTTTPP--SRRPVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 98 N----LSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIR 173
Cdd:PRK10771 91 NiglgLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180
....*....|....*....|...
gi 503446380 174 LFKYLNQDKGITFLIATlASIDD 196
Cdd:PRK10771 171 LVSQVCQERQLTLLMVS-HSLED 192
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-180 |
6.18e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.25 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 10 SFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDfnvSDLNYSGILLLRRYLGIIFEDIRL 89
Cdd:PRK11231 11 GYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD---KPISMLSSRQLARRLALLPQHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 90 ISNMTVKE--------NLSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLR 161
Cdd:PRK11231 88 PEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170
....*....|....*....
gi 503446380 162 YLSEDYRIKVIRLFKYLNQ 180
Cdd:PRK11231 168 YLDINHQVELMRLMRELNT 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-187 |
7.01e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 7.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYLgiIFE 85
Cdd:PRK15439 16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL--VPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 DIRLISNMTVKENLSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSE 165
Cdd:PRK15439 94 EPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTP 173
|
170 180
....*....|....*....|....*.
gi 503446380 166 dyrIKVIRLF----KYLNQDKGITFL 187
Cdd:PRK15439 174 ---AETERLFsrirELLAQGVGIVFI 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-159 |
8.12e-09 |
|
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: 54.39 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 14 RTVFSNLSFRIAAN-RInqIILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGillLRRYLGIIFEDIRLIs 91
Cdd:COG4987 348 RPVLDGLSLTLPPGeRV--AIVGPSGsGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD---LRRRIAVVPQRPHLF- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 92 NMTVKENLsaitKLTRRDLylS-EEIFDMLS---IGHLLDKYPHEL---------SIS--EQSLINIARGVIYNFPLVIA 156
Cdd:COG4987 422 DTTLRENL----RLARPDA--TdEELWAALErvgLGDWLAALPDGLdtwlgeggrRLSggERRRLALARALLRDAPILLL 495
|
...
gi 503446380 157 DEP 159
Cdd:COG4987 496 DEP 498
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
33-199 |
9.05e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 53.57 E-value: 9.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 33 ILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSdlnYSgilllRRYLGIIFEdirlisnMTVKENLSAITKLTRRDLY 111
Cdd:cd03237 30 ILGPNGiGKTTFIKMLAGVLKPDEGDIEIELDTVS---YK-----PQYIKADYE-------GTVRDLLSSITKDFYTHPY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 112 LSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRI---KVIRLFkYLNQDKgitfli 188
Cdd:cd03237 95 FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLmasKVIRRF-AENNEK------ 167
|
170
....*....|.
gi 503446380 189 aTLASIDDDFY 199
Cdd:cd03237 168 -TAFVVEHDII 177
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
39-190 |
9.62e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 53.70 E-value: 9.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 39 GKSTIIRMIYGAEKPDSGfvRVFdFNVSDLNYS--GILLLRRYLGIIFE--DIRLISNMTVKE------NLSAITKLTRR 108
Cdd:PRK13636 44 GKSTLFQNLNGILKPSSG--RIL-FDGKPIDYSrkGLMKLRESVGMVFQdpDNQLFSASVYQDvsfgavNLKLPEDEVRK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 109 DLylsEEIFDMLSIGHLLDKYPHELSISEQSLINIArGVIYNFPLV-IADEPLRYLSEDYRIKVIRLFKYLNQDKGITFL 187
Cdd:PRK13636 121 RV---DNALKRTGIEHLKDKPTHCLSFGQKKRVAIA-GVLVMEPKVlVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTII 196
|
...
gi 503446380 188 IAT 190
Cdd:PRK13636 197 IAT 199
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-134 |
1.11e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.11 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgiLLLRRYLGI--- 82
Cdd:COG1137 8 NLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----MHKRARLGIgyl 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503446380 83 -----IFEDirlisnMTVKENLSAI---TKLTRRDLY-LSEEIFDMLSIGHLLDKYPHELS 134
Cdd:COG1137 84 pqeasIFRK------LTVEDNILAVlelRKLSKKEREeRLEELLEEFGITHLRKSKAYSLS 138
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
36-189 |
1.13e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.94 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 36 QSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYLGIIFED--IRLISNMTVKENLSAITKLTRRDLYl 112
Cdd:PRK15079 55 ESGcGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLRTYHPKLS- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 113 SEEIFD-----MLSIG---HLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGI 184
Cdd:PRK15079 134 RQEVKDrvkamMLKVGllpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGL 213
|
....*.
gi 503446380 185 TFL-IA 189
Cdd:PRK15079 214 SLIfIA 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-60 |
1.57e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 53.53 E-value: 1.57e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAAN-RINqIILPQSGGKSTIIRMIYGAEKPDSGFVRV 60
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGdRIG-LIGPNGAGKSTLLKLLAGELEPDSGTVKL 374
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-190 |
1.58e-08 |
|
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: 53.68 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVvkSF----NKRTVFSNLSFRIAAN-RInqIILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilL 75
Cdd:COG2274 474 IELENV--SFrypgDSPPVLDNISLTIKPGeRV--AIVGRSGsGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPA---S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LRRYLGIIFEDIRLISnMTVKENLSaitkLTRRDLYLSE--EIFDMLSIGHLLDKYPH--ELSISEQS---------LIN 142
Cdd:COG2274 547 LRRQIGVVLQDVFLFS-GTIRENIT----LGDPDATDEEiiEAARLAGLHDFIEALPMgyDTVVGEGGsnlsggqrqRLA 621
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503446380 143 IARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKgiTFLIAT 190
Cdd:COG2274 622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIA 667
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
39-203 |
1.59e-08 |
|
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: 53.63 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 39 GKSTIIRMIYGAEKPDSGFVrvfDFNVsDLNYSGilllrRYLGIIFEdirlisnMTVKENLSAITKLTRRDLYLSEEIFD 118
Cdd:COG1245 378 GKTTFAKILAGVLKPDEGEV---DEDL-KISYKP-----QYISPDYD-------GTVEEFLRSANTDDFGSSYYKTEIIK 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 119 MLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIatlasIDDDF 198
Cdd:COG1245 442 PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMV-----VDHDI 516
|
....*
gi 503446380 199 YTVEL 203
Cdd:COG1245 517 YLIDY 521
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-187 |
1.72e-08 |
|
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: 51.66 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRInQIILPQSG-GKSTIIRMIYGAEKPDSGFVRV----FDF-NVSDLNYSGIll 75
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEV-HALLGENGaGKSTLMKILSGLYKPDSGEILVdgkeVSFaSPRDARRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 lrrylGIIfedirlisnmtvkenlsaitkltrrdlylseeifdmlsighlldkypHELSISEQSLINIARGVIYNFPLVI 155
Cdd:cd03216 78 -----AMV-----------------------------------------------YQLSVGERQMVEIARALARNARLLI 105
|
170 180 190
....*....|....*....|....*....|....
gi 503446380 156 ADEPLRYLSEDyriKVIRLFKYLNQ--DKGITFL 187
Cdd:cd03216 106 LDEPTAALTPA---EVERLFKVIRRlrAQGVAVI 136
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
14-190 |
2.18e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.88 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 14 RTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgILLLRRYLGIIFE--DIRLIS 91
Cdd:PRK13652 17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN---IREVRKFVGLVFQnpDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 92 NmTVKE-------NLSAITKLTRRDLylsEEIFDMLSIGHLLDKYPHELSISEQSLINIArGVIYNFPLV-IADEPLRYL 163
Cdd:PRK13652 94 P-TVEQdiafgpiNLGLDEETVAHRV---SSALHMLGLEELRDRVPHHLSGGEKKRVAIA-GVIAMEPQVlVLDEPTAGL 168
|
170 180
....*....|....*....|....*..
gi 503446380 164 SEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK13652 169 DPQGVKELIDFLNDLPETYGMTVIFST 195
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-190 |
2.34e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.37 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDlnysgillLRRYLGIIFE 85
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE--------AREDTRLMFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 DIRLISNMTVKENLSAITKLTRRDLYLseEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSE 165
Cdd:PRK11247 89 DARLLPWKKVIDNVGLGLKGQWRDAAL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180
....*....|....*....|....*
gi 503446380 166 DYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVT 191
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-203 |
2.43e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 53.27 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNkrtvfsNLSFRIAANRINQ-----IILPQSGGKSTIIRMIYGAEKPDSGFVrvfDFNVsDLNYSgill 75
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEVEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPEL-KISYK---- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 lRRYLGIIFEdirlisnMTVKENLSAITKlTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVI 155
Cdd:PRK13409 406 -PQYIKPDYD-------GTVEDLLRSITD-DLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 503446380 156 ADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIatlasIDDDFYTVEL 203
Cdd:PRK13409 477 LDEPSAHLDVEQRLAVAKAIRRIAEEREATALV-----VDHDIYMIDY 519
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-196 |
5.10e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 52.15 E-value: 5.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLnySGILLLRRY- 79
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL--SARAASRRVa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 -----LGIIFE-DIRLISNMTVKENLSAITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPL 153
Cdd:PRK09536 81 svpqdTSLSFEfDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503446380 154 VIADEPLRYLSEDYRIKVIRLFKYLNQDKGitfliATLASIDD 196
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGK-----TAVAAIHD 198
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-100 |
5.93e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRYL 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM 86
|
90 100
....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLS 100
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVA 106
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-188 |
9.94e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 50.65 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILllRRYL 80
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM--REAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLSAITKLTRRDLYLS--EEIFDMLSigHLLDKYPHE---LSISEQSLINIARGVIYNFPLVI 155
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQEriKWVYELFP--RLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 503446380 156 ADEPLRYLSEdyrIKVIRLFKYLNQ--DKGIT-FLI 188
Cdd:PRK11614 161 LDEPSLGLAP---IIIQQIFDTIEQlrEQGMTiFLV 193
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-202 |
1.71e-07 |
|
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: 49.74 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 19 NLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILllRRYLGIIFEDIRLISNMTVKEN 98
Cdd:cd03224 18 GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--RAGIGYVPEGRRIFPELTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 99 L-SAITKLTRRDLYLS-EEIFDMLSI-GHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSedyrIKVIR-L 174
Cdd:cd03224 96 LlLGAYARRRAKRKARlERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA----PKIVEeI 171
|
170 180 190
....*....|....*....|....*....|....*
gi 503446380 175 FKYLNQ--DKGITFLI----ATLA-SIDDDFYTVE 202
Cdd:cd03224 172 FEAIRElrDEGVTILLveqnARFAlEIADRAYVLE 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-99 |
3.96e-07 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 49.03 E-value: 3.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSdlnySGILLLRRYLG 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP----SRARHARQRVG 83
|
90
....*....|....*...
gi 503446380 82 IIFEDIRLISNMTVKENL 99
Cdd:PRK13537 84 VVPQFDNLDPDFTVRENL 101
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-190 |
7.38e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.25 E-value: 7.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRT---------VFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVS--DLN 69
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 70 Y------------SGILLLRRYLGIIFE-DIRLISNMTVKENLSAITKLTRRdlylseeifdmlsIGHLLDK---YPHEL 133
Cdd:PRK15112 84 YrsqrirmifqdpSTSLNPRQRISQILDfPLRLNTDLEPEQREKQIIETLRQ-------------VGLLPDHasyYPHML 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503446380 134 SISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK15112 151 APGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-184 |
8.59e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.99 E-value: 8.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 10 SFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRM------IYgAEKPDSGFVRVfdfNVSDLNYSGILLLRRYLGII 83
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrlieLY-PEARVSGEVYL---DGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 84 FEDIRLISNMTVKENLSAITKLTR---RDLYLSEEIFDMLSIGHL-------LDKYPHELSISEQSLINIARGVIYNFPL 153
Cdd:PRK14247 88 FQIPNPIPNLSIFENVALGLKLNRlvkSKKELQERVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190
....*....|....*....|....*....|.
gi 503446380 154 VIADEPLRYLSEDYRIKVIRLFKYLNQDKGI 184
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTI 198
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-202 |
9.30e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 48.19 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 11 FNKRTVFsNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSG-ILLLRRYLGIIFE--DI 87
Cdd:PRK13643 17 FASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 88 RLISNMTVK------ENLSAITKLTRRdlyLSEEIFDMLSIG-HLLDKYPHELSISEQSLINIArGVIYNFP-LVIADEP 159
Cdd:PRK13643 96 QLFEETVLKdvafgpQNFGIPKEKAEK---IAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIA-GILAMEPeVLVLDEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503446380 160 LRYLSEDYRIKVIRLFKYLNQDKG----ITFLIATLASIDDDFYTVE 202
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESIHQSGQtvvlVTHLMDDVADYADYVYLLE 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-158 |
1.16e-06 |
|
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: 47.61 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNK--RTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGillLRRY 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNmTVKENLS-AITKLTRrdlylsEEIFDMLSIGHLLD---KYPH-----------ELSISEQSLINIA 144
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIAyGRPGATR------EEVEEAARAANAHEfimELPEgydtvigergvKLSGGQRQRIAIA 150
|
170
....*....|....
gi 503446380 145 RGVIYNFPLVIADE 158
Cdd:cd03251 151 RALLKDPPILILDE 164
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-190 |
1.34e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRT-VFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVfDFNVSDLNYSGILLLRRY 79
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFE--DIRLISNmTVKENLsAITKLtrrDLYLSEE-----IFDML---SIGHLLDKYPHELSISEQSLINIArGVIY 149
Cdd:PRK13639 80 VGIVFQnpDDQLFAP-TVEEDV-AFGPL---NLGLSKEevekrVKEALkavGMEGFENKPPHHLSGGQKKRVAIA-GILA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503446380 150 NFPLVIA-DEPLRYLSEDYRIKVIRLFKYLNqDKGITFLIAT 190
Cdd:PRK13639 154 MKPEIIVlDEPTSGLDPMGASQIMKLLYDLN-KEGITIIIST 194
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
37-190 |
2.27e-06 |
|
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: 46.97 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 37 SG-GKSTIIRMIYGAEKP---DSGFVRVFDFNVSDLNYSGILLLR-RYLGIIFED----------IRLIsnmtVKENLSA 101
Cdd:COG0444 40 SGsGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIRgREIQMIFQDpmtslnpvmtVGDQ----IAEPLRI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 102 ITKLTRRDLY-LSEEIFDMLSI---GHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEP---LrylseDYRI--KVI 172
Cdd:COG0444 116 HGGLSKAEAReRAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKLLIADEPttaL-----DVTIqaQIL 190
|
170
....*....|....*...
gi 503446380 173 RLFKYLNQDKGITFLIAT 190
Cdd:COG0444 191 NLLKDLQRELGLAILFIT 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
20-190 |
2.71e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 46.65 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 20 LSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgILLLRRYLGIIFEDIR-LISNMTVKEN 98
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEN---EKWVRSKVGLVFQDPDdQVFSSTVWDD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 99 LS--------AITKLTRRdlylSEEIFDMLSIGHLLDKYPHELSISEQSLINIArGVIYNFP-LVIADEPLRYLSEDYRI 169
Cdd:PRK13647 101 VAfgpvnmglDKDEVERR----VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIA-GVLAMDPdVIVLDEPMAYLDPRGQE 175
|
170 180
....*....|....*....|.
gi 503446380 170 KVIRLFKYLNQdKGITFLIAT 190
Cdd:PRK13647 176 TLMEILDRLHN-QGKTVIVAT 195
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-158 |
3.30e-06 |
|
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: 45.87 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSF--NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLnysGILLLRRY 79
Cdd:cd03369 7 IEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNmTVKENLSaitkltRRDLYLSEEIFDMLSI--GHLldkyphELSISEQSLINIARGVIYNFPLVIAD 157
Cdd:cd03369 84 LTIIPQDPTLFSG-TIRSNLD------PFDEYSDEEIYGALRVseGGL------NLSQGQRQLLCLARALLKRPRVLVLD 150
|
.
gi 503446380 158 E 158
Cdd:cd03369 151 E 151
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
128-202 |
3.53e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 46.77 E-value: 3.53e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503446380 128 KYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIatlasIDDDFYTVE 202
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLF-----ISHDMAVVE 528
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-99 |
3.65e-06 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 46.70 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVvkSF---NKRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGillLR 77
Cdd:COG1132 340 IEFENV--SFsypGDRPVLKDISLTIPPGETVALVGP-SGsGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LR 413
|
90 100
....*....|....*....|..
gi 503446380 78 RYLGIIFEDIRLISnMTVKENL 99
Cdd:COG1132 414 RQIGVVPQDTFLFS-GTIRENI 434
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
6-163 |
4.66e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGaEKPDSgfvrvfdfnvsdlnYSGILLL---RRYLGI 82
Cdd:PRK10938 265 NGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG--------------YSNDLTLfgrRRGSGE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 83 IFEDIR----LISN---MTVKENLSAIT--------------KLTRRDLYLSEEIFDMLSIGHLLDKYP-HELSISEQSL 140
Cdd:PRK10938 330 TIWDIKkhigYVSSslhLDYRVSTSVRNvilsgffdsigiyqAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRL 409
|
170 180
....*....|....*....|...
gi 503446380 141 INIARGVIYNFPLVIADEPLRYL 163
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGL 432
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-190 |
5.07e-06 |
|
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: 46.13 E-value: 5.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRT-VFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGillLRRYL 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS---WRDQI 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 G------IIFEDirlisnmTVKENLsaitKLTRRDLYLSE-----------EIFDMLSIGH--LLDKYPHELSISEQSLI 141
Cdd:TIGR02857 399 AwvpqhpFLFAG-------TIAENI----RLARPDASDAEirealeragldEFVAALPQGLdtPIGEGGAGLSGGQAQRL 467
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503446380 142 NIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQdkGITFLIAT 190
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVT 514
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-158 |
5.56e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 45.75 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFN--KRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgILLLRR 78
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 79 YLGIIFE--DIRLISnMTVK-------ENlsaiTKLTRRDLylsEEIFDMLS----IGHLLDKYPHELSISEQSLINIAR 145
Cdd:PRK13632 84 KIGIIFQnpDNQFIG-ATVEddiafglEN----KKVPPKKM---KDIIDDLAkkvgMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170
....*....|...
gi 503446380 146 GVIYNFPLVIADE 158
Cdd:PRK13632 156 VLALNPEIIIFDE 168
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-195 |
5.76e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.75 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 11 FNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSdlNYSGILLLRRyLGIIFEDIRLI 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ--HYASKEVARR-IGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 91 SNMTVKENLS--------AITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRY 162
Cdd:PRK10253 94 GDITVQELVArgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190
....*....|....*....|....*....|...
gi 503446380 163 LSEDYRIKVIRLFKYLNQDKGITfLIATLASID 195
Cdd:PRK10253 174 LDISHQIDLLELLSELNREKGYT-LAAVLHDLN 205
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-164 |
6.78e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 45.67 E-value: 6.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 3 EFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRV------FDfNVSDLNYSGIlll 76
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdgqemrFA-STTAALAAGV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 77 rrylGIIFEDIRLISNMTVKENL------SAITKLTRRDLYlsEEIFDMLS-IGHLLDkyPH----ELSISEQSLINIAR 145
Cdd:PRK11288 82 ----AIIYQELHLVPEMTVAENLylgqlpHKGGIVNRRLLN--YEAREQLEhLGVDID--PDtplkYLSIGQRQMVEIAK 153
|
170 180
....*....|....*....|
gi 503446380 146 GVIYNfPLVIA-DEPLRYLS 164
Cdd:PRK11288 154 ALARN-ARVIAfDEPTSSLS 172
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-187 |
8.10e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 45.76 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVS-----DLNYSGIlllrryl 80
Cdd:PRK10762 9 GIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkSSQEAGI------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENL-------SAITKLTRRDLYL-SEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFP 152
Cdd:PRK10762 82 GIIHQELNLIPQLTIAENIflgrefvNRFGRIDWKKMYAeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESK 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 503446380 153 LVIADEPLRYLSE---DYRIKVIRLFKylNQDKGITFL 187
Cdd:PRK10762 162 VIIMDEPTDALTDtetESLFRVIRELK--SQGRGIVYI 197
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
14-165 |
1.11e-05 |
|
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: 44.78 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 14 RTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRV--FDFNVSDLNYsgillLRRYLGIIFEDiRLIS 91
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdgHDLALADPAW-----LRRQVGVVLQE-NVLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 92 NMTVKENLSaitkLTRR--DLYLSEEIFDMLSIGHLLDKYPH-----------ELSISEQSLINIARGVIYNFPLVIADE 158
Cdd:cd03252 89 NRSIRDNIA----LADPgmSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170
....*....|
gi 503446380 159 ---PLRYLSE 165
Cdd:cd03252 165 atsALDYESE 174
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-59 |
1.21e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.72 E-value: 1.21e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVR 59
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK 62
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-190 |
1.42e-05 |
|
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: 44.08 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 13 KRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMI--YGAEKPDSGFVRVFDFNVSDLNYsgilllRRYLGIIFEDIRLI 90
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSF------RKIIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 91 SNMTVKENLSAITKLTRrdlylseeifdmlsighlldkypheLSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIK 170
Cdd:cd03213 95 PTLTVRETLMFAAKLRG-------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180
....*....|....*....|
gi 503446380 171 VIRLFKYLNQDkGITFLIAT 190
Cdd:cd03213 150 VMSLLRRLADT-GRTIICSI 168
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-182 |
1.75e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.72 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 5 IDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRvfdFNVSDLNY-SGILLLRRYLGII 83
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIL---FQGKEIDFkSSKEALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 84 FEDIRLISNMTVKENLsAITKLTRRDLYLSEE--------IFDMLSIghllDKYPHE----LSISEQSLINIARGVIYNF 151
Cdd:PRK10982 79 HQELNLVLQRSVMDNM-WLGRYPTKGMFVDQDkmyrdtkaIFDELDI----DIDPRAkvatLSVSQMQMIEIAKAFSYNA 153
|
170 180 190
....*....|....*....|....*....|.
gi 503446380 152 PLVIADEPLRYLSEDyriKVIRLFKYLNQDK 182
Cdd:PRK10982 154 KIVIMDEPTSSLTEK---EVNHLFTIIRKLK 181
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-110 |
2.34e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 43.92 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTV-----FSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLN-YSgil 74
Cdd:COG1101 1 MLELKNLSKTFNPGTVnekraLDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPeYK--- 77
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 503446380 75 llR-RYLGIIFEDIRL--ISNMTVKENLS-AITKLTRRDL 110
Cdd:COG1101 78 --RaKYIGRVFQDPMMgtAPSMTIEENLAlAYRRGKRRGL 115
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-62 |
2.62e-05 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 43.41 E-value: 2.62e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503446380 2 VEFIDVVKSFN------KRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEK--PDSGFVRVFD 62
Cdd:COG2401 25 ERVAIVLEAFGvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPD 93
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-190 |
3.78e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.10 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 10 SFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDS-----GFVRVFDFNVSDLNYSgILLLRRYLGIIF 84
Cdd:PRK14258 16 YYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVN-LNRLRRQVSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 85 EDIRLISnMTVKENLSAITKLT--RRDLYLSEEIFDMLSIGHLLDKYPH-------ELSISEQSLINIARGVIYNFPLVI 155
Cdd:PRK14258 95 PKPNLFP-MSVYDNVAYGVKIVgwRPKLEIDDIVESALKDADLWDEIKHkihksalDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190
....*....|....*....|....*....|....*
gi 503446380 156 ADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVS 208
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
39-190 |
4.10e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 43.19 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 39 GKSTIIRMIYGAEKPDSGFVRVFDFNV-SDLNYSGILLLRRYLGIIFE--DIRLISNMTVKE----------NLSAITKL 105
Cdd:PRK13649 45 GKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKKVGLVFQfpESQLFEETVLKDvafgpqnfgvSQEEAEAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 106 TRRDLYL---SEEIFDmlsighlldKYPHELSISEQSLINIArGVIYNFPLVIA-DEPLRYLSEDYRIKVIRLFKYLNQD 181
Cdd:PRK13649 125 AREKLALvgiSESLFE---------KNPFELSGGQMRRVAIA-GILAMEPKILVlDEPTAGLDPKGRKELMTLFKKLHQS 194
|
....*....
gi 503446380 182 kGITFLIAT 190
Cdd:PRK13649 195 -GMTIVLVT 202
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-192 |
4.33e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.16 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 5 IDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNV---SDLNYSGILLLRRYLG 81
Cdd:PRK14271 25 VNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLggrSIFNYRDVLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 82 IIFEDIRLISnMTVKENLSA---ITKLTRRDLYLSEEIFDMLSIG------HLLDKYPHELSISEQSLINIARGVIYNFP 152
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAgvrAHKLVPRKEFRGVAQARLTEVGlwdavkDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503446380 153 LVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIATLA 192
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLA 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-196 |
4.92e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 42.89 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 19 NLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNV-SDLNYSGILLLRRYLGIIFE--DIRLISNMTV 95
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQfpEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 96 KE------NLSAITKLTR-------RDLYLSEEifdmlsighLLDKYPHELSISEQSLINIArGVIYNFPLVIA-DEPLR 161
Cdd:PRK13641 105 KDvefgpkNFGFSEDEAKekalkwlKKVGLSED---------LISKSPFELSGGQMRRVAIA-GVMAYEPEILClDEPAA 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 503446380 162 YLSEDYRIKVIRLFK-YlnQDKGITFLIATlASIDD 196
Cdd:PRK13641 175 GLDPEGRKEMMQLFKdY--QKAGHTVILVT-HNMDD 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-159 |
5.23e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.09 E-value: 5.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIIlpqsG----GKSTIIRMIYGAEKPDSGFVRVFDFNVS-----DLNYS 71
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALL----GengaGKSTLMKILYGLYQPDSGEILIDGKPVRirsprDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 72 GIlllrrylGIIFEDIRLISNMTVKENL---SAITKLTRRDLY-LSEEifdmlsIGHLLDKYP---------HELSISEQ 138
Cdd:COG3845 81 GI-------GMVHQHFMLVPNLTVAENIvlgLEPTKGGRLDRKaARAR------IRELSERYGldvdpdakvEDLSVGEQ 147
|
170 180
....*....|....*....|..
gi 503446380 139 SLINIARgVIYNFP-LVIADEP 159
Cdd:COG3845 148 QRVEILK-ALYRGArILILDEP 168
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-160 |
6.43e-05 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.10 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 14 RTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRvfdFNVSDLN-----YSGILLlrrYLG----IIF 84
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL---WQGEPIRrqrdeYHQDLL---YLGhqpgIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 85 EdirlisnMTVKENLSAITKLtrRDLYLSEEIFDMLS-IGhlLDKY---P-HELSISEQSLINIARGVIYNFPLVIADEP 159
Cdd:PRK13538 88 E-------LTALENLRFYQRL--HGPGDDEALWEALAqVG--LAGFedvPvRQLSAGQQRRVALARLWLTRAPLWILDEP 156
|
.
gi 503446380 160 L 160
Cdd:PRK13538 157 F 157
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
124-194 |
1.03e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 42.20 E-value: 1.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503446380 124 HLLDKYPHELS--ISEQSLINIArgvIYNFP-LVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT--LASI 194
Cdd:COG4170 150 DIMNSYPHELTegECQKVMIAMA---IANQPrLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLIShdLESI 222
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-193 |
1.04e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.40 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFsNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgilllRRYL 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYC 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLSAITKltrrdLYLSEEIFDM----LSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIA 156
Cdd:PRK13541 73 TYIGHNLGLKLEMTVFENLKFWSE-----IYNSAETLYAaihyFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 503446380 157 DEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIATLAS 193
Cdd:PRK13541 148 DEVETNLSKENRDLLNNLIVMKANSGGIVLLSSHLES 184
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-190 |
1.14e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 41.92 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 12 NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGIlllRRYLGIIFE--DIRL 89
Cdd:PRK13635 18 AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV---RRQVGMVFQnpDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 90 ISNmTVK-------EN--LSAITKLTRRDLYLSEeiFDMLSighLLDKYPHELSISEQSLINIArGVIYNFP-LVIADEP 159
Cdd:PRK13635 95 VGA-TVQddvafglENigVPREEMVERVDQALRQ--VGMED---FLNREPHRLSGGQKQRVAIA-GVLALQPdIIILDEA 167
|
170 180 190
....*....|....*....|....*....|.
gi 503446380 160 LRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSIT 198
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-99 |
1.35e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.51 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 19 NLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLnySGILLLRRYLGIIFEDIRLISNMTVKEN 98
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL--PGHQIARMGVVRTFQHVRLFREMTVIEN 100
|
.
gi 503446380 99 L 99
Cdd:PRK11300 101 L 101
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-134 |
1.64e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.37 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF-NKRTVFSNLSFRIAANRINQIILPqSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilllRR 78
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGP-SGcGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-----DR 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503446380 79 YLGIIFEDIRLISNMTVKENLS---AITKLTRrdlylsEEI-------FDMLSIGHLLDKYPHELS 134
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENMAyglKIRGMPK------AEIeervaeaARILELEPLLDRKPRELS 136
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-56 |
1.71e-04 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 41.59 E-value: 1.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503446380 6 DVVKSFNKRTVFSNLSFRIAA-NRI-----NqiilpqsG-GKSTIIRMIYGAEKPDSG 56
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPgDRIglvgrN-------GaGKSTLLKILAGELEPDSG 53
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-88 |
1.98e-04 |
|
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: 40.98 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 13 KRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRV-------FDFNVS-DLNYSG---ILLLRRYLG 81
Cdd:cd03220 34 EFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvsslLGLGGGfNPELTGrenIYLNGRLLG 113
|
....*..
gi 503446380 82 IIFEDIR 88
Cdd:cd03220 114 LSRKEID 120
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-165 |
2.18e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.70 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSdlnySGILLLRRYL 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 81 GIIFEDIRLISNMTVKENLSAITKLTRRDLYLSeEIFDMLSIGHLLDkYP-HELSISEQSLINIARGVIYNFPLVIADEP 159
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDIHFSPGAVGIT-ELCRLFSLEHLID-YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
....*.
gi 503446380 160 LRYLSE 165
Cdd:PRK13540 155 LVALDE 160
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
14-195 |
2.24e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 40.93 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 14 RTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilLLRRYLGIIFEDIRLISNM 93
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK---AFARKVAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 94 TVKENLS--------AITKLTRRDLYLSEEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSE 165
Cdd:PRK10575 101 TVRELVAigrypwhgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190
....*....|....*....|....*....|
gi 503446380 166 DYRIKVIRLFKYLNQDKGITfLIATLASID 195
Cdd:PRK10575 181 AHQVDVLALVHRLSQERGLT-VIAVLHDIN 209
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-159 |
3.76e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 40.58 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 16 VFSNLSFRIAANriNQI-ILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGillLRRYLGIIFEDIRLISNm 93
Cdd:PRK11160 355 VLKGLSLQIKAG--EKVaLLGRTGcGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA---LRQAISVVSQRVHLFSA- 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503446380 94 TVKENLsAITKLTRRDlylsEEIFDMLS---IGHLLDKYP----------HELSISEQSLINIARGVIYNFPLVIADEP 159
Cdd:PRK11160 429 TLRDNL-LLAAPNASD----EALIEVLQqvgLEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-59 |
4.11e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 4.11e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503446380 2 VEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVR 59
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-165 |
1.17e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.14 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 3 EFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMI--------YGAEKPDSGFVRVFDfNVSDLNYSGIL 74
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLsgvyphgtYEGEIIFEGEELQAS-NIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 75 llrrylgIIFEDIRLISNMTVKENL---SAITKLTRRD---LYL-SEEIFDMLSIGHLLDKYPHELSISEQSLINIARGV 147
Cdd:PRK13549 86 -------IIHQELALVKELSVLENIflgNEITPGGIMDydaMYLrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170
....*....|....*...
gi 503446380 148 IYNFPLVIADEPLRYLSE 165
Cdd:PRK13549 159 NKQARLLILDEPTASLTE 176
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-163 |
1.17e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 39.25 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 32 IILPQSG-GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILLLRRY-LGIIFEDIRLISNMTVKEN------LSAIT 103
Cdd:PRK10070 58 VIMGLSGsGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMTVLDNtafgmeLAGIN 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 104 KLTRRDLYLseEIFDMLSIGHLLDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYL 163
Cdd:PRK10070 138 AEERREKAL--DALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-165 |
1.22e-03 |
|
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: 39.04 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEkPDSGFVRVFDFNVSDLNYSGIL-LLRRY 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGTWDGEIYWSGSPLKASNIRdTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 80 LGIIFEDIRLISNMTVKENLSAITKLTRR-------DLYL-SEEIFDMLSIGHLLDKYP-HELSISEQSLINIARGVIYN 150
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPggrmaynAMYLrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170
....*....|....*
gi 503446380 151 FPLVIADEPLRYLSE 165
Cdd:TIGR02633 160 ARLLILDEPSSSLTE 174
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-158 |
1.46e-03 |
|
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: 38.29 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKR---TVFSNLSFRIAANRINQIILPQSGGKSTIIRMI---YGaekPDSGFVRVFDFNVSDLNysgILL 75
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLerfYD---PTSGEILLDGVDIRDLN---LRW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LRRYLGIIFEDIRLIsNMTVKENLsaitKLTRRDLYLSEEI----------FdmlsIGHLLDKY-----PH--ELSISEQ 138
Cdd:cd03249 75 LRSQIGLVSQEPVLF-DGTIAENI----RYGKPDATDEEVEeaakkanihdF----IMSLPDGYdtlvgERgsQLSGGQK 145
|
170 180
....*....|....*....|
gi 503446380 139 SLINIARGVIYNFPLVIADE 158
Cdd:cd03249 146 QRIAIARALLRNPKILLLDE 165
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
19-188 |
2.03e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 38.11 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 19 NLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgILLLRRYLGIIFE--DIRLISNmTVK 96
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKKVGLVFQypEYQLFEE-TIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 97 ENLSaitkLTRRDLYLSEEIFDM----------LSIGHLLDKYPHELSISEQSLINIArGVIYNFPLV-IADEPLRYLSE 165
Cdd:PRK13637 103 KDIA----FGPINLGLSEEEIENrvkramnivgLDYEDYKDKSPFELSGGQKRRVAIA-GVVAMEPKIlILDEPTAGLDP 177
|
170 180
....*....|....*....|...
gi 503446380 166 DYRIKVIRLFKYLNQDKGITFLI 188
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIIL 200
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-60 |
3.20e-03 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 37.37 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 1 MVEFIDVVKSF----------------------NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
..
gi 503446380 59 RV 60
Cdd:COG1134 84 EV 85
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-158 |
3.62e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 37.78 E-value: 3.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 2 VEFIDVVKSFNKRT---VFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSgilLLRR 78
Cdd:TIGR00958 479 IEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH---YLHR 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 79 YLGIIFEDIRLISNmTVKENLSAITKLTRRD--LYLSEEIFDMLSIGHLLDKYPHE-------LSISEQSLINIARGVIY 149
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYGLTDTPDEeiMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVR 634
|
....*....
gi 503446380 150 NFPLVIADE 158
Cdd:TIGR00958 635 KPRVLILDE 643
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
126-190 |
5.35e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 36.99 E-value: 5.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503446380 126 LDKYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLIAT 190
Cdd:PRK15134 150 LTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFIT 214
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-159 |
5.70e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 36.56 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 12 NKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRM------IYGAEKPDSGFVRVFDFNVSDLNysgILLLRRYLGIIFE 85
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQID---AIKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 86 DIRLISNMTVKENLS---------------AITKLTRRDLYLSEEIFDMLsighllDKYPHELSISEQSLINIARGVIYN 150
Cdd:PRK14246 98 QPNPFPHLSIYDNIAyplkshgikekreikKIVEECLRKVGLWKEVYDRL------NSPASQLSGGQQQRLTIARALALK 171
|
....*....
gi 503446380 151 FPLVIADEP 159
Cdd:PRK14246 172 PKVLLMDEP 180
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
9-159 |
5.90e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 36.75 E-value: 5.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 9 KSFNKRTVFSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILL------------- 75
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELItnpyskkiknfke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 76 LRRYLGIIFE--DIRLISNmTVKENLS----AITKLTRRDLYLSEEIFDMLSIGH-LLDKYPHELSISEQSLINIARGVI 148
Cdd:PRK13631 114 LRRRVSMVFQfpEYQLFKD-TIEKDIMfgpvALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILA 192
|
170
....*....|.
gi 503446380 149 YNFPLVIADEP 159
Cdd:PRK13631 193 IQPEILIFDEP 203
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
39-119 |
8.04e-03 |
|
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: 36.11 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 39 GKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNYSGILllRRylGIIF--EDIRLISNMTVKENL------SAITKLTRRDL 110
Cdd:COG0410 41 GKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA--RL--GIGYvpEGRRIFPSLTVEENLllgayaRRDRAEVRADL 116
|
....*....
gi 503446380 111 ylsEEIFDM 119
Cdd:COG0410 117 ---ERVYEL 122
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-190 |
8.20e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 36.22 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 4 FIDVVKSF---NKRTV--FSNLSFRIAANRINQIILPQSGGKSTIIRMIYGAEKPDSGFVRVFDFNVSDLNysgILLLRR 78
Cdd:COG4586 20 LKGALKGLfrrEYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRR---KEFARR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 79 yLGIIF-EDIRLISNMTVKENLSAItkltrRDLY-LSEEIF--------DMLSIGHLLDKYPHELSISEQSLINIARGVI 148
Cdd:COG4586 97 -IGVVFgQRSQLWWDLPAIDSFRLL-----KAIYrIPDAEYkkrldelvELLDLGELLDTPVRQLSLGQRMRCELAAALL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503446380 149 YNFPLVIADEP---LRYLSEDyriKVIRLFKYLNQDKGITFLIAT 190
Cdd:COG4586 171 HRPKILFLDEPtigLDVVSKE---AIREFLKEYNRERGTTILLTS 212
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
129-188 |
8.37e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 36.32 E-value: 8.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503446380 129 YPHELSISE--QSLINIArgvIYNFP-LVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFLI 188
Cdd:PRK15093 155 FPYELTEGEcqKVMIAIA---LANQPrLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILL 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
128-187 |
8.76e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 36.61 E-value: 8.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503446380 128 KYPHELSISEQSLINIARGVIYNFPLVIADEPLRYLSEDYRIKVIRLFKYLNQDKGITFL 187
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
|
|
| |
