|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
8-242 |
1.99e-98 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 287.37 E-value: 1.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCT---PKVGMVFQ 84
Cdd:COG1116 10 LRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV--DGKPVTgpgPDRGVVFQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 85 ESRLMPWLNVSENILLHTEKDNRNKVD----LDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFA 160
Cdd:COG1116 88 EPALLPWLTVLDNVALGLELRGVPKAErrerARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 161 ALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK-RIKQ-FSVEDEYNRDLTKNY---YINLKKE 235
Cdd:COG1116 168 ALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPgRIVEeIDVDLPRPRDRELRTspeFAALRAE 247
|
....*..
gi 497578899 236 ILRELGE 242
Cdd:COG1116 248 ILDLLRE 254
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
8-213 |
3.46e-87 |
|
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: 257.40 E-value: 3.46e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPKVGMVFQES 86
Cdd:cd03293 3 VRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPvTGPGPDRGYVFQQD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 87 RLMPWLNVSENILL------HTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFA 160
Cdd:cd03293 83 ALLPWLTVLDNVALglelqgVPKAEARERAE--ELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 161 ALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK-RIKQ 213
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPgRIVA 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-214 |
2.77e-72 |
|
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: 219.31 E-value: 2.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----KVGMVF 83
Cdd:cd03259 3 LKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPperrNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 QESRLMPWLNVSENI------LLHTEKDNRNKVDLdkYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDE 157
Cdd:cd03259 79 QDYALFPHLTVAENIafglklRGVPKAEIRARVRE--LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 158 PFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNkRIKQF 214
Cdd:cd03259 157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG-RIVQV 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-222 |
2.91e-71 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 221.51 E-value: 2.91e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 1 MVRSGFLLENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP--- 77
Cdd:COG3842 1 MAMPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPpek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 -KVGMVFQESRLMPWLNVSENI-----LLHTEKDNRN-KVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNP 150
Cdd:COG3842 77 rNVGMVFQDYALFPHLTVAENVafglrMRGVPKAEIRaRVA--ELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 151 DILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQF-SVEDEYNR 222
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVM-NDGRIEQVgTPEEIYER 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-222 |
1.13e-67 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 212.31 E-value: 1.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDK----KCTP---KVG 80
Cdd:COG1118 5 VRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL--NGRdlftNLPPrerRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 81 MVFQESRLMPWLNVSENI------LLHTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:COG1118 79 FVFQHYALFPHMTVAENIafglrvRPPSKAEIRARVE--ELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKnKRIKQF-SVEDEYNR 222
Cdd:COG1118 157 LDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ-GRIEQVgTPDEVYDR 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-206 |
3.42e-64 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 200.47 E-value: 3.42e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCT---PKVGMVFQ 84
Cdd:COG4525 6 VRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL--DGVPVTgpgADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 85 ESRLMPWLNVSENI-----LLHTEKDNRNKVdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:COG4525 84 KDALLPWLNVLDNVafglrLRGVPKAERRAR-AEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497578899 160 AALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFS 206
Cdd:COG4525 163 GALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
8-222 |
1.36e-62 |
|
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: 195.53 E-value: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKehLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----KVGMVF 83
Cdd:cd03300 3 LENVSKFY--GGF--VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 QESRLMPWLNVSENIL--LHTEKDNRNKVD--LDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:cd03300 79 QNYALFPHLTVFENIAfgLRLKKLPKAEIKerVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 160 AALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKrIKQF-SVEDEYNR 222
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGK-IQQIgTPEEIYEE 221
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
8-214 |
2.78e-61 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 194.54 E-value: 2.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPKV------GM 81
Cdd:COG1125 4 FENVTKRY---PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrrriGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENI-----LLHTEKDN-RNKVD-LdkyLKMMKL--EKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:COG1125 81 VIQQIGLFPHMTVAENIatvprLLGWDKERiRARVDeL---LELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 153 LLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQF 214
Cdd:COG1125 158 LLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM-REGRIVQY 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-209 |
4.93e-61 |
|
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: 189.71 E-value: 4.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 6 FLLENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN--------NDKKCTP 77
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedltdledELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 KVGMVFQESRLMPWLNVSENILLhtekdnrnkvdldkylkmmklekfknsypnELSGGMAHRVSIARALSFNPDILLMDE 157
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIAL------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497578899 158 PFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-222 |
7.43e-60 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 192.21 E-value: 7.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCT---PK---VGM 81
Cdd:COG3839 6 LENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI--GGRDVTdlpPKdrnIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENI-----LLHTEKDNRN-KVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLM 155
Cdd:COG3839 80 VFQSYALYPHMTVYENIafplkLRKVPKAEIDrRVR--EAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 156 DEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQF-SVEDEYNR 222
Cdd:COG3839 158 DEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVM-NDGRIQQVgTPEELYDR 224
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
8-203 |
4.36e-59 |
|
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: 186.16 E-value: 4.36e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK-------- 78
Cdd:cd03255 3 LKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDiSKLSEKelaafrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 -VGMVFQESRLMPWLNVSENILL----HTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDIL 153
Cdd:cd03255 83 hIGFVFQSFNLLPDLTALENVELplllAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 154 LMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAmEIAKKII 203
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRII 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
8-219 |
6.63e-58 |
|
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: 184.04 E-value: 6.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGM 81
Cdd:cd03295 3 FENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDpvelrrKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENI-----LLHTEKDNRNKvDLDKYLKMMKLE--KFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:cd03295 80 VIQQIGLFPHMTVEENIalvpkLLKWPKEKIRE-RADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQFSVEDE 219
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM-KNGEIVQVGTPDE 222
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
8-206 |
7.34e-57 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 180.62 E-value: 7.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN------NDKKCTP---- 77
Cdd:COG1136 7 LRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGqdisslSERELARlrrr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 KVGMVFQESRLMPWLNVSENILL------HTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPD 151
Cdd:COG1136 87 HIGFVFQFFNLLPELTALENVALplllagVSRKERRERAR--ELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 152 ILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNiEEAMEIAKKIIVFS 206
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLR 218
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
25-219 |
8.97e-57 |
|
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: 181.00 E-value: 8.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----KVGMVFQESRLMPWLNVSENILL 100
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPvqerNVGFVFQHYALFRHMTVFDNVAF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 101 ----------HTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKM 170
Cdd:cd03296 98 glrvkprserPPEAEIRAKVH--ELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497578899 171 QKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNkRIKQFSVEDE 219
Cdd:cd03296 176 RRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG-RIEQVGTPDE 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-214 |
1.38e-56 |
|
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: 179.37 E-value: 1.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK---VGMVF 83
Cdd:cd03301 3 LENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvTDLPPKdrdIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 QESRLMPWLNVSENILLHTEKDNRNKVDLDKYL----KMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVrevaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 160 AALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQF 214
Cdd:cd03301 159 SNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM-NDGQIQQI 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-219 |
1.03e-55 |
|
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: 178.99 E-value: 1.03e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 1 MVRSGFLLENIYKKylvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-------- 72
Cdd:cd03294 20 LLAKGKSKEEILKK----TGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaamsrke 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 73 -----KKctpKVGMVFQESRLMPWLNVSENILLHTE-----KDNRNKVDLdKYLKMMKLEKFKNSYPNELSGGMAHRVSI 142
Cdd:cd03294 96 lrelrRK---KISMVFQSFALLPHRTVLENVAFGLEvqgvpRAEREERAA-EALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 143 ARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQFSVEDE 219
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIM-KDGRLVQVGTPEE 247
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-204 |
1.26e-55 |
|
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: 177.70 E-value: 1.26e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTPK 78
Cdd:cd03257 4 VKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQE--SRLMPWLNVSENI----LLHTEKDNRNKVDLDKYLKMMKL---EKFKNSYPNELSGGMAHRVSIARALSFN 149
Cdd:cd03257 84 IQMVFQDpmSSLNPRMTIGEQIaeplRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 150 PDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAV 218
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
7-219 |
2.78e-55 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 176.91 E-value: 2.78e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 7 LLENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----KVGMV 82
Cdd:TIGR00968 2 EIANISKRF----GSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHardrKIGFV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLNVSENILLHTEKDNRN----KVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:TIGR00968 78 FQHYALFKHLTVRDNIAFGLEIRKHPkakiKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKrIKQFSVEDE 219
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGK-IEQIGSPDE 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-214 |
1.18e-54 |
|
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: 175.55 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTP--------K 78
Cdd:COG1127 8 VRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDiTGLSEkelyelrrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENILL----HTEKDN---RNKVDLdkYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPD 151
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFplreHTDLSEaeiRELVLE--KLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 152 ILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVF----------------SKNKRIKQF 214
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLadgkiiaegtpeellaSDDPWVRQF 240
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-213 |
3.99e-54 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 173.25 E-value: 3.99e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNIS---SEEITVILGESGCGKTTLLRILAGLENATSGNIYF-----FNNDKK-CTP----KVGMVFQESRLMPW 91
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlFDSRKKiNLPpqqrKIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 LNVSENIL--LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRK 169
Cdd:cd03297 90 LNVRENLAfgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497578899 170 MQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:cd03297 170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
24-242 |
1.82e-53 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 176.04 E-value: 1.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND----KKCTPKVGMVFQESRLMPWLNVSENI- 98
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDvsrlHARDRKVGFVFQHYALFRHMTVFDNIa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 -----LLHTEKDNRNKVD--LDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQ 171
Cdd:PRK10851 97 fgltvLPRRERPNAAAIKakVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 172 KEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKrIKQFSVEDEYNRDLTKNYYINLKKEILRELGE 242
Cdd:PRK10851 177 RWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN-IEQAGTPDQVWREPATRFVLEFMGEVNRLQGT 246
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
25-202 |
2.08e-53 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 176.83 E-value: 2.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDK---KCTP---------KVGMVFQESRLMPWL 92
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLI--DGEditKLSKkelrelrrkKMSMVFQHFALLPHR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENI-----LLHTEKDNRNKVdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:COG4175 121 TVLENVafgleIQGVPKAERRER-AREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIR 199
|
170 180 190
....*....|....*....|....*....|....*
gi 497578899 168 RKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKI 202
Cdd:COG4175 200 REMQDELLELQAKLKKTIVFITHDLDEALRLGDRI 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
8-218 |
1.26e-52 |
|
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: 169.99 E-value: 1.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTPK 78
Cdd:cd03261 3 LRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisglseaelYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENILL----HT---EKDNRNKVdLDKyLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPD 151
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFplreHTrlsEEEIREIV-LEK-LEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 152 ILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE 223
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-209 |
1.67e-52 |
|
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: 168.80 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND------KKCTPKVGM 81
Cdd:cd03225 2 LKNLSFSY--PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDltklslKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESR---LMPwlNVSENI------LLHTEKDNRNKVdlDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:cd03225 80 VFQNPDdqfFGP--TVEEEVafglenLGLPEEEIEERV--EEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 153 LLMDEPFAALDYFTRRKMQKEVVNIHKNtKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
8-242 |
8.30e-52 |
|
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: 168.11 E-value: 8.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-----KVGMV 82
Cdd:COG4555 4 VENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPrearrQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLNVSENIL----LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:COG4555 80 PDERGLYDRLTVRENIRyfaeLYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 159 FAALDYFTRRKMQKEVVNiHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDLTKnyyiNLKKEILR 238
Cdd:COG4555 160 TNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE----NLEDAFVA 234
|
....
gi 497578899 239 ELGE 242
Cdd:COG4555 235 LIGS 238
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
8-218 |
3.07e-51 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 166.35 E-value: 3.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTP-----KVGM 81
Cdd:COG1122 3 LENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDiTKKNLrelrrKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQ--ESRL-MPwlNVSENI------LLHTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:COG1122 80 VFQnpDDQLfAP--TVEEDVafgpenLGLPREEIRERVE--EALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 153 LLMDEPFAALDYFTRRKMQKEVVNIHKNtKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-218 |
1.41e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.85 E-value: 1.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-----KKCTPKVGMV 82
Cdd:COG1131 3 VRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDvardpAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLNVSENILLH------TEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMD 156
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFarlyglPRKEARERID--ELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 157 EPFAALDYFTRRKMqKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:COG1131 157 EPTSGLDPEARREL-WELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDE 217
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
23-227 |
8.10e-50 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 167.26 E-value: 8.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 23 LVLD--NISLNISSEEITVILGESGCGKTTLLRILAGLeNATS----------GNIYFFNNDKKC-----TPKVGMVFQE 85
Cdd:TIGR03415 36 LVLGvhNASLDIEEGEICVLMGLSGSGKSTLLRAVNGL-NPVSrgsvlvkdgdGSVDVANCDAATlrrlrTHRVSMVFQQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 86 SRLMPWLNVSENILLHTE------KDNRNKVdlDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:TIGR03415 115 FALLPWRTVEENVAFGLEmqgmpkAERRKRV--DEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPF 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 160 AALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQFSV--------EDEYNRDLTKN 227
Cdd:TIGR03415 193 SALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRIAIM-EGGRIIQHGTpeeivlnpANDYVADFVAH 267
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-213 |
2.82e-49 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 165.51 E-value: 2.82e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----KVGMVF 83
Cdd:PRK09452 17 LRGISKSF--DGKE--VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPaenrHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 QESRLMPWLNVSENILLHTEKDNRNKVDLDKY----LKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMQKTPAAEITPRvmeaLRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 160 AALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQ 213
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM-RDGRIEQ 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-208 |
4.47e-49 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 161.79 E-value: 4.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPKVGMVFQESRLMPWLNVSENI---- 98
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPvEGPGAERGVVFQNEGLLPWRNVQDNVafgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 -LLHTEKDNRNKVDLdKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNI 177
Cdd:PRK11248 96 qLAGVEKMQRLEIAH-QMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
170 180 190
....*....|....*....|....*....|.
gi 497578899 178 HKNTKKGVVFVTHNIEEAMEIAKKIIVFSKN 208
Cdd:PRK11248 175 WQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
4-222 |
1.43e-48 |
|
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: 163.28 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 4 SGFL-LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----K 78
Cdd:TIGR03265 2 SPYLsIDNIRKRF----GAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPpqkrD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENIL--LHTEKDNRNKVD--LDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:TIGR03265 78 YGIVFQSYALFPNLTVADNIAygLKNRGMGRAEVAerVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNkRIKQFSVEDE-YNR 222
Cdd:TIGR03265 158 LDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHG-VIEQVGTPQEiYRH 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
40-209 |
6.73e-48 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 160.74 E-value: 6.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 40 ILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPK----VGMVFQESRLMPWLNVSENIL--LHTEKDNRNKVD-- 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPhlrhINMVFQSYALFPHMTVEENVAfgLKMRKVPRAEIKpr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 112 LDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHN 191
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|....*...
gi 497578899 192 IEEAMEIAKKIIVFSKNK 209
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKGK 178
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
25-206 |
3.34e-47 |
|
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: 156.09 E-value: 3.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCT---PKVGMVFQESRLMPWLNVSENILL- 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVIL--EGKQITepgPDRMVVFQNYSLLPWLTVRENIALa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 101 ------HTEKDNRNKVdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEV 174
Cdd:TIGR01184 79 vdrvlpDLSKSERRAI-VEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157
|
170 180 190
....*....|....*....|....*....|..
gi 497578899 175 VNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFS 206
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-204 |
3.69e-47 |
|
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: 163.15 E-value: 3.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHL-VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTP 77
Cdd:COG1123 263 VRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltklsrrslRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 KVGMVFQ--ESRLMPWLNVSENI----LLH---TEKDNRNKVDldKYLKMMKL-EKFKNSYPNELSGGMAHRVSIARALS 147
Cdd:COG1123 343 RVQMVFQdpYSSLNPRMTVGDIIaeplRLHgllSRAERRERVA--ELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 148 FNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAV 477
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
8-203 |
1.55e-46 |
|
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: 153.84 E-value: 1.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFF----NNDKKCTP----KV 79
Cdd:cd03262 3 IKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglklTDDKKNINelrqKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 80 GMVFQESRLMPWLNVSENILLHTEK-DNRNKVDLD----KYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEeralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497578899 155 MDEPFAALDyftrRKMQKEVVNIHKN-TKKG--VVFVTHNIEEAMEIAKKII 203
Cdd:cd03262 159 FDEPTSALD----PELVGEVLDVMKDlAEEGmtMVVVTHEMGFAREVADRVI 206
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
8-214 |
4.12e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 153.61 E-value: 4.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF----FNNDKKCTP----KV 79
Cdd:COG1126 4 IENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdgedLTDSKKDINklrrKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 80 GMVFQESRLMPWLNVSENI---LLHTEKDNRNKVDLD--KYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVtlaPIKVKKMSKAEAEERamELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 155 MDEPFAALDyftrRKMQKEVVNIHKN-TKKG--VVFVTHNIEEAMEIAKKII---------------VFS--KNKRIKQF 214
Cdd:COG1126 160 FDEPTSALD----PELVGEVLDVMRDlAKEGmtMVVVTHEMGFAREVADRVVfmdggriveegppeeFFEnpQHERTRAF 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
27-207 |
5.01e-45 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 154.10 E-value: 5.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 27 NISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF-----FNNDKK-CTP----KVGMVFQESRLMPWLNVSE 96
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlQDSARGiFLPphrrRIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILL---HTEKDNRnKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKE 173
Cdd:COG4148 97 NLLYgrkRAPRAER-RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPY 175
|
170 180 190
....*....|....*....|....*....|....
gi 497578899 174 VVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSK 207
Cdd:COG4148 176 LERLRDELDIPILYVSHSLDEVARLADHVVLLEQ 209
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-224 |
6.99e-45 |
|
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: 150.72 E-value: 6.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN------NDKKCTPKVGM 81
Cdd:COG1124 4 VRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGrpvtrrRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESR--LMPWLNV----SENILLHTEKDNRNKVDldkylKMMKL----EKFKNSYPNELSGGMAHRVSIARALSFNPD 151
Cdd:COG1124 84 VFQDPYasLHPRHTVdrilAEPLRIHGLPDREERIA-----ELLEQvglpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 152 ILLMDEPFAALDYFTrrkmQKEVVN----IHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED-------EY 220
Cdd:COG1124 159 LLLLDEPTSALDVSV----QAEILNllkdLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADllagpkhPY 234
|
....
gi 497578899 221 NRDL 224
Cdd:COG1124 235 TREL 238
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-218 |
1.22e-44 |
|
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: 149.65 E-value: 1.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP---------K 78
Cdd:cd03258 4 LKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkelrkarrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENI-----LLHTEKDNRNKvDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDIL 153
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENValpleIAGVPKAEIEE-RVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 154 LMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
8-213 |
3.52e-44 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 148.62 E-value: 3.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNI----YFFNNDKKCTP------ 77
Cdd:COG4161 5 LKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniagHQFDFSQKPSEkairll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 --KVGMVFQESRLMPWLNVSEN-------ILLHTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSF 148
Cdd:COG4161 81 rqKVGMVFQQYNLWPHLTVMENlieapckVLGLSKEQAREKAM--KLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 149 NPDILLMDEPFAALDyftrRKMQKEVVNIHKNTKK-GV--VFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:COG4161 159 EPQVLLFDEPTAALD----PEITAQVVEIIRELSQtGItqVIVTHEVEFARKVASQVVYMEKGRIIEQ 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-209 |
1.75e-43 |
|
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: 144.31 E-value: 1.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGM 81
Cdd:cd00267 2 IENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPleelrrRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQesrlmpwlnvsenillhtekdnrnkvdldkylkmmklekfknsypneLSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:cd00267 78 VPQ-----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSG 110
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497578899 162 LDYFTRRKMQKEVVNIHKNtKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd00267 111 LDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-204 |
1.89e-43 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 150.18 E-value: 1.89e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN---NDKKctPK---VGM 81
Cdd:PRK11000 6 LRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmNDVP--PAergVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENILLHTEKDNRNKVDLDKYLK----MMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDE 157
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNqvaeVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497578899 158 PFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVV 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-209 |
2.54e-43 |
|
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: 144.08 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-----KKCTPKVGMV 82
Cdd:cd03230 3 VRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDikkepEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLNVSENIllhtekdnrnkvdldkylkmmklekfknsypnELSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:cd03230 79 PEEPSLYENLTVRENL--------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497578899 163 DYFTRRKMqKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03230 127 DPESRREF-WELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
7-226 |
3.95e-43 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 149.60 E-value: 3.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 7 LLE--NIYKKYlvdNKEHLVlDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPK----VG 80
Cdd:PRK11607 19 LLEirNLTKSF---DGQHAV-DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPyqrpIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 81 MVFQESRLMPWLNVSENILLHTEKDNRNKVDL----DKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMD 156
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIasrvNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 157 EPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDLTK 226
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
8-206 |
8.39e-43 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 144.63 E-value: 8.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENA-----TSGNIYFFN---NDKKCTP-- 77
Cdd:cd03260 3 LRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGkdiYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 ---KVGMVFQESRLMPwLNVSENIL----LHTEKDNRN----------KVDLDKYLKmmklekfKNSYPNELSGGMAHRV 140
Cdd:cd03260 79 lrrRVGMVFQKPNPFP-GSIYDNVAyglrLHGIKLKEElderveealrKAALWDEVK-------DRLHALGLSGGQQQRL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 141 SIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTkkGVVFVTHNIEEAMEIAKKIIVFS 206
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLL 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-219 |
5.52e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.50 E-value: 5.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 1 MVRsgflLENIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-----KKC 75
Cdd:COG2884 1 MIR----FENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrlkRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 76 TP----KVGMVFQESRLMPWLNVSENILL------HTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARA 145
Cdd:COG2884 74 IPylrrRIGVVFQDFRLLPDRTVYENVALplrvtgKSRKEIRRRVR--EVLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 146 LSFNPDILLMDEPFAALDYFTRRkmqkEVVNI-HKNTKKG--VVFVTHNIEEAMEIAKKIIVFsKNKRIkqfsVEDE 219
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSW----EIMELlEEINRRGttVLIATHDLELVDRMPKRVLEL-EDGRL----VRDE 219
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
8-209 |
7.06e-42 |
|
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: 141.87 E-value: 7.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-----KKCTPKVGMV 82
Cdd:cd03263 3 IRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSirtdrKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLNVSENILLHTE----KDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARlkglPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 159 FAALDYFTRRKM----QKEVVNihkntkKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03263 161 TSGLDPASRRAIwdliLEVRKG------RSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
8-204 |
1.85e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 141.43 E-value: 1.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnkEHLVLdNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP------KVGM 81
Cdd:COG3840 4 LDDLTYRY-----GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILW--NGQDLTAlppaerPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENILL--H-----TEKDnrnKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:COG3840 76 LFQENNLFPHLTVAQNIGLglRpglklTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLL 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-203 |
5.90e-41 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 140.97 E-value: 5.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 7 LLENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNndkkcTP------KVG 80
Cdd:PRK11247 14 LLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT-----APlaeareDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 81 MVFQESRLMPWLNVSENILLHTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFA 160
Cdd:PRK11247 85 LMFQDARLLPWKKVIDNVGLGLKGQWRDAAL--QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497578899 161 ALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKII 203
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
8-209 |
7.56e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.18 E-value: 7.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIykKYLVDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP--------KV 79
Cdd:COG4619 3 LEGL--SFRVGGKP--ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYL--DGKPLSAmpppewrrQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 80 GMVFQESRLmpWLN-VSENIL----LHTEKDNRNKvdLDKYLKMMKL-EKFKNSYPNELSGGMAHRVSIARALSFNPDIL 153
Cdd:COG4619 77 AYVPQEPAL--WGGtVRDNLPfpfqLRERKFDRER--ALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 154 LMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-160 |
1.32e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 136.62 E-value: 1.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGMVFQESRLMPWLNVSENI 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDErkslrkEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 ----LLHTEKDNRNKVDLDKYLKMMKLEKFKN----SYPNELSGGMAHRVSIARALSFNPDILLMDEPFA 160
Cdd:pfam00005 81 rlglLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-218 |
1.86e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 139.89 E-value: 1.86e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND------KKCTP---KVGMVFQ--ESRLM 89
Cdd:TIGR04521 17 EKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDitakkkKKLKDlrkKVGLVFQfpEHQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 90 PwLNVSENI------LLHTEKDNRNKVDldKYLKMMKL-EKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:TIGR04521 97 E-ETVYKDIafgpknLGLSEEEAEERVK--EALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 163 DYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPRE 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-204 |
3.20e-40 |
|
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: 140.57 E-value: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 7 LLE--NIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENA---TSGNIYFFNND-KKCTPK-- 78
Cdd:COG0444 1 LLEvrNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDlLKLSEKel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 -------VGMVFQESrlMPWLN--------VSENILLH---TEKDNRNKVDldKYLKMMKL---EKFKNSYPNELSGGMA 137
Cdd:COG0444 81 rkirgreIQMIFQDP--MTSLNpvmtvgdqIAEPLRIHgglSKAEARERAI--ELLERVGLpdpERRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 138 HRVSIARALSFNPDILLMDEPFAALDyFTrrkMQKEVVN----IHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALD-VT---IQAQILNllkdLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
8-213 |
5.33e-40 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 140.60 E-value: 5.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEhLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----KVGMVF 83
Cdd:NF040840 4 IENLSKDW----KE-FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPpekrGIAYVY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 QESRLMPWLNVSENIL--LHTEKDNRNKVDlDKYLKMMKL---EKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:NF040840 79 QNYMLFPHKTVFENIAfgLKLRKVPKEEIE-RKVKEIMELlgiSHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQ 213
Cdd:NF040840 158 LSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIM-LNGRLSQ 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
24-218 |
5.57e-40 |
|
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: 143.89 E-value: 5.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGL--ENAT-SGNIYFFNNDKKCTP------KVGMVFQE--SRLMPwL 92
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRiSGEVLLDGRDLLELSealrgrRIGMVFQDpmTQLNP-V 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENI------LLHTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFT 166
Cdd:COG1123 100 TVGDQIaealenLGLSRAEARARVL--ELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497578899 167 RRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:COG1123 178 QAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-222 |
2.71e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 139.08 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 1 MVRSGFL-LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND--KKCTP 77
Cdd:PRK11432 1 MTQKNFVvLKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDvtHRSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 K--VGMVFQESRLMPWLNVSENI-----LLHTEKDNRnKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNP 150
Cdd:PRK11432 77 QrdICMVFQSYALFPHMSLGENVgyglkMLGVPKEER-KQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 151 DILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNR 222
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
8-213 |
2.88e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 135.91 E-value: 2.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNI----YFFNNDKKCTPK----- 78
Cdd:PRK11124 5 LNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagNHFDFSKTPSDKairel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 ---VGMVFQESRLMPWLNVSENIL------LHTEKDNRNKvDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFN 149
Cdd:PRK11124 81 rrnVGMVFQQYNLWPHLTVQQNLIeapcrvLGLSKDQALA-RAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 150 PDILLMDEPFAALDyftrRKMQKEVVNIHK---NTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:PRK11124 160 PQVLLFDEPTAALD----PEITAQIVSIIRelaETGITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-228 |
3.94e-39 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 138.71 E-value: 3.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 28 ISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIY-----FFNNDKK-CTP----KVGMVFQESRLMPWLNVSEN 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVlngrtLFDSRKGiFLPpekrRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 iLLHTEKDNRNK---VDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEV 174
Cdd:TIGR02142 96 -LRYGMKRARPSerrISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 175 VNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQFSVEDEYNRDLTKNY 228
Cdd:TIGR02142 175 ERLHAEFGIPILYVSHSLQEVLRLADRVVVL-EDGRVAAAGPIAEVWASPDLPW 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
29-211 |
1.13e-38 |
|
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: 133.77 E-value: 1.13e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 29 SLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----KVGMVFQESRLMPWLNVSENI------ 98
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPpadrPVSMLFQENNLFAHLTVEQNVglglsp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 LLHTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIH 178
Cdd:cd03298 98 GLKLTAEDRQAIE--VALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|...
gi 497578899 179 KNTKKGVVFVTHNIEEAMEIAKKiIVFSKNKRI 211
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQR-VVFLDNGRI 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
8-163 |
1.79e-38 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 136.36 E-value: 1.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTP--------K 78
Cdd:COG1135 4 LENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDlTALSErelraarrK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENI-----LLHTEKDNRN-KVdlDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAENValpleIAGVPKAEIRkRV--AELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170
....*....|.
gi 497578899 153 LLMDEPFAALD 163
Cdd:COG1135 162 LLCDEATSALD 172
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-213 |
1.17e-37 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 132.09 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK-----VGMVFQESRLMPWLNV 94
Cdd:COG1120 13 GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDlASLSRRelarrIAYVPQEPPAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILL-----------HTEKDnRNKVdlDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:COG1120 93 RELVALgryphlglfgrPSAED-REAV--EEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 164 YftrrKMQKEVVNI----HKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:COG1120 170 L----AHQLEVLELlrrlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-203 |
2.22e-37 |
|
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: 131.15 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlVDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTPK 78
Cdd:cd03256 3 VENLSKTY-PNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENIL---------------LHTEKDNRNKVDLdkyLKMMKLEKFKNSYPNELSGGMAHRVSIA 143
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLsgrlgrrstwrslfgLFPKEEKQRALAA---LERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 144 RALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKII 203
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIV 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-228 |
3.80e-37 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 134.39 E-value: 3.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 23 LVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND----------KKCTPKVGMVFQESRLMPWL 92
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakisdaelrEVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENILLHTE-----KDNRNKVDLDKyLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:PRK10070 122 TVLDNTAFGMElaginAEERREKALDA-LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 168 RKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQFSVEDEYNRDLTKNY 228
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIM-QNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
8-214 |
4.82e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 130.15 E-value: 4.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnkEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP------KVGM 81
Cdd:cd03299 3 VENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL--NGKDITNlppekrDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENILLHTEKDNRNKVDLDKYL----KMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDE 157
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVleiaEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 158 PFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFsKNKRIKQF 214
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM-LNGKLIQV 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-209 |
1.28e-36 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 127.11 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTP-----KVGM 81
Cdd:cd03228 3 FKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlRDLDLeslrkNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPwLNVSENIllhtekdnrnkvdldkylkmmklekfknsypneLSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:cd03228 81 VPQDPFLFS-GTIRENI---------------------------------LSGGQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497578899 162 LDYFTRRKMQKevvNIHKNTK-KGVVFVTHNIeEAMEIAKKIIVFSKNK 209
Cdd:cd03228 127 LDPETEALILE---ALRALAKgKTVIVIAHRL-STIRDADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-209 |
1.80e-36 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 136.12 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK-----VGM 81
Cdd:COG2274 476 LENVSFRY--PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlRQIDPAslrrqIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPwLNVSENILLHtekdnRNKVDLDKY---LKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALS 147
Cdd:COG2274 554 VLQDVFLFS-GTIRENITLG-----DPDATDEEIieaARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALL 627
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 148 FNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNiEEAMEIAKKIIVFSKNK 209
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHR-LSTIRLADRIIVLDKGR 686
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
21-190 |
6.24e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 126.44 E-value: 6.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-----KVGMVFQESRLMPWLNVS 95
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARedyrrRLAYLGHADGLKPELTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENILLHTE--KDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQkE 173
Cdd:COG4133 94 ENLRFWAAlyGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLA-E 172
|
170
....*....|....*..
gi 497578899 174 VVNIHKNTKKGVVFVTH 190
Cdd:COG4133 173 LIAAHLARGGAVLLTTH 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-205 |
8.34e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.45 E-value: 8.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTPK---------VGMVFQESRLMPWLNV 94
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL--DGEPVRFRsprdaqaagIAIIHQELNLVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLHTEKDNRNKVDLDK-------YLKMMKLEkFKnsyPNELSG--GMAHR--VSIARALSFNPDILLMDEPFAALD 163
Cdd:COG1129 97 AENIFLGREPRRGGLIDWRAmrrrareLLARLGLD-ID---PDTPVGdlSVAQQqlVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497578899 164 yftrrkmQKEVVN----IHKNTKKGV--VFVTHNIEEAMEIAKKIIVF 205
Cdd:COG1129 173 -------EREVERlfriIRRLKAQGVaiIYISHRLDEVFEIADRVTVL 213
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-211 |
1.69e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPKVGMVFQES---RLMPwLNVSE 96
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPpRRARRRIGYVPQRAevdWDFP-ITVRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILL-----------HTEKDnRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYF 165
Cdd:COG1121 97 VVLMgrygrrglfrrPSRAD-REAVD--EALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497578899 166 TRRKMQKEVVNIHKNtKKGVVFVTHNIEEAMEIAKKIIVFskNKRI 211
Cdd:COG1121 174 TEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL--NRGL 216
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-213 |
3.13e-35 |
|
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: 123.70 E-value: 3.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND------KKCTPKVGM 81
Cdd:cd03214 2 VENLSVGY----GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDlaslspKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQesrlmpwlnvsenillhtekdnrnkvdldkYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:cd03214 78 VPQ------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497578899 162 LDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:cd03214 128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-218 |
4.44e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 127.61 E-value: 4.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTPK 78
Cdd:PRK11153 4 LKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltalsekelRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENILLHTEKDNRNKVDLDK----YLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKArvteLLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSE 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
8-204 |
2.11e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 123.15 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnkEHLVLdNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP----KVGMVF 83
Cdd:PRK10771 4 LTDITWLY-----HHLPM-RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPpsrrPVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 QESRLMPWLNVSENI---------LLHTEKDNrnkvdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:PRK10771 78 QENNLFSHLTVAQNIglglnpglkLNAAQREK-----LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLV 202
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
8-211 |
2.33e-34 |
|
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: 121.00 E-value: 2.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTPK--------- 78
Cdd:cd03216 3 LRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV--DGKEVSFAsprdarrag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQesrlmpwlnvsenillhtekdnrnkvdldkylkmmklekfknsypneLSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:cd03216 77 IAMVYQ-----------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 159 FAALDyftrrkmQKEVVN----IHKNTKKG--VVFVTHNIEEAMEIAKKIIVFSKNKRI 211
Cdd:cd03216 110 TAALT-------PAEVERlfkvIRRLRAQGvaVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-214 |
3.69e-34 |
|
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: 121.87 E-value: 3.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPK-VGMVFQeSRLMPW---LNVSEN 97
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKrIGYVPQ-RRSIDRdfpISVRDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 ILL----------HTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDyftr 167
Cdd:cd03235 91 VLMglyghkglfrRLSKADKAKVD--EALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD---- 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 168 RKMQKEVVNIHKNTK---KGVVFVTHNIEEAMEIAKKIIVFskNKRIKQF 214
Cdd:cd03235 165 PKTQEDIYELLRELRregMTILVVTHDLGLVLEYFDRVLLL--NRTVVAS 212
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-209 |
5.30e-34 |
|
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: 121.71 E-value: 5.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 7 LLENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-----KVGM 81
Cdd:cd03266 3 TADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPaearrRLGF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENIL----LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDE 157
Cdd:cd03266 83 VSDSTGLYDRLTARENLEyfagLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497578899 158 PFAALDYFTRRKMqKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03266 163 PTTGLDVMATRAL-REFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGR 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
8-203 |
6.95e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.82 E-value: 6.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTPK-----VGMV 82
Cdd:cd03226 2 IENISFSY---KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILL--NGKPIKAKerrksIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLN-VSENILLHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:cd03226 77 MQDVDYQLFTDsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497578899 162 LDYftrRKMQK--EVVNIHKNTKKGVVFVTHNIEEAMEIAKKII 203
Cdd:cd03226 157 LDY---KNMERvgELIRELAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
8-203 |
8.57e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.09 E-value: 8.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTPK 78
Cdd:COG3638 5 LRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtalrgralRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENIL---------------LHTEKDNRNKVDLdkyLKMMKLEKFKNSYPNELSGGMAHRVSIA 143
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLagrlgrtstwrsllgLFPPEDRERALEA---LERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 144 RALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKII 203
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
8-213 |
1.40e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 123.80 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKeHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN---NDKKctPK---VGM 81
Cdd:PRK11650 6 LQAVRKSY--DGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNELE--PAdrdIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENI-----LLHTEKDNRNKvDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMD 156
Cdd:PRK11650 81 VFQNYALYPHMSVRENMayglkIRGMPKAEIEE-RVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 157 EPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNkRIKQ 213
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG-VAEQ 215
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-226 |
2.45e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.52 E-value: 2.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKY--LVDNkehlvlDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTPK------- 78
Cdd:COG3845 8 LRGITKRFggVVAN------DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI--DGKPVRIRsprdaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 --VGMVFQESRLMPWLNVSENILLHTEKDNRNKVDLDKYLKmmKLEKFKNSY-----PN----ELSGGMAHRVSIARALS 147
Cdd:COG3845 80 lgIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKAARA--RIRELSERYgldvdPDakveDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 148 FNPDILLMDEP------------FAALdyftrRKMQKEvvnihkntKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFS 215
Cdd:COG3845 158 RGARILILDEPtavltpqeadelFEIL-----RRLAAE--------GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVD 224
|
250
....*....|.
gi 497578899 216 VEDEYNRDLTK 226
Cdd:COG3845 225 TAETSEEELAE 235
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
9-202 |
3.44e-33 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 119.76 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND----------KKCTPK 78
Cdd:TIGR02211 5 ENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSlsklssneraKLRNKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENILLHTEKDNRNKVDL-DKYLKMMK---LEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:TIGR02211 85 LGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAkERAYEMLEkvgLEHRINHRPSELSGGERQRVAIARALVNQPSLVL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNieeaMEIAKKI 202
Cdd:TIGR02211 165 ADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD----LELAKKL 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-209 |
3.62e-33 |
|
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: 119.43 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKehlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-----KKCTP----K 78
Cdd:cd03292 3 FINVTKTYPNGTA---ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDvsdlrGRAIPylrrK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 VGMVFQESRLMPWLNVSENILL------HTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFalevtgVPPREIRKRVP--AALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 153 LLMDEPFAALDYFTRRkmqkEVVNIHKNTKKG---VVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03292 158 LIADEPTGNLDPDTTW----EIMNLLKKINKAgttVVVATHAKELVDTTRHRVIALERGK 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
24-211 |
3.72e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 120.20 E-value: 3.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIY---FFNNDKKCTPK-----VGMVFQESRLMPWLNVS 95
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIvdgLKVNDPKVDERlirqeAGMVFQQFYLFPHLTAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENILL------HTEKDNRNKVDLDkYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDyftrRK 169
Cdd:PRK09493 96 ENVMFgplrvrGASKEEAEKQARE-LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD----PE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497578899 170 MQKEVVNIHKN-TKKG--VVFVTHNIEEAMEIAKKIIvFSKNKRI 211
Cdd:PRK09493 171 LRHEVLKVMQDlAEEGmtMVIVTHEIGFAEKVASRLI-FIDKGRI 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-218 |
5.59e-33 |
|
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: 119.01 E-value: 5.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-----KVGMVF 83
Cdd:cd03265 4 ENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPrevrrRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 QESRLMPWLNVSENILLHTE----KDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:cd03265 80 QDLSVDDELTGWENLYIHARlygvPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 160 AALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
19-215 |
9.67e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 118.43 E-value: 9.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 19 NKEHLVLDnISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPK----VGMVFQESRLMPWLNV 94
Cdd:TIGR01277 9 EYEHLPME-FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPyqrpVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILL-----------HTEK--DNRNKVDLDKYLKMMklekfknsyPNELSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:TIGR01277 88 RQNIGLglhpglklnaeQQEKvvDAAQQVGIADYLDRL---------PEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 162 LDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSkNKRIKQFS 215
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVS-QGKIKVVS 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
8-229 |
5.76e-32 |
|
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: 116.87 E-value: 5.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-----KVGMV 82
Cdd:cd03218 3 AENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhkraRLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 F--QESRLMPWLNVSENILL----HTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMD 156
Cdd:cd03218 79 YlpQEASIFRKLTVEENILAvleiRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 157 EPFAALDYFTRRKMQKeVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDLTKNYY 229
Cdd:cd03218 159 EPFAGVDPIAVQDIQK-IIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
8-213 |
2.11e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 116.24 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND------KKCTPKVGM 81
Cdd:PRK13632 10 VENVSFSY--PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQEsrlmP-----WLNVSENIL--LHTEKDNRNKVD--LDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:PRK13632 88 IFQN----PdnqfiGATVEDDIAfgLENKKVPPKKMKdiIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 153 LLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMeIAKKIIVFSKNKRIKQ 213
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQ 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-218 |
2.50e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 118.05 E-value: 2.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDnISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNI-----YFFNNDKK-CTP----KVGMVFQESRLMPW 91
Cdd:PRK11144 12 DLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrVLFDAEKGiCLPpekrRIGYVFQDARLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 LNVSENilLHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRR--- 168
Cdd:PRK11144 91 YKVRGN--LRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRell 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 169 ----KMQKEvVNIhkntkkGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:PRK11144 169 pyleRLARE-INI------PILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
21-199 |
8.95e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 112.17 E-value: 8.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnnDKKCTP------------KVGMVFQESRL 88
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILF---DGENIPamsrsrlytvrkRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 89 MPWLNVSENILLHTEKDNRNKVDLDKYLKMMKLEKF-----KNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PRK11831 96 FTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVglrgaAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 497578899 164 YFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIA 199
Cdd:PRK11831 176 PITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIA 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
4-213 |
1.22e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.38 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 4 SGFLLENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNI----YFFNNDKKCTP-- 77
Cdd:PRK11264 2 SAIEVKNLVKKF----HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdITIDTARSLSQqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 --------KVGMVFQESRLMPWLNVSENIL---LHTEKDNRNKVDL--DKYLKMMKLEKFKNSYPNELSGGMAHRVSIAR 144
Cdd:PRK11264 78 glirqlrqHVGFVFQNFNLFPHRTVLENIIegpVIVKGEPKEEATAraRELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 145 ALSFNPDILLMDEPFAALDyftrRKMQKEVVNIHK---NTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALD----PELVGEVLNTIRqlaQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQ 225
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-205 |
1.30e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.88 E-value: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAG-LENA--TSGNIYFfnNDKKCTP------KVGMVFQESRLMPWL 92
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLL--NGRRLTAlpaeqrRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENILL---HTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRK 169
Cdd:COG4136 92 SVGENLAFalpPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 497578899 170 MQKEVVNIHKNTKKGVVFVTHNIEEAmEIAKKIIVF 205
Cdd:COG4136 172 FREFVFEQIRQRGIPALLVTHDEEDA-PAAGRVLDL 206
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-205 |
5.62e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 109.74 E-value: 5.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGL-----ENATSGNIYFFN---NDKKCTP-----KVGMVFQESR 87
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGediYDPDVDVvelrrRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 LMPwLNVSENIL----LHtekDNRNKVDLD----KYLKMMKL-EKFK---NSYPNELSGGMAHRVSIARALSFNPDILLM 155
Cdd:COG1117 103 PFP-KSIYDNVAyglrLH---GIKSKSELDeiveESLRKAALwDEVKdrlKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497578899 156 DEPFAALDYFTRRKMQKEVVNIHKN-TkkgVVFVTHNIEEAMEIAKKIIVF 205
Cdd:COG1117 179 DEPTSALDPISTAKIEELILELKKDyT---IVIVTHNMQQAARVSDYTAFF 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-190 |
1.72e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 107.52 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDkkCTP------------KVGMVFQESRLMPW 91
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFAldedararlrarHVGFVFQSFQLLPT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 LNVSENILLHTE----KDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:COG4181 105 LTALENVMLPLElagrRDARARAR--ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATG 182
|
170 180
....*....|....*....|...
gi 497578899 168 RKMQKEVVNIHKNTKKGVVFVTH 190
Cdd:COG4181 183 EQIIDLLFELNRERGTTLVLVTH 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-209 |
2.88e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 108.60 E-value: 2.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN---NDKKCT-----PKVGMVFQ--ESRLMP 90
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvdiTDKKVKlsdirKKVGLVFQypEYQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 91 W------------LNVSENILLHTEKDNRNKVDLDKylkmmklEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:PRK13637 99 EtiekdiafgpinLGLSEEEIENRVKRAMNIVGLDY-------EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
24-199 |
8.22e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 105.59 E-value: 8.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND--KKCTPK-----VGMVFQESRLMPWLNVSE 96
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDitGLPPHEraragIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILL--HTEKDNRNKVDLDKYLKMM-KLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALdyftRRKMQKE 173
Cdd:cd03224 95 NLLLgaYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL----APKIVEE 170
|
170 180
....*....|....*....|....*....
gi 497578899 174 VVN-IHKNTKKG--VVFVTHNIEEAMEIA 199
Cdd:cd03224 171 IFEaIRELRDEGvtILLVEQNARFALEIA 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-194 |
1.07e-27 |
|
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: 105.94 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGN-IYFFNNDKKCT------PKVGMVfqESRLMPWLN 93
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEdvwelrKRIGLV--SPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSENIL------------LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:COG1119 93 RDETVLdvvlsgffdsigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180 190
....*....|....*....|....*....|...
gi 497578899 162 LDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEE 194
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGAPTLVLVTHHVEE 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
9-198 |
4.06e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.34 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP-------KVGM 81
Cdd:COG1137 7 ENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL--DGEDITHlpmhkraRLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VF--QESRLMPWLNVSENIL--LHTEKDNRNKVD--LDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLM 155
Cdd:COG1137 81 GYlpQEASIFRKLTVEDNILavLELRKLSKKEREerLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497578899 156 DEPFAALDYFTRRKMQKEvvnIHKNTKKGV-VFVT-HNIEEAMEI 198
Cdd:COG1137 161 DEPFAGVDPIAVADIQKI---IRHLKERGIgVLITdHNVRETLGI 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-218 |
9.64e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.42 E-value: 9.64e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTPKVGMVF---- 83
Cdd:COG4152 4 LKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLW--DGEPLDPEDRRRIgylp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 QESRLMPWLNVSENIL----LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:COG4152 78 EERGLYPKMKVGEQLVylarLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 160 AALDYFTRRKMQKEVVNiHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:COG4152 158 SGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-214 |
1.90e-26 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 101.52 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 13 KKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFF----NNDKKCTPKVGMVFQESRL 88
Cdd:cd03268 8 KTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDgksyQKNIEALRRIGALIEAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 89 MPWLNVSENILLHTEKDNRNKVDLDKYLKMMKL-----EKFKNsypneLSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:cd03268 84 YPNLTARENLRLLARLLGIRKKRIDEVLDVVGLkdsakKKVKG-----FSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497578899 164 YFTRRKMQKEVVNiHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQF 214
Cdd:cd03268 159 PDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
24-195 |
2.11e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 102.16 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSG-------NIYFFNNDKKCTPK---VGMVFQESRLMPWLN 93
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGevslvgqPLHQMDEEARAKLRakhVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSENI----LLHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRK 169
Cdd:PRK10584 105 ALENVelpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180
....*....|....*....|....*.
gi 497578899 170 MQKEVVNIHKNTKKGVVFVTHNIEEA 195
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
8-209 |
2.37e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 101.50 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISsEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-----KVGMV 82
Cdd:cd03264 3 LENLTKRY----GKKRALDGVSLTLG-PGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPqklrrRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLNVSENI----LLHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyiaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03264 158 TAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGK 206
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-218 |
4.46e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.79 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN-------NDKKCTP---KVGMVFQ--ESRL 88
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErvitagkKNKKLKPlrkKVGIVFQfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 89 MPwLNVSENILLH------TEKDNRNKVDldkylKMMKL----EKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:PRK13634 99 FE-ETVEKDICFGpmnfgvSEEDAKQKAR-----EMIELvglpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPRE 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
9-230 |
5.13e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-------KVGM 81
Cdd:PRK10895 7 KNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhararrGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSENIL--LHTEKDNRNKVDLDKYLKMMK---LEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMD 156
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMavLQIRDDLSAEQREDRANELMEefhIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 157 EPFAALDYFTRRKMQKEVVNIhKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDLTKNYYI 230
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
25-176 |
5.75e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 103.27 E-value: 5.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTPKVGMVFQE--SRLMPWLN 93
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitglsgrelRPLRRRMQMVFQDpyASLNPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 V----SENILLHTEKDNRNKvdLDKYLKMMKL----EKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYf 165
Cdd:COG4608 114 VgdiiAEPLRIHGLASKAER--RERVAELLELvglrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDV- 190
|
170
....*....|.
gi 497578899 166 trrKMQKEVVN 176
Cdd:COG4608 191 ---SIQAQVLN 198
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
8-205 |
6.33e-26 |
|
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: 100.97 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-------KKCTPKVG 80
Cdd:cd03219 3 VRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDitglpphEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 81 MVFQESRLMPWLNVSENILL----------------HTEKDNRNKVdlDKYLKMMKLEKFKNSYPNELSGGMAHRVSIAR 144
Cdd:cd03219 79 RTFQIPRLFPELTVLENVMVaaqartgsglllararREEREARERA--EELLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 145 ALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNtKKGVVFVTHNIEEAMEIAKKIIVF 205
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVL 216
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
8-209 |
6.68e-26 |
|
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: 100.74 E-value: 6.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGM 81
Cdd:cd03245 5 FRNVSFSY--PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDpadlrrNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMpWLNVSENILL-HTEKDNRnkvDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFN 149
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLgAPLADDE---RILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 150 PDILLMDEPFAALDYFTRRKMQKEVvnihKNTKKG--VVFVTHNIeEAMEIAKKIIVFSKNK 209
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERL----RQLLGDktLIIITHRP-SLLDLVDRIIVMDSGR 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-166 |
8.64e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 100.42 E-value: 8.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAG-LEN--ATSGNIYFFN--NDKKCTPK-VGM 81
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrVEGggTTSGQILFNGqpRKPDQFQKcVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSE------NILLHTEKDN--RNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDIL 153
Cdd:cd03234 86 VRQDDILLPGLTVREtltytaILRLPRKSSDaiRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170
....*....|...
gi 497578899 154 LMDEPFAALDYFT 166
Cdd:cd03234 166 ILDEPTSGLDSFT 178
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-204 |
2.25e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 101.71 E-value: 2.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 26 DNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK--------VGMVFQE--SRLMPWLNV 94
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDlLGMKDDewravrsdIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENIL--LHTEKDNRNKVDLDKYLK--MMK---LEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYftr 167
Cdd:PRK15079 118 GEIIAepLRTYHPKLSRQEVKDRVKamMLKvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV--- 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497578899 168 rKMQKEVVNIHKNTKK----GVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK15079 195 -SIQAQVVNLLQQLQRemglSLIFIAHDLAVVKHISDRVLV 234
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
24-204 |
3.67e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 99.34 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTP----KVGMV--FQESRLMPWLNVSE 96
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDiTGLPPhriaRLGIArtFQNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILL---------------------HTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLM 155
Cdd:COG0411 99 NVLVaaharlgrgllaallrlprarREEREARERAE--ELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497578899 156 DEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVV 225
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-204 |
4.69e-25 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 97.93 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 17 VDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFnndkkctPKVGMVFQEsrlmPWL---N 93
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-------GSIAYVSQE----PWIqngT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSENILLHTEKDNR--NKV----DLDKYLKMMKL-------EKFKNsypneLSGGMAHRVSIARALSFNPDILLMDEPFA 160
Cdd:cd03250 82 IRENILFGKPFDEEryEKVikacALEPDLEILPDgdlteigEKGIN-----LSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 497578899 161 ALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIeEAMEIAKKIIV 204
Cdd:cd03250 157 AVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHADQIVV 199
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-209 |
5.21e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 99.27 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 1 MVRSGFLLENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNN--------- 71
Cdd:PRK10619 1 MSENKLNVIDLHKRY----GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkd 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 72 ------DKK----CTPKVGMVFQESRLMPWLNVSENI-------LLHTEKDNRNKVDldKYLKMMKL-EKFKNSYPNELS 133
Cdd:PRK10619 77 gqlkvaDKNqlrlLRTRLTMVFQHFNLWSHMTVLENVmeapiqvLGLSKQEARERAV--KYLAKVGIdERAQGKYPVHLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 134 GGMAHRVSIARALSFNPDILLMDEPFAALDyftrRKMQKEVVNIHKNTK---KGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALD----PELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
25-227 |
5.59e-25 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 100.16 E-value: 5.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-----KKCTPKVGMVFQESRLMPWLNVSENIL 99
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDvvrepRKVRRSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 100 LHTE-----KDNRNKvDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEV 174
Cdd:TIGR01188 89 MMGRlyglpKDEAEE-RAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497578899 175 VNIhKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEdEYNRDLTKN 227
Cdd:TIGR01188 168 RAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE-ELKRRLGKD 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
8-213 |
5.63e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 97.74 E-value: 5.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP--KVGMVFQE 85
Cdd:cd03269 3 VENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAArnRIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 86 SRLMPWLNVSENIL----LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:cd03269 79 RGLYPKMKVIDQLVylaqLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497578899 162 LDYFTRRKMqKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:cd03269 159 LDPVNVELL-KDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-212 |
8.99e-25 |
|
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: 101.80 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYL-VDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF-------------FNNDK 73
Cdd:TIGR03269 282 VRNVSKRYIsVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvdmtkpgPDGRG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 74 KCTPKVGMVFQESRLMPWLNVSENIllhTEKDNrnkVDLDKYLKMMKL--------------EKFKNSYPNELSGGMAHR 139
Cdd:TIGR03269 362 RAKRYIGILHQEYDLYPHRTVLDNL---TEAIG---LELPDELARMKAvitlkmvgfdeekaEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 140 VSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIK 212
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-207 |
1.74e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 101.39 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 19 NKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK-----VGMVFQEsrlmPWL 92
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDiRDLTLEslrrqIGVVPQD----TFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 ---NVSENILLHteKDNRNKVDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:COG1132 426 fsgTIRENIRYG--RPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNIEEAMEiAKKIIVFSK 207
Cdd:COG1132 504 TSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDD 549
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-207 |
2.86e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 96.63 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 2 VRSGFLLENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF-----FNNDKKCT 76
Cdd:cd03267 14 SKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVaglvpWKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 77 PKVGMVF-QESRLMPWLNVSENILLHTE----KDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPD 151
Cdd:cd03267 94 RRIGVVFgQKTQLWWDLPVIDSFYLLAAiydlPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 152 ILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSK 207
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-206 |
3.01e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.16 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLEN-----ATSGNIYFFN---NDKKCTP-----KVGMVFQESRL 88
Cdd:PRK14243 23 FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGknlYAPDVDPvevrrRIGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 89 MPwLNVSENILlHTEKDNRNKVDLD----KYLKMMKL-----EKFKNSyPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:PRK14243 103 FP-KSIYDNIA-YGARINGYKGDMDelveRSLRQAALwdevkDKLKQS-GLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497578899 160 AALDYFTRRKMQkEVVNIHKNtKKGVVFVTHNIEEAMEIAKKIIVFS 206
Cdd:PRK14243 180 SALDPISTLRIE-ELMHELKE-QYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-204 |
5.24e-24 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 99.83 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP--------KVGMVFQESRLMPWl 92
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILI--NGVDLSDldpaswrrQIAWVPQNPYLFAG- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENILLHteKDNRNKVDLDKYLKMMKLEKFKNSYPN-------E----LSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:COG4988 426 TIRENLRLG--RPDASDEELEAALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAH 503
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497578899 162 LDYFTRRKMQKEVVNIHKNtkKGVVFVTHNIeEAMEIAKKIIV 204
Cdd:COG4988 504 LDAETEAEILQALRRLAKG--RTVILITHRL-ALLAQADRILV 543
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
10-202 |
5.44e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.04 E-value: 5.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 10 NIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN---NDKKCTPK-------V 79
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmSKLSSAAKaelrnqkL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 80 GMVFQESRLMPWLNVSENIL--LHTEKDNRNKVDlDKYLKMMK---LEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:PRK11629 90 GFIYQFHHLLPDFTALENVAmpLLIGKKKPAEIN-SRALEMLAavgLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 155 MDEPFAALDyftrrkmQKEVVNIHK-----NTKKGVVF--VTHNIEEAMEIAKKI 202
Cdd:PRK11629 169 ADEPTGNLD-------ARNADSIFQllgelNRLQGTAFlvVTHDLQLAKRMSRQL 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
9-213 |
6.58e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 96.70 E-value: 6.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYLVD--NKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-------KV 79
Cdd:PRK13633 8 KNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdirnKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 80 GMVFQ--ESRLMPWLnVSENILLHTE------KDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPD 151
Cdd:PRK13633 88 GMVFQnpDNQIVATI-VEEDVAFGPEnlgippEEIRERVD--ESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 152 ILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEiAKKIIVFSKNKRIKQ 213
Cdd:PRK13633 165 CIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
25-231 |
7.62e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.82 E-value: 7.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNI----YFFN------NDKKCTPKVGMVFQesrlMPWLNV 94
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItiagYHITpetgnkNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLH-----------TEKDNRNKVDldKYLKMMKL-EKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:PRK13641 99 FENTVLKdvefgpknfgfSEDEAKEKAL--KWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 163 DyftrRKMQKEVVNIHKNTKKG---VVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEY-NRDLTKNYYIN 231
Cdd:PRK13641 177 D----PEGRKEMMQLFKDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFsDKEWLKKHYLD 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-228 |
9.12e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 95.75 E-value: 9.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGL-----ENATSGNIYFFNNDKKCTP------KVGMVFQESRLMPWL 92
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDvielrrRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENILLHTeKDNR---NKVDLDKYLKMmKLEKFK---------NSYPNELSGGMAHRVSIARALSFNPDILLMDEPFA 160
Cdd:PRK14247 98 SIFENVALGL-KLNRlvkSKKELQERVRW-ALEKAQlwdevkdrlDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 161 ALDYFTRRKMQKEVVNIHKNTKkgVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNR---DLTKNY 228
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMT--IVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNprhELTEKY 244
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-213 |
9.31e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 95.25 E-value: 9.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDnkEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPK------VGM 81
Cdd:cd03252 3 FEHVRFRYKPD--GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPawlrrqVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLmpwLN--VSENILLHTEKDNRNKVDLDKYLK-----MMKLEKFKNSYPNE----LSGGMAHRVSIARALSFNP 150
Cdd:cd03252 81 VLQENVL---FNrsIRDNIALADPGMSMERVIEAAKLAgahdfISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 151 DILLMDEPFAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNIEEAMEiAKKIIVFSKNKRIKQ 213
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQ 217
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
8-203 |
1.10e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.03 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSG-------NIYFFNNDKKCTPK-- 78
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLRre 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 -VGMVFQESRLMPWLNVSEN-----ILLHTEKDNRNK--VDLdkyLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNP 150
Cdd:PRK10535 87 hFGFIFQRYHLLSHLTAAQNvevpaVYAGLERKQRLLraQEL---LQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 151 DILLMDEPFAALDYFTrrkmQKEVVNI-HKNTKKG--VVFVTHNIEEAMEiAKKII 203
Cdd:PRK10535 164 QVILADEPTGALDSHS----GEEVMAIlHQLRDRGhtVIIVTHDPQVAAQ-AERVI 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
8-204 |
1.18e-23 |
|
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: 99.07 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK-----VGM 81
Cdd:COG4987 336 LEDVSFRY--PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDlRDLDEDdlrrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMpwlN--VSENILLhtEKDNRNKVDLDKYLKMMKLEKFKNSYPN-------E----LSGGMAHRVSIARALSF 148
Cdd:COG4987 414 VPQRPHLF---DttLRENLRL--ARPDATDEELWAALERVGLGDWLAALPDgldtwlgEggrrLSGGERRRLALARALLR 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 149 NPDILLMDEPFAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNiEEAMEIAKKIIV 204
Cdd:COG4987 489 DAPILLLDEPTEGLDAATEQALLADLLEALAG--RTVLLITHR-LAGLERMDRILV 541
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
8-204 |
2.03e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 92.66 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCT------PKVGM 81
Cdd:cd03246 3 VENVSFRY--PGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWdpnelgDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWlNVSENIllhtekdnrnkvdldkylkmmklekfknsypneLSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:cd03246 81 LPQDDELFSG-SIAENI---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497578899 162 LDYFTRRKMQKEVVNIhKNTKKGVVFVTHNIeEAMEIAKKIIV 204
Cdd:cd03246 127 LDVEGERALNQAIAAL-KAAGATRIVIAHRP-ETLASADRILV 167
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-214 |
2.83e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.72 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGL-----ENATSGNIYFFN--------NDKKCTPKVGMVFQESRLMP 90
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNqniyerrvNLNRLRRQVSMVHPKPNLFP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 91 wLNVSENILLHTEKDN-RNKVDLD----KYLKMMKL-EKFKNSYPN---ELSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:PRK14258 102 -MSVYDNVAYGVKIVGwRPKLEIDdiveSALKDADLwDEIKHKIHKsalDLSGGQQQRLCIARALAVKPKVLLMDEPCFG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 162 LDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK-RIKQF 214
Cdd:PRK14258 181 LDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNEnRIGQL 234
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-213 |
4.08e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-----KKCTPKVGMV 82
Cdd:PRK13537 10 FRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPvpsraRHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLNVSENILLH------TEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMD 156
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFgryfglSAAAARALVP--PLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 157 EPFAALDYFTRRKMQKEVVNIHKNTKKgVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:PRK13537 164 EPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAE 219
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
26-222 |
6.78e-23 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 92.82 E-value: 6.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 26 DNISLNISSEEITVILGESGCGKTT----LLRILAGLENATSGNIYFfnNDKKCTP------KVGMVFQESR--LMPWLN 93
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILL--DGRPLLPlsirgrHIATIMQNPRtaFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VS----ENILLHT--EKDNRN-------KVDLDKYLKMMKlekfknSYPNELSGGMAHRVSIARALSFNPDILLMDEPFA 160
Cdd:TIGR02770 81 MGnhaiETLRSLGklSKQARAlilealeAVGLPDPEEVLK------KYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 161 ALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNR 222
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYN 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
8-224 |
1.79e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.88 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKehlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFF------NNDKKCTPKVGM 81
Cdd:PRK13647 7 VEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMgrevnaENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQES-----RLMPWLNVS---ENI-LLHTEKDNRnkvdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:PRK13647 84 VFQDPddqvfSSTVWDDVAfgpVNMgLDKDEVERR----VEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 153 LLMDEPFAALDYFTRRKMqKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDL 224
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDI 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-235 |
3.28e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.76 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLR------------ILAGLENATSGNIYFFNNDK-KCTPKVGMVFQESRLMPw 91
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRsinrmndlnpevTITGSIVYNGHNIYSPRTDTvDLRKEIGMVFQQPNPFP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 LNVSENIL----LHTEKDnRNKVD--LDKYLKMMKL-EKFKNSYPNE---LSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:PRK14239 100 MSIYENVVyglrLKGIKD-KQVLDeaVEKSLKGASIwDEVKDRLHDSalgLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 162 LDYFTRRKMQKEVVNIHKntKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIkqfsvedEYNRdlTKNYYINLKKE 235
Cdd:PRK14239 179 LDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASRISDRTGFFLDGDLI-------EYND--TKQMFMNPKHK 241
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
8-213 |
4.41e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 90.75 E-value: 4.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCT-----PKVGM 81
Cdd:cd03253 3 FENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDiREVTldslrRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLmpwLN--VSENILLhtEKDNRNKVDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSF 148
Cdd:cd03253 80 VPQDTVL---FNdtIGYNIRY--GRPDATDEEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 149 NPDILLMDEPFAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNIEEAMEiAKKIIVFSKNKRIKQ 213
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTIVN-ADKIIVLKDGRIVER 216
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
24-190 |
4.80e-22 |
|
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: 89.53 E-value: 4.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLEN--ATSGNIYF--FNNDKKCTPK-VGMVFQESRLMPWLNVSENI 98
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLIngRPLDKRSFRKiIGYVPQDDILHPTLTVRETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 LLHTEkdnrnkvdldkyLKmmklekfknsypnELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIh 178
Cdd:cd03213 104 MFAAK------------LR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL- 157
|
170
....*....|..
gi 497578899 179 KNTKKGVVFVTH 190
Cdd:cd03213 158 ADTGRTIICSIH 169
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-209 |
7.45e-22 |
|
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: 89.90 E-value: 7.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNK------------------EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyff 69
Cdd:cd03220 3 LENVSKSYPTYKGgssslkklgilgrkgevgEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 70 NNDKKCTPKVGMvfqESRLMPWLNVSENILL------HTEKDNRNKVDldkYLKMM-KLEKFKNSYPNELSGGMAHRVSI 142
Cdd:cd03220 80 TVRGRVSSLLGL---GGGFNPELTGRENIYLngrllgLSRKEIDEKID---EIIEFsELGDFIDLPVKTYSSGMKARLAF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 143 ARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTkKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03220 154 AIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQG-KTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
24-192 |
7.46e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 90.90 E-value: 7.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTPKVGMVFQES--RLMPWL 92
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPlaklnraqrKAFRRDIQMVFQDSisAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENI---LLH--TEKDNRNKVDLDKYLKMMKL-EKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDyft 166
Cdd:PRK10419 107 TVREIIrepLRHllSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD--- 183
|
170 180 190
....*....|....*....|....*....|
gi 497578899 167 rRKMQKEVVNIHKNTKK----GVVFVTHNI 192
Cdd:PRK10419 184 -LVLQAGVIRLLKKLQQqfgtACLFITHDL 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
9-213 |
8.14e-22 |
|
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: 89.98 E-value: 8.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGMV 82
Cdd:cd03254 6 ENVNFSY---DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISrkslrsMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWlNVSENILLHTEKDNRNKV-DLDKYLKM----MKLEKFKNSYPNE----LSGGMAHRVSIARALSFNPDIL 153
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNATDEEViEAAKEAGAhdfiMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 154 LMDEPFAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNIeEAMEIAKKIIVFSKNKRIKQ 213
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRL-STIKNADKILVLDDGKIIEE 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-213 |
8.83e-22 |
|
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: 89.91 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGMVFQESRLMPwLNV 94
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNlrwlrsQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLhtEKDNRNKVDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:cd03249 94 AENIRY--GKPDATDEEVEEAAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 164 YFTRRKMQKEVVNIHKNTKkgVVFVTHNIeEAMEIAKKIIVFSKNKRIKQ 213
Cdd:cd03249 172 AESEKLVQEALDRAMKGRT--TIVIAHRL-STIRNADLIAVLQNGQVVEQ 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-218 |
9.13e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.14 E-value: 9.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCT---PK------VGMVFQESRLMPWLNVS 95
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILY--LGKEVTfngPKssqeagIGIIHQELNLIPQLTIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENILLHTEKDNR------NKV--DLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALdyfTR 167
Cdd:PRK10762 98 ENIFLGREFVNRfgridwKKMyaEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL---TD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497578899 168 RKMQK--EVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:PRK10762 175 TETESlfRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-230 |
1.23e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.11 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 10 NIYKKYLVDNkEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGL------ENATSGNIYFFNNDK------KCTP 77
Cdd:PRK14246 12 NISRLYLYIN-DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIfqidaiKLRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 KVGMVFQESRLMPWLNVSENILL----HTEKDNRN-KVDLDKYLKMMKLEK----FKNSYPNELSGGMAHRVSIARALSF 148
Cdd:PRK14246 91 EVGMVFQQPNPFPHLSIYDNIAYplksHGIKEKREiKKIVEECLRKVGLWKevydRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 149 NPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTkkGVVFVTHNIEEAMEIAkKIIVFSKNKRIKQFSVEDEY----NRDL 224
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNEI--AIVIVSHNPQQVARVA-DYVAFLYNGELVEWGSSNEIftspKNEL 247
|
....*.
gi 497578899 225 TKNYYI 230
Cdd:PRK14246 248 TEKYVI 253
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-204 |
1.39e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.18 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND---------KKCTPKVGMVFQE--SRLMPWLN 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkadpeaqKLLRQKIQIVFQNpyGSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VS----ENILLHTE---KDNRNKVdldkyLKMMKL----EKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:PRK11308 111 VGqileEPLLINTSlsaAERREKA-----LAMMAKvglrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497578899 163 DYftrrKMQKEVVN----IHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK11308 186 DV----SVQAQVLNlmmdLQQELGLSYVFISHDLSVVEHIADEVMV 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-197 |
2.00e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.06 E-value: 2.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyffnnDKKCTPKVGMVFQESRL---MPwLNVSENI 98
Cdd:NF040873 5 RPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----RRAGGARVAYVPQRSEVpdsLP-LTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 LL-----------HTEKDNRnkvDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:NF040873 79 AMgrwarrglwrrLTRDDRA---AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|
gi 497578899 168 RKMQKEVVNIHKnTKKGVVFVTHNIEEAME 197
Cdd:NF040873 156 ERIIALLAEEHA-RGATVVVVTHDLELVRR 184
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-199 |
3.74e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 88.75 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGL-----ENATSGNIYFFNND---KKCTP-----KVGMVFQESRLMP 90
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNiysPDVDPievrrEVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 91 WLNVSENILLHTEKDN--RNKVDLDKY----LKMMKL-EKFK---NSYPNELSGGMAHRVSIARALSFNPDILLMDEPFA 160
Cdd:PRK14267 99 HLTIYDNVAIGVKLNGlvKSKKELDERvewaLKKAALwDEVKdrlNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 497578899 161 ALDYFTRRKMQKEVVNIHKNTKkgVVFVTHNIEEAMEIA 199
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEYT--IVLVTHSPAQAARVS 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
8-212 |
7.20e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.99 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEHL-VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNI-YFFNNDKKCTP-------- 77
Cdd:PRK13651 5 VKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIeWIFKDEKNKKKtkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 78 ---------------------KVGMVFQ--ESRLMPwLNVSENIL-----LHTEKDNRNKVDLdKYLKMMKL-EKFKNSY 128
Cdd:PRK13651 85 eklviqktrfkkikkikeirrRVGVVFQfaEYQLFE-QTIEKDIIfgpvsMGVSKEEAKKRAA-KYIELVGLdESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 129 PNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKgVVFVTHNIEEAMEIAKKIIVFSKN 208
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT-IILVTHDLDNVLEWTKRTIFFKDG 241
|
....
gi 497578899 209 KRIK 212
Cdd:PRK13651 242 KIIK 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-226 |
9.25e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.44 E-value: 9.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNK------------------EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYff 69
Cdd:COG1134 7 VENVSKSYRLYHEpsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 70 nNDKKCTP--KVGMVFQesrlmPWLNVSENILL------HTEKDNRNKVD-------LDKYLKM-MKlekfknSYpnelS 133
Cdd:COG1134 85 -VNGRVSAllELGAGFH-----PELTGRENIYLngrllgLSRKEIDEKFDeivefaeLGDFIDQpVK------TY----S 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 134 GGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTkKGVVFVTHNIEEAMEIAKKIIVFSKNkRIKQ 213
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESG-RTVIFVSHSMGAVRRLCDRAIWLEKG-RLVM 226
|
250
....*....|....*..
gi 497578899 214 F-SVED---EYNRDLTK 226
Cdd:COG1134 227 DgDPEEviaAYEALLAG 243
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
8-209 |
1.08e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.15 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFnnDKKCTP--------KV 79
Cdd:PRK13635 8 VEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG--GMVLSEetvwdvrrQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 80 GMVFQ-------------------ESRLMPwlnvsenillHTEKDNRnkvdLDKYLKMMKLEKFKNSYPNELSGGMAHRV 140
Cdd:PRK13635 84 GMVFQnpdnqfvgatvqddvafglENIGVP----------REEMVER----VDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 141 SIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEiAKKIIVFSKNK 209
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGE 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-206 |
1.45e-20 |
|
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: 87.08 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 31 NISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPKVGMVFQESRLMPWLnvSENILLHTEkDNRNKV 110
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLL--SSITKDFYT-HPYFKT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 111 DLdkyLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTH 190
Cdd:cd03237 98 EI---AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEH 174
|
170
....*....|....*.
gi 497578899 191 NIEEAMEIAKKIIVFS 206
Cdd:cd03237 175 DIIMIDYLADRLIVFE 190
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-221 |
1.54e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.50 E-value: 1.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN------NDKKCTPKVGMVFQ--ESRLMPWL 92
Cdd:PRK13648 21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitddNFEKLRKHIGIVFQnpDNQFVGSI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 ---NVS---ENILLHTEKDNRnkvDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFT 166
Cdd:PRK13648 101 vkyDVAfglENHAVPYDEMHR---RVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 167 RRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEiAKKIIVFSKNKRIKQFSVEDEYN 221
Cdd:PRK13648 178 RQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-212 |
1.68e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.37 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 19 NKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIY---FFNND-------------------KKCT 76
Cdd:PRK13631 36 ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQvgdIYIGDkknnhelitnpyskkiknfKELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 77 PKVGMVFQ--ESRLMPwLNVSENILLHT----EKDNRNKVDLDKYLKMMKL-EKFKNSYPNELSGGMAHRVSIARALSFN 149
Cdd:PRK13631 116 RRVSMVFQfpEYQLFK-DTIEKDIMFGPvalgVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 150 PDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKgVVFVTHNIEEAMEIAKKIIVFSKNKRIK 212
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT-VFVITHTMEHVLEVADEVIVMDKGKILK 256
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
25-234 |
2.35e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.48 E-value: 2.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF-------FNNDKKCTP---KVGMVFQ--ESRLMpwl 92
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIKPvrkKVGVVFQfpESQLF--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 nvSENIL---------LHTEKDNRNKVDLDKyLKMMKLEK-FKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:PRK13643 99 --EETVLkdvafgpqnFGIPKEKAEKIAAEK-LEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 163 DYFTRRKMQKEVVNIHKnTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNR-DLTKNYYINLKK 234
Cdd:PRK13643 176 DPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEvDFLKAHELGVPK 247
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
24-194 |
2.39e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.92 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGMVFQesrlMPWL---NV 94
Cdd:PRK10247 22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeiyrqQVSYCAQ----TPTLfgdTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLHTEKDNRnKVDLDKYLKmmKLEKFK------NSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRR 168
Cdd:PRK10247 98 YDNLIFPWQIRNQ-QPDPAIFLD--DLERFAlpdtilTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|....*.
gi 497578899 169 KMQKEVVNIHKNTKKGVVFVTHNIEE 194
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
8-209 |
3.34e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 83.65 E-value: 3.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGniyffnndkkctpkvgmvfqesr 87
Cdd:cd03221 3 LENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG----------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 lmpwlnvsenillhtekdnrnKVDLDKYLKMmklekfknSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:cd03221 56 ---------------------IVTWGSTVKI--------GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497578899 168 RKMQKEVvnihKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:cd03221 107 EALEEAL----KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-207 |
3.51e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 84.41 E-value: 3.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTPKV-------GMVF-QESR----LM 89
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITL--DGKPVTRRSprdairaGIAYvPEDRkregLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 90 PWLNVSENILLhtekdnrnkvdldkylkmmklekfknsyPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRK 169
Cdd:cd03215 91 LDLSVAENIAL----------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190
....*....|....*....|....*....|....*...
gi 497578899 170 MQKeVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSK 207
Cdd:cd03215 143 IYR-LIRELADAGKAVLLISSELDELLGLCDRILVMYE 179
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-204 |
4.59e-20 |
|
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: 88.50 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP--------KVGMVFQEsrlmPWL--- 92
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAV--NGVPLADadadswrdQIAWVPQH----PFLfag 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENILLH----TEKDNRN---KVDLDKYLKMMK--LEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:TIGR02857 411 TIAENIRLArpdaSDAEIREaleRAGLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497578899 164 YFTRRKMQKEVVNIHKNtkKGVVFVTHNIeEAMEIAKKIIV 204
Cdd:TIGR02857 491 AETEAEVLEALRALAQG--RTVLLVTHRL-ALAALADRIVV 528
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-204 |
8.30e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.82 E-value: 8.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLEnATSGNIYFFNND------KKCTP---KVGMVFQE--SRLMPWLN 93
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDldglsrRALRPlrrRMQVVFQDpfGSLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 V----SENILLH------TEKDNR-----NKVDLDkylkmmklEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:COG4172 381 VgqiiAEGLRVHgpglsaAERRARvaealEEVGLD--------PAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 159 FAALDyftrRKMQKEVVNIHKN--TKKGV--VFVTHNIEEAMEIAKKIIV 204
Cdd:COG4172 453 TSALD----VSVQAQILDLLRDlqREHGLayLFISHDLAVVRALAHRVMV 498
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-163 |
9.83e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 9.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 1 MVRsgflLENIYKKYLVDNKehlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-----KKC 75
Cdd:PRK10908 1 MIR----FEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrlkNRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 76 TP----KVGMVFQESRLMPWLNVSENILL------HTEKDNRNKVD--LDKylkMMKLEKFKNsYPNELSGGMAHRVSIA 143
Cdd:PRK10908 74 VPflrrQIGMIFQDHHLLMDRTVYDNVAIpliiagASGDDIRRRVSaaLDK---VGLLDKAKN-FPIQLSGGEQQRVGIA 149
|
170 180
....*....|....*....|
gi 497578899 144 RALSFNPDILLMDEPFAALD 163
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLD 169
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-199 |
1.01e-19 |
|
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: 84.65 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND--KKCTPK-----VGMVFQESRLMPWLNVSE 96
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDitGLPPHRiarlgIGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILL--HTEKDNRN-KVDLDKYLKMM-KLEKFKNSYPNELSGG---MahrVSIARALSFNPDILLMDEPFAALDyftrRK 169
Cdd:COG0410 98 NLLLgaYARRDRAEvRADLERVYELFpRLKERRRQRAGTLSGGeqqM---LAIGRALMSRPKLLLLDEPSLGLA----PL 170
|
170 180 190
....*....|....*....|....*....|...
gi 497578899 170 MQKEVVNI---HKNTKKGVVFVTHNIEEAMEIA 199
Cdd:COG0410 171 IVEEIFEIirrLNREGVTILLVEQNARFALEIA 203
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
24-228 |
1.91e-19 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 83.73 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPK-------VGMVFQESRLMPWLNVSE 96
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPheraragIAYVPQGREIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILLHTE--KDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPfaaldyfTR------- 167
Cdd:TIGR03410 95 NLLTGLAalPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP-------TEgiqpsii 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 168 RKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNkRIKQFSVEDEYNRDLTKNY 228
Cdd:TIGR03410 168 KDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERG-RVVASGAGDELDEDKVRRY 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-191 |
2.49e-19 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 86.28 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 18 DNKEHLVLDNISLNISSEEITVILGESGCGKT----TLLRILAGLENATSGNIYFfnNDK---KCTPK---------VGM 81
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILF--DGQdllGLSERelrrirgnrIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESrlMPWLN--------VSENILLH---TEKDNRNKV-DLdkyLKMMKL---EKFKNSYPNELSGGMAHRVSIARAL 146
Cdd:COG4172 97 IFQEP--MTSLNplhtigkqIAEVLRLHrglSGAAARARAlEL---LERVGIpdpERRLDAYPHQLSGGQRQRVMIAMAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497578899 147 SFNPDILLMDEPFAALDYFTrrkmQKEVVNIHKNTKK----GVVFVTHN 191
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTV----QAQILDLLKDLQRelgmALLLITHD 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
21-203 |
3.91e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.52 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGL---ENATSGNIYFFNNDKKCTPKV-----------GMVFQES 86
Cdd:PRK09984 16 QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRLardirksrantGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 87 RLMPWLNVSENILLHTEKDN------------RNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:PRK09984 96 NLVNRLSVLENVLIGALGSTpfwrtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKII 203
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
25-209 |
4.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKkCTPK--------VGMVFQ--ESRLMPwLNV 94
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDT-GDFSklqgirklVGIVFQnpETQFVG-RTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLHTEK------DNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRR 168
Cdd:PRK13644 96 EEDLAFGPENlclppiEIRKRVD--RALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497578899 169 KMQKEVVNIHKNTKKgVVFVTHNIEEaMEIAKKIIVFSKNK 209
Cdd:PRK13644 174 AVLERIKKLHEKGKT-IVYITHNLEE-LHDADRIIVMDRGK 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-211 |
4.39e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 84.50 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN-----NDKKCTPKVGMVFQESRLMPWLNVSENI 98
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpaRARLARARIGVVPQFDNLDLEFTVRENL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 LLHTEKDNRNKVDLD----KYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEV 174
Cdd:PRK13536 136 LVFGRYFGMSTREIEavipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL 215
|
170 180 190
....*....|....*....|....*....|....*..
gi 497578899 175 VNIHKNTKKgVVFVTHNIEEAMEIAKKIIVFSKNKRI 211
Cdd:PRK13536 216 RSLLARGKT-ILLTTHFMEEAERLCDRLCVLEAGRKI 251
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-215 |
5.35e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 5.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGL-----------ENATSGNIYFFNNDKKCTPKVGMVFQESRLM 89
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiisetgqtivgDYAIPANLKKIKEVKRLRKEIGLVFQFPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 90 PWLNVSEN------ILLHTEKDNRNKvDLDKYLKMMKL-EKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:PRK13645 103 LFQETIEKdiafgpVNLGENKQEAYK-KVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497578899 163 DYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFS 215
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
25-226 |
7.31e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 7.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK------VGMVFQESRLMPWLNVSEN 97
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINyNKLDHKlaaqlgIGIIYQELSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 IL---LHTEKD-NRNKVDLDKY-------LKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALdyft 166
Cdd:PRK09700 101 LYigrHLTKKVcGVNIIDWREMrvraammLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL---- 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 167 rrkMQKEV------VNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDLTK 226
Cdd:PRK09700 177 ---TNKEVdylfliMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-209 |
9.56e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 85.07 E-value: 9.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCT-----PKVGMVFQESRLMPWLNVSENIL 99
Cdd:TIGR01257 946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNldavrQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 100 LHTEKDNRN----KVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVV 175
Cdd:TIGR01257 1026 FYAQLKGRSweeaQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLL 1105
|
170 180 190
....*....|....*....|....*....|....
gi 497578899 176 NIHknTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:TIGR01257 1106 KYR--SGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
8-219 |
1.18e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.47 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP--------KV 79
Cdd:PRK13650 7 VKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII--DGDLLTEenvwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 80 GMVFQE-SRLMPWLNVSENILLHTE------KDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:PRK13650 84 GMVFQNpDNQFVGATVEDDVAFGLEnkgiphEEMKERVN--EALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 153 LLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEaMEIAKKIIVFsKNKRIKQFSVEDE 219
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVM-KNGQVESTSTPRE 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
24-221 |
1.24e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 82.45 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSG------------NIYFFNNDKKCTPKVGMVFQESRLMPw 91
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrSIFNYRDVLEFRRRVGMLFQRPNPFP- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 LNVSENIL-------LHTEKDNR-------NKVDLDKYLKmmklEKFKNSyPNELSGGMAHRVSIARALSFNPDILLMDE 157
Cdd:PRK14271 115 MSIMDNVLagvrahkLVPRKEFRgvaqarlTEVGLWDAVK----DRLSDS-PFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 158 PFAALDYFTRRKMQKEVVNIHKntKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYN 221
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
25-193 |
1.54e-18 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 81.22 E-value: 1.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfNNDKKCTPKVGMVFQESRL-------MPWL---NV 94
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHW-SNKNESEPSFEATRSRNRYsvayaaqKPWLlnaTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLHTE-KDNRNKVDLDKYLKMMKLEKFKNSYPNE-------LSGGMAHRVSIARALSFNPDILLMDEPFAALD-YF 165
Cdd:cd03290 96 EENITFGSPfNKQRYKAVTDACSLQPDIDLLPFGDQTEigerginLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHL 175
|
170 180
....*....|....*....|....*...
gi 497578899 166 TRRKMQKEVVNIHKNTKKGVVFVTHNIE 193
Cdd:cd03290 176 SDHLMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-223 |
1.81e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.13 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGN-------IYFFNNDKKCTP---KVGMVFQ--ESRL 88
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTvtvdditITHKTKDKYIRPvrkRIGMVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 89 MPwLNVSENILLHTEKDNRN--KVDLDKYLKMMKLEKFKN---SYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PRK13646 99 FE-DTVEREIIFGPKNFKMNldEVKNYAHRLLMDLGFSRDvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 164 YFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRD 223
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
25-212 |
3.58e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 81.33 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFF---------NND-KKCTPKVGMVFQ--ESRLMpwl 92
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDdtlitstskNKDiKQIRKKVGLVFQfpESQLF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 nvSENIL---------LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PRK13649 100 --EETVLkdvafgpqnFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 497578899 164 YFTRRKMQKEVVNIHKNTKKgVVFVTHNIEEAMEIAKKIIVFSKNKRIK 212
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMT-IVLVTHLMDDVANYADFVYVLEKGKLVL 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-223 |
5.64e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.62 E-value: 5.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN------NDKKCTPKVGMVFQESRLMPWLNVSE- 96
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepitkeNIREVRKFVGLVFQNPDDQIFSPTVEq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 -------NILLHTEKDNRNkvdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRK 169
Cdd:PRK13652 99 diafgpiNLGLDEETVAHR---VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 170 MQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRD 223
Cdd:PRK13652 176 LIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-190 |
6.13e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyFFNNDKkctpKVGMVFQESR 87
Cdd:COG0488 1 LENLSKSF--GGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGL----RIGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 LMPWLNVSENIL--------LHTEKDNRNKVDLDKYLKMMKLEK-------------------------FKNSYPN---- 130
Cdd:COG0488 72 LDDDLTVLDTVLdgdaelraLEAELEELEAKLAEPDEDLERLAElqeefealggweaearaeeilsglgFPEEDLDrpvs 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 131 ELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVvnihKNTKKGVVFVTH 190
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFL----KNYPGTVLVVSH 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
21-198 |
1.51e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 1.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYfFNNDKKCTPKVGMVFQ----ESRLMPWLNVSE 96
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEACHylghRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILLHTEKDNRNKVDLDKYLKMMKLE-----KFKNsypneLSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRkMQ 171
Cdd:PRK13539 93 NLEFWAAFLGGEELDIAAALEAVGLAplahlPFGY-----LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA-LF 166
|
170 180 190
....*....|....*....|....*....|
gi 497578899 172 KEVVNIHKNTKKGVVFVTHN---IEEAMEI 198
Cdd:PRK13539 167 AELIRAHLAQGGIVIAATHIplgLPGAREL 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
8-213 |
2.18e-17 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 76.97 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnnDKKCTPKVGMvfQESR 87
Cdd:cd03247 3 INNVSFSY--PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITL---DGVPVSDLEK--ALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 LMPWLNVSENILLHTEKDNRNKvdldkylkmmklekfknsypnELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:cd03247 76 LISVLNQRPYLFDTTLRNNLGR---------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497578899 168 RKMQKEVVNIHKNtkKGVVFVTHNIeEAMEIAKKIIVFSKNKRIKQ 213
Cdd:cd03247 135 RQLLSLIFEVLKD--KTLIWITHHL-TGIEHMDKILFLENGKIIMQ 177
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-217 |
3.14e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 27 NISLNISSEEITVILGESGCGKT-TLLRILAGLENA----TSGNIYFFNNDKKCT---------------PKVGMVFQES 86
Cdd:PRK10261 34 NLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvQCDKMLLRRRSRQVIelseqsaaqmrhvrgADMAMIFQEP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 87 rlMPWLN--------VSENILLHT-----EKDNRNKVDLDKyLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDIL 153
Cdd:PRK10261 114 --MTSLNpvftvgeqIAESIRLHQgasreEAMVEAKRMLDQ-VRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 154 LMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVE 217
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-223 |
3.19e-17 |
|
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: 77.66 E-value: 3.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND------KKCTPKVGM 81
Cdd:cd03251 3 FKNVTFRY--PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDvrdytlASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWlNVSENILLHTEKDNRNKVDldKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNP 150
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGRPGATREEVE--EAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 151 DILLMDEPFAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNIeEAMEIAKKIIVFSKNKRIKQFSVEDEYNRD 223
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-192 |
4.65e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGM 81
Cdd:COG4604 4 IKNVSKRY----GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsrelakRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMPWLNVSEniLL-----------HTEKDnRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNP 150
Cdd:COG4604 80 LRQENHINSRLTVRE--LVafgrfpyskgrLTAED-REIID--EAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497578899 151 DILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNI 192
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDI 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-211 |
5.47e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 79.48 E-value: 5.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGL--ENATSGNIYFFNNDKKC-----TPKVGMVF--QESRLMPWLNVS 95
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKAsnirdTERAGIVIihQELTLVPELSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENILLHTE---KDNRNKVDL-----DKYLKMMKLEKFKNSYP-NELSGGMAHRVSIARALSFNPDILLMDEPFAALdyfT 166
Cdd:TIGR02633 97 ENIFLGNEitlPGGRMAYNAmylraKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL---T 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 497578899 167 RRKMQKeVVNIHKNTK-KGV--VFVTHNIEEAMEIAKKIIVFSKNKRI 211
Cdd:TIGR02633 174 EKETEI-LLDIIRDLKaHGVacVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-224 |
5.50e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 79.36 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTT----LLRILAglenaTSGNIYFFN------NDKKCTP---KVGMVFQE-- 85
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGqplhnlNRRQLLPvrhRIQVVFQDpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 86 SRLMPWLNV----SENILLH------TEKDNR-----NKVDLDKylkmmkleKFKNSYPNELSGGMAHRVSIARALSFNP 150
Cdd:PRK15134 373 SSLNPRLNVlqiiEEGLRVHqptlsaAQREQQviavmEEVGLDP--------ETRHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 151 DILLMDEPFAALDyftrRKMQKEVVNIHKNTKK----GVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVE-------DE 219
Cdd:PRK15134 445 SLIILDEPTSSLD----KTVQAQILALLKSLQQkhqlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCErvfaapqQE 520
|
....*
gi 497578899 220 YNRDL 224
Cdd:PRK15134 521 YTRQL 525
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-163 |
5.74e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 77.50 E-value: 5.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGMVFQESRL-MPWLnVSE 96
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaelarRRAVLPQHSSLsFPFT-VEE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 97 NILL----HTEKDNRNKVDLDKYLKMMKLEKFKN-SYPnELSGGMAHRVSIARAL------SFNPDILLMDEPFAALD 163
Cdd:PRK13548 96 VVAMgrapHGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALD 172
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-190 |
7.84e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.14 E-value: 7.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 18 DNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFF--NNDK-KCTPKVGMVF--QESRLMPWL 92
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFErqSIKKdLCTYQKQLCFvgHRSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENIL--LHTEKDNrnkVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDyftRRKM 170
Cdd:PRK13540 90 TLRENCLydIHFSPGA---VGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSL 163
|
170 180
....*....|....*....|..
gi 497578899 171 QKEVVNIHKNTKKG--VVFVTH 190
Cdd:PRK13540 164 LTIITKIQEHRAKGgaVLLTSH 185
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
25-211 |
1.53e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGL--ENATSGNIYFFNNDKKC-----TPKVGMV--FQESRLMPWLNVS 95
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQAsnirdTERAGIAiiHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENILLHTE-------KDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALdyfTRR 168
Cdd:PRK13549 101 ENIFLGNEitpggimDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL---TES 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497578899 169 KMQKeVVNIHKNTK-KGV--VFVTHNIEEAMEIAKKIIVFSKNKRI 211
Cdd:PRK13549 178 ETAV-LLDIIRDLKaHGIacIYISHKLNEVKAISDTICVIRDGRHI 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
25-213 |
3.41e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 75.65 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPK--------VGMVFQ--ESRLMPwLNV 94
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKglmklresVGMVFQdpDNQLFS-ASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENI------LLHTEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRR 168
Cdd:PRK13636 101 YQDVsfgavnLKLPEDEVRKRVD--NALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 497578899 169 KMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:PRK13636 179 EIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-209 |
3.97e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 74.81 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnnDKKCTP---------KVGMVFQESRLMPw 91
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL---DGKPISqyehkylhsKVSLVGQEPVLFA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 LNVSENIL--LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNE-------LSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:cd03248 102 RSLQDNIAygLQSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497578899 163 DYFTRRKMQKEVVNIHKNTKkgVVFVTHNIeEAMEIAKKIIVFSKNK 209
Cdd:cd03248 182 DAESEQQVQQALYDWPERRT--VLVIAHRL-STVERADQILVLDGGR 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
8-213 |
4.19e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.79 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTpkvgmVFQESR 87
Cdd:PRK11160 341 LNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILL--NGQPIA-----DYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 LMPWLNV------------SENILL--HTEKDNR-----NKVDLDKYLKMmklEKFKNSYPNE----LSGGMAHRVSIAR 144
Cdd:PRK11160 412 LRQAISVvsqrvhlfsatlRDNLLLaaPNASDEAlievlQQVGLEKLLED---DKGLNAWLGEggrqLSGGEQRRLGIAR 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 145 ALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNtkKGVVFVTHNIeEAMEIAKKIIVFSKNKRIKQ 213
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRL-TGLEQFDRICVMDNGQIIEQ 554
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-204 |
4.84e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 4.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP-------KVG--MVFQESRLMPWLNV 94
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEI--GGNPCARltpakahQLGiyLVPQEPLLFPNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLHTEKDNRNKVDLDKYLKMMklekfkNSYPN-ELSGG---MAHR--VSIARALSFNPDILLMDEPFAAL------ 162
Cdd:PRK15439 104 KENILFGLPKRQASMQKMKQLLAAL------GCQLDlDSSAGsleVADRqiVEILRGLMRDSRILILDEPTASLtpaete 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497578899 163 DYFTR-RKMQKEVVnihkntkkGVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK15439 178 RLFSRiRELLAQGV--------GIVFISHKLPEIRQLADRISV 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
10-213 |
5.99e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.11 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 10 NIYKKYlvdNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNN----DKK----CTPKVGM 81
Cdd:PRK13639 6 DLKYSY---PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikyDKKslleVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESR---LMPwlNVSENI--------LLHTEKDNRNKvdldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNP 150
Cdd:PRK13639 83 VFQNPDdqlFAP--TVEEDVafgplnlgLSKEEVEKRVK----EALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 151 DILLMDEPFAALDYFTRRKMQKEvvnIHKNTKKGVVFV--THNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKL---LYDLNKEGITIIisTHDVDLVPVYADKVYVMSDGKIIKE 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-228 |
6.99e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 74.64 E-value: 6.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 23 LVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP-----KVGMV--FQESRLMPWLNVS 95
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPghqiaRMGVVrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENILL--HTE----------------KDNRNKVDLDKY-LKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMD 156
Cdd:PRK11300 99 ENLLVaqHQQlktglfsgllktpafrRAESEALDRAATwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 157 EPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED-EYNRDLTKNY 228
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEiRNNPDVIKAY 251
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-212 |
8.30e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 8.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 2 VRSGFLLENIYKKYlvDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLEnatsgniyffnndkKCTPKVGM 81
Cdd:COG2401 25 ERVAIVLEAFGVEL--RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL--------------KGTPVAGC 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VfqesrLMPWLNVSEN-ILLHTEKDNRNKVDLDKYLKMMKLEK---FKNSYPnELSGGMAHRVSIARALSFNPDILLMDE 157
Cdd:COG2401 89 V-----DVPDNQFGREaSLIDAIGRKGDFKDAVELLNAVGLSDavlWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 158 PFAALD----YFTRRKMQKEVvnihKNTKKGVVFVTH--NIEEAMeIAKKIIVFSKNKRIK 212
Cdd:COG2401 163 FCSHLDrqtaKRVARNLQKLA----RRAGITLVVATHhyDVIDDL-QPDLLIFVGYGGVPE 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-204 |
8.51e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 75.33 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGlenATSGNIY-----FFNNDK---KCTPK---------VGMVFQE- 85
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG---ITKDNWHvtadrFRWNGIdllKLSPRerrkiigreIAMIFQEp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 86 -SRLMPWLNV----SENI----------------------LLHtekdnrnKVDLDKYLKMMklekfkNSYPNELSGGMAH 138
Cdd:COG4170 99 sSCLDPSAKIgdqlIEAIpswtfkgkwwqrfkwrkkraieLLH-------RVGIKDHKDIM------NSYPHELTEGECQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 139 RVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITV 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-204 |
1.21e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLEN----ATSGNIYFFNND-KKCTPK---------VGMVFQESrlMP 90
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDlQRISEKerrnlvgaeVAMIFQDP--MT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 91 WLN--------VSENILLH---TEKDNRNK-VDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:PRK11022 101 SLNpcytvgfqIMEAIKVHqggNKKTRRQRaIDLLNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIV 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-163 |
2.93e-15 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 71.62 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnnDKKCTPKVGMVFQE--------SRLMPWL 92
Cdd:TIGR01189 12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW---NGTPLAEQRDEPHEnilylghlPGLKPEL 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 93 NVSENILLHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
24-191 |
5.22e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 73.55 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNiYFFNNDKKCTPKVGMVfqeSRLMPWLN---------V 94
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGE-VTLDGVPVSSLDQDEV---RRRVSVCAqdahlfdttV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLhtEKDNRNKVDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:TIGR02868 426 RENLRL--ARPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 497578899 164 YFTRRKMQKEVVNIhkNTKKGVVFVTHN 191
Cdd:TIGR02868 504 AETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-223 |
5.24e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIY-------FFNNDKKCTPKVGMVFQESRLMPWLNVSEN 97
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILidgqemrFASTTAALAAGVAIIYQELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 ILLHTEKDNRNKVD--LDKYLKMMKLEKFKNSY-PN----ELSGGMAHRVSIARALSFNPDILLMDEPFAALdyfTRRKM 170
Cdd:PRK11288 100 LYLGQLPHKGGIVNrrLLNYEAREQLEHLGVDIdPDtplkYLSIGQRQMVEIAKALARNARVIAFDEPTSSL---SAREI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 171 QK--EVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRD 223
Cdd:PRK11288 177 EQlfRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRD 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
25-218 |
6.75e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.23 E-value: 6.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF------FNNDKKCTPK-VGMVFQESRLMPWLNVSEN 97
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFqgkeidFKSSKEALENgISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 ILLHTEKDNRNKVDLDKYLKMMKL---EKFKNSYPNE----LSGGMAHRVSIARALSFNPDILLMDEPFAALDyftrrkm 170
Cdd:PRK10982 94 MWLGRYPTKGMFVDQDKMYRDTKAifdELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT------- 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 171 QKEVVNIHKNTKK------GVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:PRK10982 167 EKEVNHLFTIIRKlkergcGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAG 220
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
24-241 |
8.47e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 71.75 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGL-----ENATSGNIYFFNNDKKCT----PKVGMVFQE-SRLMPWLN 93
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddNPNSKITVDGITLTAKTVwdirEKVGIVFQNpDNQFVGAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSENILLHTEkdNRnKVDLDKYLKMMK-------LEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFT 166
Cdd:PRK13640 102 VGDDVAFGLE--NR-AVPRPEMIKIVRdvladvgMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 167 RRKMQKEVVNIHKNTKKGVVFVTHNIEEAmEIAKKIIVFSKNKRIKQFSVEDEYNrdltknyyinlKKEILRELG 241
Cdd:PRK13640 179 KEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFS-----------KVEMLKEIG 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-206 |
1.14e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISS-----EEITVILGESGCGKTTLLRILAGLENATSGNIYFfnndkkcTPKVGMVFQESRLMPWLNVSENIL 99
Cdd:PRK13409 350 LGDFSLEVEGgeiyeGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-------ELKISYKPQYIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 100 LHTEKDNRN--KVDLdkyLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNI 177
Cdd:PRK13409 423 SITDDLGSSyyKSEI---IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499
|
170 180 190
....*....|....*....|....*....|.
gi 497578899 178 HKNTKKGVVFVTHNIeeAME--IAKKIIVFS 206
Cdd:PRK13409 500 AEEREATALVVDHDI--YMIdyISDRLMVFE 528
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-218 |
1.18e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 71.27 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdNK----EHLVLDNISLNISSEE-ITVIlGESGCGKTTLLRILAGLENATSGNIYFFNND------KKCT 76
Cdd:COG1101 4 LKNLSKTF---NPgtvnEKRALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtklpeYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 77 PKVGMVFQESrLM---PWLNVSENILLHTEKDNR-------NKVDLDKYLKmmKLEKFKNSYPNE-------LSGGMAHR 139
Cdd:COG1101 80 KYIGRVFQDP-MMgtaPSMTIEENLALAYRRGKRrglrrglTKKRRELFRE--LLATLGLGLENRldtkvglLSGGQRQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 140 VSIARALSFNPDILLMDEPFAALDYFTRRK-MQ--KEVVNIHKNTkkgVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSV 216
Cdd:COG1101 157 LSLLMATLTKPKLLLLDEHTAALDPKTAALvLEltEKIVEENNLT---TLMVTHNMEQALDYGNRLIMMHEGRIILDVSG 233
|
..
gi 497578899 217 ED 218
Cdd:COG1101 234 EE 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-163 |
1.67e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.72 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYffnndkkCTPKVGMVF--QESrLMPWLNVSENIL 99
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-------MPEGEDLLFlpQRP-YLPLGTLREQLI 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 100 lhtekdnrnkvdldkylkmmklekfknsYP--NELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:cd03223 86 ----------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
8-214 |
1.84e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.02 E-value: 1.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyffnndkKCTPKVGMVF--QE 85
Cdd:COG0488 318 LEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------KLGETVKIGYfdQH 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 86 SRLmpwLNVSENIL--LHTEKDNRNKVDLDKYLKMM-----KLEKfknsYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:COG0488 387 QEE---LDPDKTVLdeLRDGAPGGTEQEVRGYLGRFlfsgdDAFK----PVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 159 FAALDYFTRrkmqkEVVNIHKNTKKG-VVFVTHNiEEAME-IAKKIIVFsKNKRIKQF 214
Cdd:COG0488 460 TNHLDIETL-----EALEEALDDFPGtVLLVSHD-RYFLDrVATRILEF-EDGGVREY 510
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
21-163 |
2.05e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 69.45 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNndkKCTPKVGMVFQE------------SRL 88
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG---EPIRRQRDEYHQdllylghqpgikTEL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 89 MPWLNVSENILLHTEKDNRnkvDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PRK13538 90 TALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2-204 |
2.93e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 2 VRSGFLLEniykkylVDNKEHLVlDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN------NDKKC 75
Cdd:PRK10261 325 LRSGLLNR-------VTREVHAV-EKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlSPGKL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 76 TP---KVGMVFQE--SRLMPWLNVSENI--------LLHTEKDNRNKVDLDKYLKMMKLEKFKnsYPNELSGGMAHRVSI 142
Cdd:PRK10261 397 QAlrrDIQFIFQDpyASLDPRQTVGDSImeplrvhgLLPGKAAAARVAWLLERVGLLPEHAWR--YPHEFSGGQRQRICI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497578899 143 ARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK10261 475 ARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAV 536
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
8-213 |
4.04e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.12 E-value: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvdNKEHLV--LDNISLNISSEEITVILGESGCGKTTLLRILAGL------------ENATSGNIYFFNNdk 73
Cdd:PRK13642 7 VENLVFKY---EKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLfeefegkvkidgELLTAENVWNLRR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 74 kctpKVGMVFQE-SRLMPWLNVSENILLHTEKDNRNKVDL----DKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSF 148
Cdd:PRK13642 82 ----KIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMikrvDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 149 NPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEiAKKIIVFSKNKRIKQ 213
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKE 221
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-163 |
4.12e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 20 KEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPKV----GMVFQESRLMPWLNVS 95
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQIlkrtGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENI----LLHTEKDNRNKVDL---DKYLKMMKLEK-----FKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PLN03211 159 ETLvfcsLLRLPKSLTKQEKIlvaESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-239 |
5.07e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 69.27 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPKV----------------GMVFQEs 86
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPiSMLSSRQlarrlallpqhhltpeGITVRE- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 87 rLM-----PWLNVSENIllhTEKDNRNkvdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:PRK11231 96 -LVaygrsPWLSLWGRL---SAEDNAR---VNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 162 LDYftrrKMQKEVVNIH---KNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDLTKNYYiNLKKEILR 238
Cdd:PRK11231 169 LDI----NHQVELMRLMrelNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF-DVEAEIHP 243
|
.
gi 497578899 239 E 239
Cdd:PRK11231 244 E 244
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-190 |
5.63e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 70.61 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnndkkcTPKVGMVF--QESRlMPWLNVSENIL 99
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-------PAGARVLFlpQRPY-LPLGTLREALL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 100 LHTEKDNRNKVDLDKYLKMMKLEKFKNSY------PNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKE 173
Cdd:COG4178 448 YPATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
|
170
....*....|....*..
gi 497578899 174 VVNIHKNTkkGVVFVTH 190
Cdd:COG4178 528 LREELPGT--TVISVGH 542
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
9-163 |
6.82e-14 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 67.65 E-value: 6.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENA--TSGNIYF--FNNDKKCTPKVGMVFQ 84
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILIngRPLDKNFQRSTGYVEQ 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 85 ESRLMPWLNVSENILLHTekdnrnkvdldkYLKMMKLEKFKnsypnelsggmahRVSIARALSFNPDILLMDEPFAALD 163
Cdd:cd03232 87 QDVHSPNLTVREALRFSA------------LLRGLSVEQRK-------------RLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-204 |
6.93e-14 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 69.50 E-value: 6.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyffnndkKCTPKVGMVFQESRLMPWlNVSENILLhte 103
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-------KHSGRISFSSQFSWIMPG-TIKENIIF--- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 104 kdnrnKVDLDKY-----LKMMKLEKFKNSYPNE-----------LSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:cd03291 121 -----GVSYDEYryksvVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190
....*....|....*....|....*....|....*...
gi 497578899 168 RKM-QKEVVNIHKNtkKGVVFVTHNIEEaMEIAKKIIV 204
Cdd:cd03291 196 KEIfESCVCKLMAN--KTRILVTSKMEH-LKKADKILI 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
16-207 |
8.07e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.06 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 16 LVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTP----KVGMVF-QESR-- 87
Cdd:COG3845 265 VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDiTGLSPrerrRLGVAYiPEDRlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 --LMPWLNVSENILL--HTEKDNRNK--VDLDKYLKMMK--LEKFKNSYPNE------LSGGMAHRVSIARALSFNPDIL 153
Cdd:COG3845 345 rgLVPDMSVAENLILgrYRRPPFSRGgfLDRKAIRAFAEelIEEFDVRTPGPdtparsLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 154 LMDEPFAALD----YFTRRKMQKEvvnihKNTKKGVVFVTHNIEEAMEIAKKIIVFSK 207
Cdd:COG3845 425 IAAQPTRGLDvgaiEFIHQRLLEL-----RDAGAAVLLISEDLDEILALSDRIAVMYE 477
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-191 |
9.01e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.56 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 17 VDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLEN--ATSGNIYFFNND----------KKctpKVGMVFQ 84
Cdd:COG0396 10 VEGKE--ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDilelspderaRA---GIFLAFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 85 ESRLMPWLNVSEniLLHTEKDNRNKVDLD---------KYLKMMKL-EKFKNSYPNE-LSGGMAHRVSIARALSFNPDIL 153
Cdd:COG0396 85 YPVEIPGVSVSN--FLRTALNARRGEELSareflkllkEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 497578899 154 LMDEPFAALDYFTRRKMqKEVVNIHKNTKKGVVFVTHN 191
Cdd:COG0396 163 ILDETDSGLDIDALRIV-AEGVNKLRSPDRGILIITHY 199
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
24-211 |
1.02e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.60 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyffnnDKKCTPKVGMVFQESRLMPW--LNVSENILLh 101
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----KRNGKLRIGYVPQKLYLDTTlpLTVNRFLRL- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 102 teKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNT 181
Cdd:PRK09544 93 --RPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRREL 170
|
170 180 190
....*....|....*....|....*....|
gi 497578899 182 KKGVVFVTHNIEEAMeiAKKIIVFSKNKRI 211
Cdd:PRK09544 171 DCAVLMVSHDLHLVM--AKTDEVLCLNHHI 198
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-213 |
1.37e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.35 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKT-TLLRILAGLENA----TSGNIYFFNNDKKCTP----------KVGMVFQE 85
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASeqtlrgvrgnKIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 86 SrlMPWLN--------VSENILLH----TEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDIL 153
Cdd:PRK15134 101 P--MVSLNplhtlekqLYEVLSLHrgmrREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 154 LMDEPFAALDYftrrKMQKEVVNIHKNTKK----GVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:PRK15134 179 IADEPTTALDV----SVQAQILQLLRELQQelnmGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
27-213 |
1.38e-13 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 67.93 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 27 NISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPKVGMVFQESRLM---PW------------ 91
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEAERRRLmrtEWgfvhqnprdglr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 ------LNVSENIL-LHTEKDNRNKVDLDKYLKMMKLEKFK-NSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:TIGR02323 101 mrvsagANIGERLMaIGARHYGNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 164 YFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:TIGR02323 181 VSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVES 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-206 |
2.73e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 68.66 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISS-----EEITVILGESGCGKTTLLRILAGLENATSGNIyffNNDKKCTPKVGMVFQESRLmpwlNVSENIl 99
Cdd:COG1245 351 YGGFSLEVEGgeireGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLKISYKPQYISPDYDG----TVEEFL- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 100 lhtEKDNRNKVDLDKY----LKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVV 175
Cdd:COG1245 423 ---RSANTDDFGSSYYkteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170 180 190
....*....|....*....|....*....|.
gi 497578899 176 NIHKNTKKGVVFVTHNIEEAMEIAKKIIVFS 206
Cdd:COG1245 500 RFAENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
8-169 |
2.94e-13 |
|
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: 66.69 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKK---YLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDK-----KCTPK- 78
Cdd:COG4778 7 VENLSKTftlHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdlaQASPRe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 79 --------VGMVFQESRLMP---WLNVSENILLH---TEKDNRNKV-DLdkyLKMMKL-EKFKNSYPNELSGGMAHRVSI 142
Cdd:COG4778 87 ilalrrrtIGYVSQFLRVIPrvsALDVVAEPLLErgvDREEARARArEL---LARLNLpERLWDLPPATFSGGEQQRVNI 163
|
170 180
....*....|....*....|....*..
gi 497578899 143 ARALSFNPDILLMDEPFAALDYFTRRK 169
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAV 190
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-238 |
3.22e-13 |
|
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: 68.29 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLEN--ATSGNIY------------------ 67
Cdd:TIGR03269 3 VKNLTKKF--DGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskv 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 68 -----------------FFNNDKK----CTPKVGMVFQES-RLMPWLNVSENIL--LHT-----EKDNRNKVDLdkyLKM 118
Cdd:TIGR03269 79 gepcpvcggtlepeevdFWNLSDKlrrrIRKRIAIMLQRTfALYGDDTVLDNVLeaLEEigyegKEAVGRAVDL---IEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 119 MKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEI 198
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 497578899 199 AKKIIVFSKNKRIKQFSVEDEYNR------DLTKNYYINLKKEILR 238
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAVfmegvsEVEKECEVEVGEPIIK 281
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
24-207 |
4.94e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTPK---------VGMVfQESR----LMP 90
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRL--DGKPVRIRsprdairagIAYV-PEDRkgegLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 91 WLNVSENI-LLHTEKDNRNKV--------DLDKYLKMMKLekfKNSYPN----ELSGGMAHRVSIARALSFNPDILLMDE 157
Cdd:COG1129 344 DLSIRENItLASLDRLSRGGLldrrreraLAEEYIKRLRI---KTPSPEqpvgNLSGGNQQKVVLAKWLATDPKVLILDE 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 497578899 158 PFAALDYFTRRkmqkEVVN-IHKNTKKG--VVFVTHNIEEAMEIAKKIIVFSK 207
Cdd:COG1129 421 PTRGIDVGAKA----EIYRlIRELAAEGkaVIVISSELPELLGLSDRILVMRE 469
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
27-204 |
5.39e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 27 NISLNisSEEITVILGESGCGKTTLLRILAGL--ENATSGNIYFFNN-----------DKKCTPKVGMVFQE--SRLMPW 91
Cdd:PRK09473 36 NFSLR--AGETLGIVGESGSGKSQTAFALMGLlaANGRIGGSATFNGreilnlpekelNKLRAEQISMIFQDpmTSLNPY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 LNVSENIL----LHTEKDNRNKVD-----LDKyLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:PRK09473 114 MRVGEQLMevlmLHKGMSKAEAFEesvrmLDA-VKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 497578899 163 DYftrrKMQKEVVNIHKNTKK----GVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK09473 193 DV----TVQAQIMTLLNELKRefntAIIMITHDLGVVAGICDKVLV 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-204 |
6.42e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.03 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 20 KEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF-----FNNDKKCTPKVGMVF-QESRLMPWLN 93
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyvpFKRRKEFARRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSENILLHTE----KDNRNKVDLDKYLKMMKLEKFKNSYPNELSGG--MahRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:COG4586 113 AIDSFRLLKAiyriPDAEYKKRLDELVELLDLGELLDTPVRQLSLGqrM--RCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 497578899 168 RKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:COG4586 191 EAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIV 227
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
27-204 |
7.23e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.35 E-value: 7.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 27 NISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCT--------PKVGMVFQE--SRLMPWLNVSE 96
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI--DDHPLHfgdysyrsQRIRMIFQDpsTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 ----NILLHTEKD--NRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYftrrKM 170
Cdd:PRK15112 109 ildfPLRLNTDLEpeQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM----SM 184
|
170 180 190
....*....|....*....|....*....|....*...
gi 497578899 171 QKEVVN--IHKNTKKGV--VFVTHNIEEAMEIAKKIIV 204
Cdd:PRK15112 185 RSQLINlmLELQEKQGIsyIYVTQHLGMMKHISDQVLV 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-158 |
1.23e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-------KKCTPKVGMVFQESRLMPWLNVSE 96
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitdwqtaKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 97 NILL---HTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:PRK11614 100 NLAMggfFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEP 164
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-213 |
1.51e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.41 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF----FNNDKK----CTPKVGMVFQE-SRLMPWLNV 94
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqgkpLDYSKRgllaLRQQVATVFQDpEQQIFYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENILLH------TEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRR 168
Cdd:PRK13638 96 DSDIAFSlrnlgvPEAEITRRVD--EALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497578899 169 KMqkeVVNIHKNTKKG--VVFVTHNIEEAMEIAKKIIVFSKNKRIKQ 213
Cdd:PRK13638 174 QM---IAIIRRIVAQGnhVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-191 |
1.82e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.09 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 17 VDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLEN--ATSGNIYFFNND-KKCTPK------VGMVFQESR 87
Cdd:cd03217 10 VGGKE--ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDiTDLPPEerarlgIFLAFQYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 LMPWLNVSEnillhtekdnrnkvdldkYLKmmklekfknsYPNE-LSGGMAHRVSIARALSFNPDILLMDEPFAALDyFT 166
Cdd:cd03217 88 EIPGVKNAD------------------FLR----------YVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD-ID 138
|
170 180
....*....|....*....|....*
gi 497578899 167 RRKMQKEVVNIHKNTKKGVVFVTHN 191
Cdd:cd03217 139 ALRLVAEVINKLREEGKSVLIITHY 163
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
21-163 |
2.20e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 64.05 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNndkkcTPKVGMVFQESRLMPW--------- 91
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG-----GPLDFQRDSIARGLLYlghapgikt 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 92 -LNVSENilLHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:cd03231 87 tLSVLEN--LRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-198 |
2.29e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.81 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 20 KEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDkkctpkvgmvFQESRLMPWLN----VS 95
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD----------LRDYTLASLRNqvalVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENILL----------HTEKDNRNKVDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILL 154
Cdd:PRK11176 424 QNVHLfndtianniaYARTEQYSREQIEEAARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPILI 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNtkKGVVFVTH---NIEEAMEI 198
Cdd:PRK11176 504 LDEATSALDTESERAIQAALDELQKN--RTSLVIAHrlsTIEKADEI 548
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
24-239 |
2.32e-12 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 65.89 E-value: 2.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnnDkkctpkvGMVFQESRLMPWLN----VSENIL 99
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL---D-------GHDLADYTLASLRRqvalVSQDVV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 100 L----------HTEKDNRNKVDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:TIGR02203 417 LfndtianniaYGRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEA 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKNtKKGVVfVTHNIeEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDltkNYYINLKKEILR 238
Cdd:TIGR02203 497 TSALDNESERLVQAALERLMQG-RTTLV-IAHRL-STIEKADRIVVMDDGRIVERGTHNELLARN---GLYAQLHNMQFR 570
|
.
gi 497578899 239 E 239
Cdd:TIGR02203 571 E 571
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
19-190 |
2.58e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.74 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 19 NKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNN--DKKCTPKVGMVFQESRLMPWLNVSE 96
Cdd:PRK13541 10 NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCniNNIAKPYCTYIGHNLGLKLEMTVFE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILLHTEKDNRNKVdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYfTRRKMQKEVVN 176
Cdd:PRK13541 90 NLKFWSEIYNSAET-LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK-ENRDLLNNLIV 167
|
170
....*....|....
gi 497578899 177 IHKNTKKGVVFVTH 190
Cdd:PRK13541 168 MKANSGGIVLLSSH 181
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-199 |
6.81e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.62 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 36 EITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDkkctpkvgmvfqesrlmpwlnvsenillhtekdnrnkvDLDKY 115
Cdd:smart00382 3 EVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE--------------------------------------DILEE 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 116 LKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVV-----NIHKNTKKGVVFVTH 190
Cdd:smart00382 45 VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTN 124
|
....*....
gi 497578899 191 NIEEAMEIA 199
Cdd:smart00382 125 DEKDLGPAL 133
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
81-214 |
1.03e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.28 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 81 MVFQESRLMPwLNVSENILLHteKDNRNKVDLDKYLKMMKLEKFKNSYPNE-----------LSGGMAHRVSIARALSFN 149
Cdd:PTZ00265 1300 IVSQEPMLFN-MSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALLRE 1376
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 150 PDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIeEAMEIAKKIIVFSKNKRIKQF 214
Cdd:PTZ00265 1377 PKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNNPDRTGSF 1440
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-229 |
1.21e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNN------DKKCTPKVGMVFQESRLMPWLNV 94
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEhiqhyaSKEVARRIGLLAQNATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENIL--------LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFT 166
Cdd:PRK10253 99 QELVArgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 167 RRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNRDLTKNYY 229
Cdd:PRK10253 179 QIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
24-206 |
1.21e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.71 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND------KKCTPKVGMVFQESRLMPWLNVSEN 97
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaRAASRRVASVPQDTSLSFEFDVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 ILL-----------HTEKDNRNkvdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDyfT 166
Cdd:PRK09536 98 VEMgrtphrsrfdtWTETDRAA---VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--I 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 497578899 167 RRKMQK-EVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFS 206
Cdd:PRK09536 173 NHQVRTlELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLA 213
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
24-163 |
1.61e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYffnndkkCTPKVGMVFQESRLMPwLNVSENILLHTE 103
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AERSIAYVPQQAWIMN-ATVRGNILFFDE 746
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497578899 104 KDnrnKVDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PTZ00243 747 ED---AARLADAVRVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
25-162 |
3.06e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 3.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATS--GNIYF------FnNDKKCTPKVGMVF--QESRLMPWLNV 94
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFdgevcrF-KDIRDSEALGIVIihQELALIPYLSI 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 95 SENILLHTEKDNRNKVDLD-------KYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:NF040905 96 AENIFLGNERAKRGVIDWNetnrrarELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
24-163 |
4.60e-11 |
|
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: 61.87 E-value: 4.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLN-ISSEEITViLGESGCGKTTLLRILAGLENAtsgniyfFNNDKKCTP--KVGMVFQESRLMPWLNVSENILL 100
Cdd:TIGR03719 20 ILKDISLSfFPGAKIGV-LGLNGAGKSTLLRIMAGVDKD-------FNGEARPQPgiKVGYLPQEPQLDPTKTVRENVEE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 101 HTEK-----DNRNKV---------DLDKYLKMM-----------------KLEKFKNSY--P------NELSGGMAHRVS 141
Cdd:TIGR03719 92 GVAEikdalDRFNEIsakyaepdaDFDKLAAEQaelqeiidaadawdldsQLEIAMDALrcPpwdadvTKLSGGERRRVA 171
|
170 180
....*....|....*....|..
gi 497578899 142 IARALSFNPDILLMDEPFAALD 163
Cdd:TIGR03719 172 LCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
23-214 |
5.61e-11 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 60.20 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 23 LVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGMVFQEsrlmPWL---N 93
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGlhdlrsRISIIPQD----PVLfsgT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSENI---LLHTEKDnrnkvdLDKYLKMMKLEKFKNSYPNEL-----SGG----MAHR--VSIARALSFNPDILLMDEPF 159
Cdd:cd03244 94 IRSNLdpfGEYSDEE------LWQALERVGLKEFVESLPGGLdtvveEGGenlsVGQRqlLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 160 AALDYFTRRKMQKEVVNIHKNTKkgVVFVTHNIEEAMEiAKKIIVFSKNkRIKQF 214
Cdd:cd03244 168 ASVDPETDALIQKTIREAFKDCT--VLTIAHRLDTIID-SDRILVLDKG-RVVEF 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-170 |
7.10e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.85 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyffnndkKCTPKVGMVFQESRLMPWlNVSENILLHTE 103
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------KHSGRISFSPQTSWIMPG-TIKDNIIFGLS 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 104 KDNRNKVDLdkyLKMMKLEKFKNSYPNE-----------LSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKM 170
Cdd:TIGR01271 513 YDEYRYTSV---IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEI 587
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
24-227 |
7.95e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 61.30 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF-----FNNDK-KCTPKVGMVFQESRLMPWlNVSEN 97
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlSQWDReELGRHIGYLPQDVELFDG-TIAEN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 ILLHTEkdnrnkVDLDKYLKMMKL-------EKFKNSY-------PNELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:COG4618 426 IARFGD------ADPEKVVAAAKLagvhemiLRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 164 YFTRRKMQKEVVNIhKNTKKGVVFVTHNIeEAMEIAKKIIVFsKNKRIKQFSVEDEYNRDLTKN 227
Cdd:COG4618 500 DEGEAALAAAIRAL-KARGATVVVITHRP-SLLAAVDKLLVL-RDGRVQAFGPRDEVLARLARP 560
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-209 |
1.07e-10 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 60.83 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILA-----GLENATSGNIYFFNNDKKCTPKV-GMVFQESRLMPWLNVSENI 98
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAfrspkGVKGSGSVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 LLH---------TEKDNRNKVDldKYLKMMKLEKFKNS---YPNE---LSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:TIGR00955 121 MFQahlrmprrvTKKEKRERVD--EVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 164 YFtrrkMQKEVVNIHK---NTKKGVVFVTHN-IEEAMEIAKKIIVFSKNK 209
Cdd:TIGR00955 199 SF----MAYSVVQVLKglaQKGKTIICTIHQpSSELFELFDKIILMAEGR 244
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-214 |
1.20e-10 |
|
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: 58.96 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYLVDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTP------KVGM 81
Cdd:cd03369 9 VENLSVRYAPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPledlrsSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 82 VFQESRLMpwlnvSENIllhtekdnRNKVD-LDKY--LKMMKLEKFKNSYPNeLSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:cd03369 87 IPQDPTLF-----SGTI--------RSNLDpFDEYsdEEIYGALRVSEGGLN-LSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 159 FAALDYFTRRKMQKevvNIHKNTKKG-VVFVTHNIEEAMEIAkKIIVFSKNKrIKQF 214
Cdd:cd03369 153 TASIDYATDALIQK---TIREEFTNStILTIAHRLRTIIDYD-KILVMDAGE-VKEY 204
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
32-205 |
1.49e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 58.35 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 32 ISSEEITVILGESGCGKTTLLRILAGLENATSGNIyffnndkkctpkvgmvfqesrlmpwlnvsenillhtekdnrnkvD 111
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND--------------------------------------------E 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 112 LDKYLKMMKLEKFKnsypneLSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHN 191
Cdd:cd03222 58 WDGITPVYKPQYID------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHD 131
|
170
....*....|....
gi 497578899 192 IEEAMEIAKKIIVF 205
Cdd:cd03222 132 LAVLDYLSDRIHVF 145
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-209 |
1.84e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNdkkctpkVGMVFQESrlmpWL---NVSENILL- 100
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------VAYVPQQA----WIqndSLRENILFg 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 101 HTEKDNRNKVDLDKYLKMMKLEKFKNSYPNE-------LSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKE 173
Cdd:TIGR00957 723 KALNEKYYQQVLEACALLPDLEILPSGDRTEigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEH 802
|
170 180 190
....*....|....*....|....*....|....*....
gi 497578899 174 VV---NIHKNtkKGVVFVTHNIEEAMEIaKKIIVFSKNK 209
Cdd:TIGR00957 803 VIgpeGVLKN--KTRILVTHGISYLPQV-DVIIVMSGGK 838
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
25-180 |
2.17e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 59.97 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK-----VGMVFQESRLMpwlN--VSE 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDiRTVTRAslrrnIAVVFQDAGLF---NrsIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILL----HTEKDNRNKVDLDKYL-----KMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTR 167
Cdd:PRK13657 428 NIRVgrpdATDEEMRAAAERAQAHdfierKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETE 507
|
170
....*....|...
gi 497578899 168 RKMQKEVVNIHKN 180
Cdd:PRK13657 508 AKVKAALDELMKG 520
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-213 |
3.25e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 59.74 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN------NDKKCTPKVGMVFQESRLMPWlNVSEN 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqyDHHYLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 I---LLHTEKDnrnkvDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:TIGR00958 575 IaygLTDTPDE-----EIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 497578899 164 YFTRRKMQkevvNIHKNTKKGVVFVTHNIEEAmEIAKKIIVFSKNKRIKQ 213
Cdd:TIGR00958 650 AECEQLLQ----ESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEM 694
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-218 |
5.14e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 17 VDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAG------LEN--ATSGNIYFFNNDKKCTPKV------GMV 82
Cdd:PRK13547 9 VARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggAPRgaRVTGDVTLNGEPLAAIDAPrlarlrAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 83 FQESRLMPWLNVSENILL----HT----EKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALS------- 147
Cdd:PRK13547 89 PQAAQPAFAFSAREIVLLgrypHArragALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 148 --FNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:PRK13547 169 aaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-194 |
6.53e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.70 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGL----ENATSGNIYFFNNDKKCTPK-VGMVFQESRLmPWLNVSENIL 99
Cdd:PRK11174 366 AGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpyqGSLKINGIELRELDPESWRKhLSWVGQNPQL-PHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 100 LhtEKDNRNKVDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRR 168
Cdd:PRK11174 445 L--GNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180
....*....|....*....|....*..
gi 497578899 169 K-MQKEVVNIHKNTkkgVVFVTHNIEE 194
Cdd:PRK11174 523 LvMQALNAASRRQT---TLMVTHQLED 546
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
25-163 |
8.23e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.24 E-value: 8.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPKVGMVFQESRLM---PW---------- 91
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLlrtEWgfvhqhprdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 --LNVSE--NI--------------LLHTEKDNRNKVDLDkylkmmklEKFKNSYPNELSGGMAHRVSIARALSFNPDIL 153
Cdd:PRK11701 102 lrMQVSAggNIgerlmavgarhygdIRATAGDWLERVEID--------AARIDDLPTTFSGGMQQRLQIARNLVTHPRLV 173
|
170
....*....|
gi 497578899 154 LMDEPFAALD 163
Cdd:PRK11701 174 FMDEPTGGLD 183
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
36-192 |
1.28e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 36 EITVILGESGCGKTTLLRILAGLENATSGN--------------------IYF---FNNDKKCTPKVgmvfQESRLMPWL 92
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqNYFtklLEGDVKVIVKP----QYVDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENILLHTEKDNRNKvdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQK 172
Cdd:cd03236 103 VKGKVGELLKKKDERGK--LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAAR 180
|
170 180
....*....|....*....|
gi 497578899 173 EVVNIHKNTkKGVVFVTHNI 192
Cdd:cd03236 181 LIRELAEDD-NYVLVVEHDL 199
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-180 |
1.45e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 57.52 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPK-----VGMVFQESRLmpwLN- 93
Cdd:COG5265 370 ERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDiRDVTQAslraaIGIVPQDTVL---FNd 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 -VSENIL---LHTEKDnrnkvDLDKYLKMMKLEKFKNSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:COG5265 447 tIAYNIAygrPDASEE-----EVEAAARAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPPILIFDEA 521
|
170 180
....*....|....*....|..
gi 497578899 159 FAALDYFTRRKMQKEVVNIHKN 180
Cdd:COG5265 522 TSALDSRTERAIQAALREVARG 543
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-158 |
2.15e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.06 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 26 DNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN-----NDKKCTPKVGMVFQESRLMPWLNVSENILL 100
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpvdaGDIATRRRVGYMSQAFSLYGELTVRQNLEL 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497578899 101 H------TEKDNRNKVDldkylKMMK---LEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEP 158
Cdd:NF033858 363 HarlfhlPAAEIAARVA-----EMLErfdLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
3-163 |
2.30e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.35 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 3 RSGFLLENIYKKYLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGL---ENATSGNIYFFNNDKK----- 74
Cdd:cd03233 1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKefaek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 75 CTPKVGMVFQESRLMPWLNVSENillhtekdnrnkvdLDKYLKMMklekfKNSYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:cd03233 81 YPGEIIYVSEEDVHFPTLTVRET--------------LDFALRCK-----GNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 497578899 155 MDEPFAALD 163
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
24-204 |
3.04e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 56.35 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLEN----ATSGNIYFFNNDK-KCTPK---------VGMVFQESRlm 89
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDDIDLlRLSPRerrklvghnVSMIFQEPQ-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 90 PWLNVSENI------------------------------LLHtekdnrnKVDLDKYLKMMKlekfknSYPNELSGGMAHR 139
Cdd:PRK15093 100 SCLDPSERVgrqlmqnipgwtykgrwwqrfgwrkrraieLLH-------RVGIKDHKDAMR------SFPYELTEGECQK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 140 VSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINV 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-207 |
4.08e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAG-LENATSGNIyFFNNDKKCTPKVGMVFQESrlmpwlnVSENILLHTE 103
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSV-VIRGSVAYVPQVSWIFNAT-------VRENILFGSD 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 104 -KDNRNKVDLDKYLKMMKLEKFKNSYPNEL-------SGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVV 175
Cdd:PLN03232 705 fESERYWRAIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCM 784
|
170 180 190
....*....|....*....|....*....|..
gi 497578899 176 NiHKNTKKGVVFVTHNIeEAMEIAKKIIVFSK 207
Cdd:PLN03232 785 K-DELKGKTRVLVTNQL-HFLPLMDRIILVSE 814
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-209 |
4.29e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.99 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 15 YLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGL-ENATSGNIYF-------FNNDKKCTPKVGMVFQES 86
Cdd:TIGR02633 266 WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFIngkpvdiRNPAQAIRAGIAMVPEDR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 87 R---LMPWLNVSENILLHTEKD--NRNKVD----LDKYLKMMKLEKFKNSYPN----ELSGGMAHRVSIARALSFNPDIL 153
Cdd:TIGR02633 346 KrhgIVPILGVGKNITLSVLKSfcFKMRIDaaaeLQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 154 LMDEPFAALDYFTRRKMQKeVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:TIGR02633 426 ILDEPTRGVDVGAKYEIYK-LINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-163 |
5.68e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLN------ISseeitvILGESGCGKTTLLRILAGLENATSGNIYFfnndkkcTP--KVGMVFQESRLMPWLNVS 95
Cdd:PRK11819 22 ILKDISLSffpgakIG------VLGLNGAGKSTLLRIMAGVDKEFEGEARP-------APgiKVGYLPQEPQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 ENIL------------------------------------LHTEKDNRNKVDLDKYLKM-----------MKLEKfknsy 128
Cdd:PRK11819 89 ENVEegvaevkaaldrfneiyaayaepdadfdalaaeqgeLQEIIDAADAWDLDSQLEIamdalrcppwdAKVTK----- 163
|
170 180 190
....*....|....*....|....*....|....*
gi 497578899 129 pneLSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PRK11819 164 ---LSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-207 |
5.80e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.18 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIY-----FFNNDKKCTPKVGMVFQESRLMPWLNVSENIL 99
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATvagksILTNISDVHQNMGYCPQFDAIDDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 100 LHTEKDNRNKVDLDKY----LKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVV 175
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180 190
....*....|....*....|....*....|..
gi 497578899 176 NIHKNtKKGVVFVTHNIEEAMEIAKKIIVFSK 207
Cdd:TIGR01257 2115 SIIRE-GRAVVLTSHSMEECEALCTRLAIMVK 2145
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
24-234 |
9.25e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 9.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFN-------NDKKCTPKVGMVFQESRLMPwLNVSE 96
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdiNLKWWRSKIGVVSQDPLLFS-NSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NI-----------------------------------------------------LLHTEK-----DNRNKVDLDKYLKM 118
Cdd:PTZ00265 479 NIkyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneLIEMRKnyqtiKDSEVVDVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 119 M--------KLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTH 190
Cdd:PTZ00265 559 HdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 497578899 191 NIeEAMEIAKKIIVFSKNKRIKQFSVeDEYNRDLTKNYYINLKK 234
Cdd:PTZ00265 639 RL-STIRYANTIFVLSNRERGSTVDV-DIIGEDPTKDNKENNNK 680
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-204 |
1.44e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 27 NISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNND-KKCTPKV----GMVF-----QESRL-----MPW 91
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEiNALSTAQrlarGLVYlpedrQSSGLyldapLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 lNVSEniLLHTE-----KDNRNKVDLDKYLKMMKLekfKNSYPNE----LSGGMAHRVSIARALSFNPDILLMDEPFAAL 162
Cdd:PRK15439 361 -NVCA--LTHNRrgfwiKPARENAVLERYRRALNI---KFNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 497578899 163 DYFTRRKMQKEVVNIHK-NTkkGVVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK15439 435 DVSARNDIYQLIRSIAAqNV--AVLFISSDLEEIEQMADRVLV 475
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
9-203 |
1.47e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYLVDNKE----------------HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyffnnD 72
Cdd:PRK13545 8 EHVTKKYKMYNKPfdklkdlffrskdgeyHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 73 KKCTpkVGMVFQESRLMPWLNVSENI----LLHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSF 148
Cdd:PRK13545 83 IKGS--AALIAISSGLNGQLTGIENIelkgLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 149 NPDILLMDEPFAALDY-FTRRKMQKevVNIHKNTKKGVVFVTHNIEEAMEIAKKII 203
Cdd:PRK13545 161 NPDILVIDEALSVGDQtFTKKCLDK--MNEFKEQGKTIFFISHSLSQVKSFCTKAL 214
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-219 |
1.56e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 53.67 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 19 NKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPKVGMvfqESRLMPWLNVSENI 98
Cdd:PRK13546 34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGL---SGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 99 LLHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDY-FTRRKMQKevVNI 177
Cdd:PRK13546 111 LCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQtFAQKCLDK--IYE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497578899 178 HKNTKKGVVFVTHNIEEAMEIAKKiIVFSKNKRIKQFSVEDE 219
Cdd:PRK13546 189 FKEQNKTIFFVSHNLGQVRQFCTK-IAWIEGGKLKDYGELDD 229
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-170 |
1.96e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 53.73 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPKVGMV--FQESRLMPW---LNVSE 96
Cdd:PRK15056 20 HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVayVPQSEEVDWsfpVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 97 NILL----HT----EKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRR 168
Cdd:PRK15056 100 VVMMgrygHMgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
|
..
gi 497578899 169 KM 170
Cdd:PRK15056 180 RI 181
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-163 |
2.58e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 24 VLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF---FNNDKKCTPKVGMVFQESRLMPWLNVSENI-L 99
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdgkTATRGDRSRFMAYLGHLPGLKADLSTLENLhF 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497578899 100 LHTEKDNRNKVDLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARA-LSFNPdILLMDEPFAALD 163
Cdd:PRK13543 106 LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAP-LWLLDEPYANLD 169
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-213 |
3.46e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 53.57 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 20 KEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPK------VGMVFQESRLMPwLN 93
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHsvlrqgVAMVQQDPVVLA-DT 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSENILLhtekdNRNkVDLDKY---LKMMKLEKFKNSYP-----------NELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:PRK10790 431 FLANVTL-----GRD-ISEEQVwqaLETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 497578899 160 AALDYFTRRKMQKEVVNIHKNTKkgVVFVTHNIEEAMEiAKKIIVFSKNKRIKQ 213
Cdd:PRK10790 505 ANIDSGTEQAIQQALAAVREHTT--LVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
27-219 |
3.46e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 27 NISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnNDKKCTP-------KVGMVF-QESR----LMPWLNV 94
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRL--NGKDISPrspldavKKGMAYiTESRrdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENIL---------------LHTEKDNRNKVDLDKYLKMMKLEKFkNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:PRK09700 359 AQNMAisrslkdggykgamgLFHEVDEQRTAENQRELLALKCHSV-NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 160 AALDYFTRRKMQKeVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDE 219
Cdd:PRK09700 438 RGIDVGAKAEIYK-VMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDD 496
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
36-190 |
4.27e-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: 53.25 E-value: 4.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 36 EITVILGESGCGKTTLLRILAGLENATSGNI--------------------YF---FNNDKKCTPKVGMVFQESRLMPwL 92
Cdd:COG1245 100 KVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdYFkklANGEIKVAHKPQYVDLIPKVFK-G 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSEniLLhtEK-DNRNKvdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQ 171
Cdd:COG1245 179 TVRE--LL--EKvDERGK--LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVA 252
|
170
....*....|....*....
gi 497578899 172 KEVVNIHKNTKKgVVFVTH 190
Cdd:COG1245 253 RLIRELAEEGKY-VLVVEH 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-163 |
5.13e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDKKCTPKVGMVFQESrlmpwlnVSENILLHTEk 104
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVVIRGTVAYVPQVSWIFNAT-------VRDNILFGSP- 704
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497578899 105 dnrnkVDLDKYLKMMKLEKFK---NSYPN-----------ELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PLN03130 705 -----FDPERYERAIDVTALQhdlDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-190 |
5.58e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 17 VDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLE--NATSGNIYFFNND-KKCTPK------VGMVFQESR 87
Cdd:CHL00131 17 VNENE--ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESiLDLEPEerahlgIFLAFQYPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 LMPWLNVSE--NILLHTEKDNRNKVDLD---------KYLKMMKL-EKFKNSYPNE-LSGGMAHRVSIARALSFNPDILL 154
Cdd:CHL00131 95 EIPGVSNADflRLAYNSKRKFQGLPELDplefleiinEKLKLVGMdPSFLSRNVNEgFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 497578899 155 MDEPFAALDyFTRRKMQKEVVNIHKNTKKGVVFVTH 190
Cdd:CHL00131 175 LDETDSGLD-IDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
37-190 |
9.27e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 37 ITVILGESGCGKTTLLRILAGL---------ENAT--------SGNI---YF---FNNDKKCTPKVGMVFQESRLMPWlN 93
Cdd:PRK13409 101 VTGILGPNGIGKTTAVKILSGElipnlgdyeEEPSwdevlkrfRGTElqnYFkklYNGEIKVVHKPQYVDLIPKVFKG-K 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSEnILLHTekDNRNKvdLDKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKE 173
Cdd:PRK13409 180 VRE-LLKKV--DERGK--LDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARL 254
|
170
....*....|....*..
gi 497578899 174 VVNIHKNtkKGVVFVTH 190
Cdd:PRK13409 255 IRELAEG--KYVLVVEH 269
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
9-168 |
1.58e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.47 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYlvDNKehLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNndkkcTPKVGMVFQeSR- 87
Cdd:TIGR03719 326 ENLTKAF--GDK--LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-----TVKLAYVDQ-SRd 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 -LMPWLNVSENIllhtekdnrnkVDLDKYLKMMKLE----------KFKNS----YPNELSGGMAHRVSIARALSFNPDI 152
Cdd:TIGR03719 396 aLDPNKTVWEEI-----------SGGLDIIKLGKREipsrayvgrfNFKGSdqqkKVGQLSGGERNRVHLAKTLKSGGNV 464
|
170
....*....|....*.
gi 497578899 153 LLMDEPFAALDYFTRR 168
Cdd:TIGR03719 465 LLLDEPTNDLDVETLR 480
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-163 |
2.45e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.87 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDkkcTPKVGMVFQESRL-----MPWL--- 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIP---LTKLQLDSWRSRLavvsqTPFLfsd 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENILLHteKDNRNKVDLDKYLKMMKLE----KFKNSYPNE-------LSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:PRK10789 404 TVANNIALG--RPDATQQEIEHVARLASVHddilRLPQGYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSA 481
|
..
gi 497578899 162 LD 163
Cdd:PRK10789 482 VD 483
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-218 |
3.46e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 102 TEKDNRNKVDldKYLKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNT 181
Cdd:NF000106 117 SRKDARARAD--ELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDG 194
|
90 100 110
....*....|....*....|....*....|....*..
gi 497578899 182 KKgVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:NF000106 195 AT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDE 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-190 |
3.60e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.33 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIyFFNNDKKCT------PK--VGMVF---------- 83
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQDLIVArlqqdpPRnvEGTVYdfvaegieeq 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 84 --------QESRLMPwLNVSENIL-----LHTEKDNRNKVDLDKYLK--MMKLEKFKNSYPNELSGGMAHRVSIARALSF 148
Cdd:PRK11147 95 aeylkryhDISHLVE-TDPSEKNLnelakLQEQLDHHNLWQLENRINevLAQLGLDPDAALSSLSGGWLRKAALGRALVS 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 497578899 149 NPDILLMDEPFAALDYFTRRKMQkevvNIHKNTKKGVVFVTH 190
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIETIEWLE----GFLKTFQGSIIFISH 211
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
17-190 |
3.63e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.79 E-value: 3.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 17 VDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLEN--ATSGNIYFFNND-------KKCTPKVGMVFQESR 87
Cdd:PRK09580 9 VSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDllelspeDRAGEGIFMAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 LMPwlNVSENILLHTE----KDNRNKVDLDKY-----------LKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDI 152
Cdd:PRK09580 89 EIP--GVSNQFFLQTAlnavRSYRGQEPLDRFdfqdlmeekiaLLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190
....*....|....*....|....*....|....*...
gi 497578899 153 LLMDEPFAALDyFTRRKMQKEVVNIHKNTKKGVVFVTH 190
Cdd:PRK09580 167 CILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
25-218 |
1.16e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.85 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNndKKCTPKV-------GMVF-QESR----LMPWL 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG--HEVVTRSpqdglanGIVYiSEDRkrdgLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 93 NVSENI-LLHTEKDNRNKVDLDKYLKMMKLEKFKNSY----PN------ELSGGMAHRVSIARALSFNPDILLMDEPFAA 161
Cdd:PRK10762 346 SVKENMsLTALRYFSRAGGSLKHADEQQAVSDFIRLFniktPSmeqaigLLSGGNQQKVAIARGLMTRPKVLILDEPTRG 425
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 162 LDYFTRrkmqKEVVN-IHKNTKKG--VVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVED 218
Cdd:PRK10762 426 VDVGAK----KEIYQlINQFKAEGlsIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
28-68 |
1.52e-06 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.64 E-value: 1.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 497578899 28 ISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYF 68
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-204 |
1.73e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 28 ISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFfnnDKK----CTPK----VGMVF-QESR----LMPWLNV 94
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYL---DGKpidiRSPRdairAGIMLcPEDRkaegIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 95 SENI-------------LLHTEKDNRNKvdlDKYLKMMKLEKfknsyPN------ELSGGMAHRVSIARALSFNPDILLM 155
Cdd:PRK11288 349 ADNInisarrhhlragcLINNRWEAENA---DRFIRSLNIKT-----PSreqlimNLSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497578899 156 DEPFAALDYFTRRkmqkEVVN-IHKNTKKG--VVFVTHNIEEAMEIAKKIIV 204
Cdd:PRK11288 421 DEPTRGIDVGAKH----EIYNvIYELAAQGvaVLFVSSDLPEVLGVADRIVV 468
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-209 |
5.88e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 8 LENIYKKYlvDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNdkkctPKVGMVFQES- 86
Cdd:PRK15064 322 VENLTKGF--DNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN-----ANIGYYAQDHa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 87 -------RLMPWLNvseniLLHTEKDNRNKV------------DLDKYLKMmklekfknsypneLSGGMAHRVSIARALS 147
Cdd:PRK15064 393 ydfendlTLFDWMS-----QWRQEGDDEQAVrgtlgrllfsqdDIKKSVKV-------------LSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497578899 148 FNPDILLMDEPFAALDyftrrkMQK-EVVNIH-KNTKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:PRK15064 455 QKPNVLVMDEPTNHMD------MESiESLNMAlEKYEGTLIFVSHDREFVSSLATRIIEITPDG 512
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-163 |
5.96e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 20 KEHLV-LDNISLNISSEEITVILGESGCGKTTLLRILAGLENA---TSGNIY--FFNNDKKCTPKVGMVFQESRLMPWLN 93
Cdd:TIGR00956 773 KEKRViLNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLvnGRPLDSSFQRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 94 VSENILLHTEKDNRNKVDL-------DKYLKMMKLEKFKNSY---PNE-LSGGMAHRVSIARALSFNPDILL-MDEPFAA 161
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSKsekmeyvEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
..
gi 497578899 162 LD 163
Cdd:TIGR00956 933 LD 934
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-222 |
8.92e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.46 E-value: 8.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 23 LVlDNISLNISSEEITVILGESGCGKT----TLLRIL-AGLeNATSGNIYFfnNDKKCTP------KVGMVFQESR--LM 89
Cdd:PRK10418 18 LV-HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGV-RQTAGRVLL--DGKPVAPcalrgrKIATIMQNPRsaFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 90 PWLNV---------------SENILLHTEKDnrnkVDLDKYLKMMKLekfknsYPNELSGGMAHRVSIARALSFNPDILL 154
Cdd:PRK10418 94 PLHTMhtharetclalgkpaDDATLTAALEA----VGLENAARVLKL------YPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 155 MDEPFAALDYFTRRKMQKEVVNIHKNTKKGVVFVTHNIEEAMEIAKKIIVFSKNKRIKQFSVEDEYNR 222
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-188 |
1.08e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 23 LVLDniSLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIY--F-------FNNDKKctpkvgMVFQEsrlmpW-- 91
Cdd:PRK10938 19 LQLP--SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQsqFshitrlsFEQLQK------LVSDE-----Wqr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 92 --------------LNVSENILLHTEKDNRNKvDLDKYLKMMKL--EKFKnsypnELSGGMAHRVSIARALSFNPDILLM 155
Cdd:PRK10938 86 nntdmlspgeddtgRTTAEIIQDEVKDPARCE-QLAQQFGITALldRRFK-----YLSTGETRKTLLCQALMSEPDLLIL 159
|
170 180 190
....*....|....*....|....*....|...
gi 497578899 156 DEPFAALDYFTRRKMQKEVVNIHkntKKGVVFV 188
Cdd:PRK10938 160 DEPFDGLDVASRQQLAELLASLH---QSGITLV 189
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
21-191 |
1.30e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 21 EHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNdkkctPKVGMVFQESrlMPWLNVSENILL 100
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKG-----IKLGYFAQHQ--LEFLRADESPLQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 101 HTEK--DNRNKVDLDKYLKMMKLEKFKNSYPNE-LSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNI 177
Cdd:PRK10636 397 HLARlaPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF 476
|
170
....*....|....
gi 497578899 178 hkntKKGVVFVTHN 191
Cdd:PRK10636 477 ----EGALVVVSHD 486
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-67 |
3.48e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 3.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 3 RSG---FLLENIykKYLVDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIY 67
Cdd:PRK11147 314 RSGkivFEMENV--NYQIDGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-214 |
4.35e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.69 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 22 HLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENaTSGNIYFfnndkkctpkVGMVFQESRLMPWLN----VSEN 97
Cdd:cd03289 17 NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI----------DGVSWNSVPLQKWRKafgvIPQK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 98 ILLHTEKDNRNkvdLDKYLKMMKLEKFK-----------NSYPNE-----------LSGGMAHRVSIARALSFNPDILLM 155
Cdd:cd03289 86 VFIFSGTFRKN---LDPYGKWSDEEIWKvaeevglksviEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 497578899 156 DEPFAALDYFTRRKMQKEVVniHKNTKKGVVFVTHNIEEAMEiAKKIIVFSKNKrIKQF 214
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENK-VRQY 217
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
25-203 |
5.84e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLR----ILAGLENATSGNIYFFNNDKKCTPKVGMVFqesrlmpwlnvseniLL 100
Cdd:cd03227 11 FVPNDVTFGEGSLTIITGPNGSGKSTILDaiglALGGAQSATRRRSGVKAGCIVAAVSAELIF---------------TR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 101 HTekdnrnkvdldkylkmmklekfknsypneLSGGMAHRVSIARAL---SFNPDIL-LMDEPFAALDYFTRRKMqKEVVN 176
Cdd:cd03227 76 LQ-----------------------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQAL-AEAIL 125
|
170 180
....*....|....*....|....*..
gi 497578899 177 IHKNTKKGVVFVTHNiEEAMEIAKKII 203
Cdd:cd03227 126 EHLVKGAQVIVITHL-PELAELADKLI 151
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-158 |
7.35e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 43.38 E-value: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 15 YLVDNKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGL-ENATSGNIYFfnNDKKCTPK---------VGMVfQ 84
Cdd:PRK13549 268 WDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFI--DGKPVKIRnpqqaiaqgIAMV-P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 85 ESR----LMPWLNVSENILLHTEKD--NRNKVD----LDKYLKMMKLEKFKNSYP----NELSGGMAHRVSIARALSFNP 150
Cdd:PRK13549 345 EDRkrdgIVPVMGVGKNITLAALDRftGGSRIDdaaeLKTILESIQRLKVKTASPelaiARLSGGNQQKAVLAKCLLLNP 424
|
....*...
gi 497578899 151 DILLMDEP 158
Cdd:PRK13549 425 KILILDEP 432
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
25-205 |
1.36e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.15 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 25 LDNISLNISSEEITVILGESGCGKTTLLriLAGLENATSGNIyffNNDKKCTPKVGMVF--QESRLmpwlnvsenillht 102
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYASGKARL---ISFLPKFSRNKLIFidQLQFL-------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 103 ekdnrnkvdLDKYLKMMKLEKFKNSypneLSGGMAHRVSIARALSFNPD--ILLMDEPFAALDYFTRRKMQkEVVNIHKN 180
Cdd:cd03238 72 ---------IDVGLGYLTLGQKLST----LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLL-EVIKGLID 137
|
170 180
....*....|....*....|....*
gi 497578899 181 TKKGVVFVTHNiEEAMEIAKKIIVF 205
Cdd:cd03238 138 LGNTVILIEHN-LDVLSSADWIIDF 161
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
130-163 |
4.82e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 4.82e-04
10 20 30
....*....|....*....|....*....|....
gi 497578899 130 NELSGGMAHRVSIARALSFNPDILLMDEPFAALD 163
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
42-181 |
1.42e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 39.49 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 42 GESGCGKTTLLRILAGLENATSGNIYFFNNDKkctpkVGMV------FQESRLmpwLNVSenILLHTE----KDNRNKV- 110
Cdd:PRK15064 34 GANGCGKSTFMKILGGDLEPSAGNVSLDPNER-----LGKLrqdqfaFEEFTV---LDTV--IMGHTElwevKQERDRIy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 111 -----DLDKYLKMMKLE--------------------------KFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPF 159
Cdd:PRK15064 104 alpemSEEDGMKVADLEvkfaemdgytaearagelllgvgipeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPT 183
|
170 180
....*....|....*....|..
gi 497578899 160 AALDYFTRRKMQkEVVNIHKNT 181
Cdd:PRK15064 184 NNLDINTIRWLE-DVLNERNST 204
|
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
39-56 |
1.57e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.40 E-value: 1.57e-03
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-163 |
1.76e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 23 LVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNdkkctPKVGMVFQESrlmPWLNVS------- 95
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-----WQLAWVNQET---PALPQPaleyvid 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 96 --------ENILLH-TEKDNRNKV-----DLD------------KYLKMMKLEKFKNSYP-NELSGGMAHRVSIARALSF 148
Cdd:PRK10636 87 gdreyrqlEAQLHDaNERNDGHAIatihgKLDaidawtirsraaSLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALIC 166
|
170
....*....|....*
gi 497578899 149 NPDILLMDEPFAALD 163
Cdd:PRK10636 167 RSDLLLLDEPTNHLD 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
9-168 |
1.96e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 9 ENIYKKYlvdnKEHLVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNndkkcTPKVGMVFQeSR- 87
Cdd:PRK11819 328 ENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-----TVKLAYVDQ-SRd 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 88 -LMP----WLNVSENillhtekdnrnkvdLDkYLKMMKLE----------KFKNS----YPNELSGGMAHRVSIARALSF 148
Cdd:PRK11819 398 aLDPnktvWEEISGG--------------LD-IIKVGNREipsrayvgrfNFKGGdqqkKVGVLSGGERNRLHLAKTLKQ 462
|
170 180
....*....|....*....|
gi 497578899 149 NPDILLMDEPFAALDYFTRR 168
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLR 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
132-195 |
2.19e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.84 E-value: 2.19e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497578899 132 LSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQK--EVVNIHKNTKkgVVFVTHNIEEA 195
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRfvDVLISEGETQ--LLFVSHHAEDA 465
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
23-191 |
4.64e-03 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 37.35 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 23 LVLDNISLNISSEEITVILGESGCGKTTLLRILAGLENATSGNIYFFNNDkkCTPkvgmVFQESRLMPWLNVSENILLHT 102
Cdd:PRK15177 1 VVLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFIGLRGD--ALP----LGANSFILPGLTGEENARMMA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 103 EKDNRNKVDLDKY-LKMMKLEKFKNSYPNELSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNihKNT 181
Cdd:PRK15177 75 SLYGLDGDEFSHFcYQLTQLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQLRMQAALAC--QLQ 152
|
170
....*....|
gi 497578899 182 KKGVVFVTHN 191
Cdd:PRK15177 153 QKGLIVLTHN 162
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
132-209 |
6.06e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 37.40 E-value: 6.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497578899 132 LSGGMAHRVSIARALSFNPDILLMDEPFAALDYFTRRKMQKEVVNIHKNtKKGVVFVTHNIEEAMEIAKKIIVFSKNK 209
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
37-56 |
6.93e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 36.69 E-value: 6.93e-03
|
| rad24 |
TIGR00602 |
checkpoint protein rad24; All proteins in this family for which functions are known are ... |
11-128 |
7.23e-03 |
|
checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129690 [Multi-domain] Cd Length: 637 Bit Score: 37.24 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497578899 11 IYKKYLVDNKEhlVLDNISLNISSEEITVILGESGCGKTTLLRILAG------LENATSGNIYFFNNDKKCTPKVGMVFq 84
Cdd:TIGR00602 88 VHKKKIEEVET--WLKAQVLENAPKRILLITGPSGCGKSTTIKILSKelgiqvQEWSNPTLPDFQKNDHKVTLSLESCF- 164
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 497578899 85 eSRLMPWLNV-SENILLHTEKDNRNKVDLDKYLKMMKLEKFKNSY 128
Cdd:TIGR00602 165 -SNFQSQIEVfSEFLLRATNKLQMLGDDLMTDKKIILVEDLPNQF 208
|
|
| |
