|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-235 |
1.78e-102 |
|
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: 296.69 E-value: 1.78e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD----QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaEPDASRGVVF 79
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-GPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGLELPrspllgrlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:cd03293 80 QQDALLPWLTVLDNVALGLELQ---------GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVrvdphaPGAYGARITYDI 235
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSAR------PGRIVAEVEVDL 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-236 |
6.76e-99 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 289.30 E-value: 6.76e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRY----GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaEPDASRG 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-GPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI 156
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVP---------KAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKvrvdphAPGAYGARITYDIP 236
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSA------RPGRIVEEIDVDLP 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-219 |
5.07e-84 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 254.64 E-value: 5.07e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--V 78
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVgmV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGL---------RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-219 |
4.83e-79 |
|
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: 237.03 E-value: 4.83e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQR 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIgmVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:cd03259 81 YALFPHLTVAENIAFGL---------KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-242 |
2.69e-75 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 229.36 E-value: 2.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYG----DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAePDASRG 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHLTVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI 156
Cdd:COG4525 80 VVFQKDALLPWLNVLDNVAFGL---------RLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVfdkvrVDPHaPGaygaRITYDIP 236
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVV-----MSPG-PG----RIVERLE 220
|
....*.
gi 921961068 237 LNSERR 242
Cdd:COG4525 221 LDFSRR 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-220 |
2.49e-73 |
|
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: 223.27 E-value: 2.49e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQR 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVntVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLP---------KAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVD 220
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-213 |
4.27e-70 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 219.17 E-value: 4.27e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--V 78
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIamV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLELPRSPllgrlfgSAKHHAR-EQAAALLrkvGLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVP-------KAEIDRRvREAAELL---GLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAV 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-201 |
4.87e-69 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 212.21 E-value: 4.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD----QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---- 75
Cdd:COG1136 5 LELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ----GVVFQRYSVFPHLTVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAI 151
Cdd:COG1136 85 rrhiGFVFQFFNLLPELTALENVALPL---------LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-200 |
3.56e-68 |
|
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: 209.65 E-value: 3.56e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQ----VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---- 75
Cdd:cd03255 1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ----GVVFQRYSVFPHLTVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAI 151
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPL---------LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHD 200
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD 200
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-205 |
1.82e-67 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 208.69 E-value: 1.82e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA---EPDASR---GV 77
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkDINKLRrkvGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHLTVLDNVALGLELprspLLGRlfgsAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIK----VKKM----SKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLseGF 205
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEM--GF 198
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-219 |
2.02e-67 |
|
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: 208.29 E-value: 2.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR-------G 76
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELyelrrriG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHLTVLDNVALGL----ELPRSpllgrlfgsakhHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLrehtDLSEA------------EIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-219 |
3.55e-67 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 212.11 E-value: 3.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--V 78
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVntV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFGLRMQKTP---------AAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-219 |
3.73e-65 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 206.15 E-value: 3.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSfISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GV 77
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRErrvGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHLTVLDNVALGLE-LPRSpllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI 156
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRvRPPS----------KAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-216 |
2.16e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 200.68 E-value: 2.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQ 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRrriGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:COG1131 81 EPALYPDLTVRENLRF---------FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-219 |
1.50e-63 |
|
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: 198.49 E-value: 1.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA----AEPDASR---G 76
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHLTVLDNVALGL----ELPRSPLlgrlfgsakhhaREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLrehtRLSEEEI------------REIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 153 QALIMKPRVLLLDEPFGALDPgIRKD-MHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDP-IASGvIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-216 |
1.97e-63 |
|
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: 197.37 E-value: 1.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR------GV 77
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrqkvGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHLTVLDNVALGLElprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPI--------KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALWREtRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDD 210
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
4-219 |
3.27e-63 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 199.93 E-value: 3.27e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD-QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA-EPDASR---GVV 78
Cdd:COG1125 2 IEFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDlDPVELRrriGYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALgleLPRspllgrLFGSAKHHAREQAAALLRKVGLDHA--LDKYPAQLSGGMQQRLAIAQALI 156
Cdd:COG1125 82 IQQIGLFPHMTVAENIAT---VPR------LLGWDKERIRARVDELLELVGLDPEeyRDRYPHELSGGQQQRVGVARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG1125 153 ADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRI 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-202 |
4.64e-63 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 196.81 E-value: 4.64e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR------- 75
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylrrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPL---------RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLS 202
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE 198
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-220 |
9.24e-63 |
|
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: 196.79 E-value: 9.24e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSfISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--V 78
Cdd:cd03296 1 MS-IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVgfV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLELPRspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKP-----RSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVD 220
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIE 216
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-219 |
3.64e-62 |
|
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: 198.72 E-value: 3.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--GVV 78
Cdd:TIGR03265 2 SPYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRdyGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLElprspllGRLFGSAKHHAReqAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAYGLK-------NRGMGRAEVAER--VAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR03265 153 PGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVI 213
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-219 |
1.42e-60 |
|
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: 190.16 E-value: 1.42e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQR 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIamVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGLELprspllgRLFGSAKHHAR-EQAAALLrkvGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKL-------RKVPKDEIDERvREVAELL---QIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-219 |
1.60e-59 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 188.38 E-value: 1.60e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR------GV 77
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERlirqeaGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHLTVLDNVALGlelPRspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFG---PL-----RVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-220 |
2.11e-59 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 188.08 E-value: 2.11e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQR 81
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIgfVFQH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:TIGR00968 81 YALFKHLTVRDNIAFGLEIRKHP---------KAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVD 220
Cdd:TIGR00968 152 LLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIE 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-210 |
4.77e-59 |
|
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: 188.24 E-value: 4.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA--------SRG 76
Cdd:cd03294 26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrkKIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHLTVLDNVALGLELPrspllgrlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI 156
Cdd:cd03294 106 MVFQSFALLPHRTVLENVAFGLEVQ---------GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTR 210
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDR 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-241 |
1.25e-58 |
|
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: 185.75 E-value: 1.25e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaEPDASRGVVFQRYSVFPHLTVLDNVALGL 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPDRMVVFQNYSLLPWLTVRENIALAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 99 ElprsPLLGRLFGSAKHHAREQAAALlrkVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKD 178
Cdd:TIGR01184 80 D----RVLPDLSKSERRAIVEEHIAL---VGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 179 MHQLLLALWRETRLTVFMVTHDLSEGfslgtrLLVFDKVRVDPHAPGAY-GARITYDIPLNSER 241
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEA------LLLSDRVVMLTNGPAANiGQILEVPFPRPRDR 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-242 |
1.49e-58 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 186.44 E-value: 1.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAePDASRGVVFQRYS 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VFPHLTVLDNVALGLELPrspllgrlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLA---------GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 164 LDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFdkvrvdphAPGAygARITYDIPLNSERR 242
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLL--------SPGP--GRVVERLPLNFARR 220
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-251 |
1.61e-58 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 185.34 E-value: 1.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVleGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQR 81
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVsmLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGLelprSPLLgRLfgSAKhhAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:COG3840 80 NNLFPHLTVAQNIGLGL----RPGL-KL--TAE--QRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHAPgaygariTYDIpLNSER 241
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGP-------TAAL-LDGEP 222
|
250
....*....|
gi 921961068 242 RKALAAELGA 251
Cdd:COG3840 223 PPALAAYLGI 232
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-210 |
4.19e-58 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 189.16 E-value: 4.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQV--VLEGL----------------------NLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETAS 56
Cdd:COG4175 1 MPKIEVRNLYKIFGKRPerALKLLdqgkskdeilektgqtvgvndaSFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 57 KGQILLDGQALAAEPDAS----R----GVVFQRYSVFPHLTVLDNVALGLELPrspllgrlfGSAKHHAREQAAALLRKV 128
Cdd:COG4175 81 AGEVLIDGEDITKLSKKElrelRrkkmSMVFQHFALLPHRTVLENVAFGLEIQ---------GVPKAERRERAREALELV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 129 GLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLG 208
Cdd:COG4175 152 GLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLDEALRLG 231
|
..
gi 921961068 209 TR 210
Cdd:COG4175 232 DR 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-215 |
9.31e-58 |
|
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: 181.62 E-value: 9.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR------GV 77
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplrrriGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHLTVLDNVALGlelprspllgrlfgsakhhareqaaallrkvgldhaldkypaqLSGGMQQRLAIAQALIM 157
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-------------------------------------------LSGGQQQRVALARALAM 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFD 215
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-216 |
6.14e-57 |
|
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: 180.74 E-value: 6.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQ--VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----GVV 78
Cdd:cd03225 1 ELKNLSFSYPDGarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQrysvFP-----HLTVLDNVALGLELprspllgrlFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQ 153
Cdd:cd03225 81 FQ----NPddqffGPTVEEEVAFGLEN---------LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 154 ALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWREtRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-251 |
1.74e-56 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 181.03 E-value: 1.74e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRgVVFQRYS 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR-LMFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VFPHLTVLDNVALGLelprspllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:PRK11247 92 LLPWKKVIDNVGLGL---------------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 164 LDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKvrvdphapGAYGARITYDIPLNSERRK 243
Cdd:PRK11247 157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEE--------GKIGLDLTVDLPRPRRRGS 228
|
....*...
gi 921961068 244 ALAAELGA 251
Cdd:PRK11247 229 ARLAELEA 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-219 |
2.98e-56 |
|
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: 180.19 E-value: 2.98e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD-QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA----SRGVV 78
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALgleLPRspllgrLFGSAKHHAREQAAALLRKVGLDHA--LDKYPAQLSGGMQQRLAIAQALI 156
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL---VPK------LLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-202 |
2.97e-55 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 185.11 E-value: 2.97e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY-----GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--- 75
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLrel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ----GVVFQ--RYSVFPHLTVLDNVALGLelprspllgRLFGSA-KHHAREQAAALLRKVGLD-HALDKYPAQLSGGMQQ 147
Cdd:COG1123 341 rrrvQMVFQdpYSSLNPRMTVGDIIAEPL---------RLHGLLsRAERRERVAELLERVGLPpDLADRYPHELSGGQRQ 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLA 466
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-219 |
3.84e-54 |
|
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: 174.06 E-value: 3.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAE--PDASR--GVV 78
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnlRELRRkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQrysvFP-----HLTVLDNVALGLE---LPRSpllgrlfgsakhHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLA 150
Cdd:COG1122 81 FQ----NPddqlfAPTVEEDVAFGPEnlgLPRE------------EIRERVEEALELVGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 151 IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDGRI 212
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-216 |
4.00e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.51 E-value: 4.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPdASRGVVFQ 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRAR-RRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSV---FPhLTVLDNVALGLeLPRSPLLGRLfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:COG1121 83 RAEVdwdFP-ITVRDVVLMGR-YGRRGLFRRP----SRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNR 214
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-216 |
4.07e-54 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 177.99 E-value: 4.07e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 2 SFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VF 79
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIcmVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGL---------KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNK 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-219 |
1.86e-53 |
|
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: 172.52 E-value: 1.86e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDqVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--GVVFQR 81
Cdd:cd03299 1 LKVENLSKDWKE-FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRdiSYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVD---------KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-215 |
2.90e-53 |
|
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: 172.24 E-value: 2.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD---ASRGVV-- 78
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLELP-RSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARtGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFD 215
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLD 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-202 |
4.66e-53 |
|
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: 171.46 E-value: 4.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQ----VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA---EPDASR- 75
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldeDARARLr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ----GVVFQRYSVFPHLTVLDNVALGLELPRSPllgrlfgsakhHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAI 151
Cdd:COG4181 89 arhvGFVFQSFQLLPTLTALENVMLPLELAGRR-----------DARARARALLERVGLGHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-219 |
8.25e-53 |
|
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: 171.52 E-value: 8.25e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNV----WQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---- 75
Cdd:COG1124 2 LEVRNLsvsyGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrrrv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRY--SVFPHLTVLDNVALGLELPRSPllgrlfgsakhHAREQAAALLRKVGLDHA-LDKYPAQLSGGMQQRLAIA 152
Cdd:COG1124 82 QMVFQDPyaSLHPRHTVDRILAEPLRIHGLP-----------DREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-219 |
4.15e-52 |
|
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: 168.44 E-value: 4.15e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVleGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQR 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVsmLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGlelpRSPLLgRLfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:cd03298 79 NNLFAHLTVEQNVGLG----LSPGL-KL----TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03298 150 LLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-216 |
7.02e-52 |
|
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: 169.07 E-value: 7.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----GVVF 79
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELarriAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGlelpRSPLLGRlFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:COG1120 82 QEPPAPFGLTVRELVALG----RYPHLGL-FGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-201 |
1.23e-51 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 168.31 E-value: 1.23e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR------- 75
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlrrri 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGLeLPRSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAGR-LGRTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARAL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:COG3638 162 VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQV 207
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-213 |
2.41e-51 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 170.65 E-value: 2.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSfISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQalaaepDASR----- 75
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT------DVSRlhard 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ---GVVFQRYSVFPHLTVLDNVALGLE-LPRSPllgRLFGSAkhhAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAI 151
Cdd:PRK10851 74 rkvGFVFQHYALFRHMTVFDNIAFGLTvLPRRE---RPNAAA---IKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVV 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-216 |
1.19e-50 |
|
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: 164.63 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDaSRGVVFQRYSV 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-RIGYVPQRRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 85 ---FPhLTVLDNVALGLELPRspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:cd03235 80 drdFP-ISVRDVVLMGLYGHK-----GLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLLNR 207
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-224 |
2.00e-50 |
|
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: 164.66 E-value: 2.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL-----LGQETASKGQILLDGQ---ALAAEPDASR 75
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLDGKdiyDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ---GVVFQRYSVFPhLTVLDNVALGLelprspllgRLFGSAKHHAREQ-AAALLRKVGL-DHALDKYPA-QLSGGMQQRL 149
Cdd:cd03260 81 rrvGMVFQKPNPFP-GSIYDNVAYGL---------RLHGIKLKEELDErVEEALRKAALwDEVKDRLHAlGLSGGQQQRL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 150 AIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHAP 224
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
11-213 |
2.08e-50 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 168.88 E-value: 2.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 11 QRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--------GVVFQRY 82
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELrevrrkkiGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 83 SVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVL 162
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPELLGWP---------EQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 163 LLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:TIGR01186 152 LMDEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVI 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-219 |
2.33e-50 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 168.67 E-value: 2.33e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--V 78
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVgmV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLELPrspllgrlfGSAKHHAR---EQAAALLRkvgLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLA---------GAKKEEINqrvNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK11000 149 VAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
4-202 |
1.29e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 163.43 E-value: 1.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLR---LLlgqETASKGQILLDGQALAAEPD-------A 73
Cdd:COG4598 9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRcinLL---ETPDSGEIRVGGEEIRLKPDrdgelvpA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 74 SR----------GVVFQRYSVFPHLTVLDNValgLELPRspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSG 143
Cdd:COG4598 86 DRrqlqrirtrlGMVFQSFNLWSHMTVLENV---IEAPV-----HVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 144 GMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLS 202
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMG 215
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
1.66e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 162.87 E-value: 1.66e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSfISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQA--LAAEPDASR--- 75
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKAirl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 -----GVVFQRYSVFPHLTVLDNvalgleLPRSPLlgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLA 150
Cdd:COG4161 80 lrqkvGMVFQQYNLWPHLTVMEN------LIEAPC--KVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 151 IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
12-202 |
2.07e-49 |
|
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: 161.90 E-value: 2.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR-------GVVFQR-YS 83
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkeiQMVFQDpMS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VF-PHLTVLDNVAlglElprsPLLGRLFGSAKHHAREQAAALLRKVGLDHA-LDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:cd03257 94 SLnPRMTIGEQIA---E----PLRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALALNPKL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:cd03257 167 LIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLG 207
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-219 |
2.70e-49 |
|
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: 161.98 E-value: 2.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQ----VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---- 75
Cdd:cd03258 2 IELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ---GVVFQRYSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:cd03258 82 rriGMIFQHFNLLSSRTVFENVALPLEIAGVP---------KAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-216 |
4.22e-49 |
|
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: 159.49 E-value: 4.22e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQ 80
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrriGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNValglelprspllgrlfgsakhhareqaaallrkvgldhaldkypaQLSGGMQQRLAIAQALIMKPR 160
Cdd:cd03230 81 EPSLYENLTVRENL---------------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNN 170
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-219 |
1.47e-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: 163.05 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 34 LVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--GVVFQRYSVFPHLTVLDNVALGLELPRSPllgrlfg 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRhiNMVFQSYALFPHMTVEENVAFGLKMRKVP------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 112 saKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETR 191
Cdd:TIGR01187 74 --RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151
|
170 180
....*....|....*....|....*...
gi 921961068 192 LTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKI 179
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-219 |
3.19e-48 |
|
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: 166.23 E-value: 3.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY--GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG---QETASKGQILLDGQALAAEPDASRG-- 76
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALRGrr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 --VVFQ--RYSVFPhLTVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:COG1123 85 igMVFQdpMTQLNP-VTVGDQIAEAL---------ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-219 |
4.36e-48 |
|
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: 158.23 E-value: 4.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVD---EGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAE------PDASR--GVVFQRYSVFPH 87
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinlPPQQRkiGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 88 LTVLDNVALGLELPRSPLLgrlfgsakhhaREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEP 167
Cdd:cd03297 90 LNVRENLAFGLKRKRNRED-----------RISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 921961068 168 FGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
12-211 |
5.64e-48 |
|
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: 163.02 E-value: 5.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILL---DGQALAAEPDASR---------GVVF 79
Cdd:TIGR03415 33 RTGLVLGVHNASLDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVkdgDGSVDVANCDAATlrrlrthrvSMVF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGLELPrspllgrlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:TIGR03415 113 QQFALLPWRTVEENVAFGLEMQ---------GMPKAERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEA 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRL 211
Cdd:TIGR03415 184 PILLMDEPFSALDPLIRTQLQDELLELQSKLKKTIVFVSHDLDEALKIGNRI 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-219 |
7.11e-48 |
|
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: 159.54 E-value: 7.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYG-----DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--- 75
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLkdl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ----GVVFQrysvFPH-----LTVLDNVALGlelPRSpllgrlFGSAKHHAREQAAALLRKVGLDHA-LDKYPAQLSGGM 145
Cdd:TIGR04521 81 rkkvGLVFQ----FPEhqlfeETVYKDIAFG---PKN------LGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKI 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-219 |
1.13e-47 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 158.25 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSfISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQA--LAAEPDASR--- 75
Cdd:PRK11124 1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAire 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 -----GVVFQRYSVFPHLTVLDNValgLELPRspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLA 150
Cdd:PRK11124 80 lrrnvGMVFQQYNLWPHLTVQQNL---IEAPC-----RVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 151 IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
19-219 |
6.91e-47 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 159.09 E-value: 6.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQRYSVFPHLTVLDNVAL 96
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIayVYQNYMLFPHKTVFENIAF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 97 GLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIR 176
Cdd:NF040840 96 GLKLRKVP---------KEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 921961068 177 KDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:NF040840 167 DELIREMKRWHREFGFTAIHVTHNFEEALSLADRVGIMLNGRL 209
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-202 |
1.28e-46 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 157.93 E-value: 1.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNV----WQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---- 75
Cdd:COG1135 2 IELENLsktfPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ---GVVFQRYSVFPHLTVLDNVALglelprsPLlgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:COG1135 82 rkiGMIFQHFNLLSSRTVAENVAL-------PL--EIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMD 202
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-202 |
1.66e-46 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 154.33 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA-------SR 75
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRqlpllrrRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:TIGR02673 82 GVVFQDFRLLPDRTVYENVALPLEVRGKK---------EREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrLTVFMVTHDLS 202
Cdd:TIGR02673 153 VNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRG-TTVIVATHDLS 198
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
5-200 |
4.82e-46 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 153.02 E-value: 4.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQ---ETASKGQILLDGQALAAEPDASR--GVVF 79
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlspAFSASGEVLLNGRRLTALPAEQRriGILF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGLelPRSPllgrlfgsAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:COG4136 83 QDDLLFPHLSVGENLAFAL--PPTI--------GRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHD 200
Cdd:COG4136 153 RALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-222 |
7.43e-46 |
|
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: 153.47 E-value: 7.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQ 80
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrqiGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:COG4555 82 ERGLYDRLTVRENIRY---------FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVDPH 222
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-201 |
8.48e-46 |
|
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: 152.51 E-value: 8.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR------- 75
Cdd:TIGR02211 5 ENLGKRYQEGKLDTrVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERaklrnkk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 -GVVFQRYSVFPHLTVLDNVALglelprsPLLgrLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQA 154
Cdd:TIGR02211 85 lGFIYQFHHLLPDFTALENVAM-------PLL--IGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 921961068 155 LIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:TIGR02211 156 LVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDL 202
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-216 |
1.35e-45 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 156.53 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQR 81
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPInmMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:PRK11607 100 YALFPHMTVEQNIAFGLKQDKLP---------KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:PRK11607 171 LLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNR 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-202 |
1.63e-45 |
|
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: 152.34 E-value: 1.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS----R--- 75
Cdd:cd03256 1 IEVENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlRrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGLeLPRSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGR-LGRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVD 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-219 |
1.67e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 152.04 E-value: 1.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 23 NLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQRYSVFPHLTVLDNVALGLel 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVsmLFQENNLFSHLTVAQNIGLGL-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 101 prSPLLgRLfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMH 180
Cdd:PRK10771 97 --NPGL-KL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 921961068 181 QLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-213 |
2.18e-45 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 151.12 E-value: 2.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA-EPDASR---GVVF 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRrqvAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRySVFPHLTVLDNVALGLELprspllgrlfgSAKHHAREQAAALLRKVGLDHA-LDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:COG4619 81 QE-PALWGGTVRDNLPFPFQL-----------RERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLT 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
4-200 |
5.90e-45 |
|
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: 150.25 E-value: 5.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVV-LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA-------SR 75
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipylrrKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGLELPRSPllGRLfgsakhhAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVP--PRE-------IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHD 200
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKI-NKAGTTVVVATHA 195
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-219 |
7.76e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 153.85 E-value: 7.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV-- 77
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIam 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHLTVLDNVALGLELprspllgRLFGSAKHHAREQAAAllRKVGLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKI-------RGMPKAEIEERVAEAA--RILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
1.11e-44 |
|
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: 147.41 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----GVVFQRYSVFPHLTVLDNV 94
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 95 ALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALD----KYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPF 168
Cdd:pfam00005 81 RLGL---------LLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-219 |
1.59e-44 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 150.29 E-value: 1.59e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQIlldgQALAAEPDASR----- 75
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI----RVGDITIDTARslsqq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 -----------GVVFQRYSVFPHLTVLDNVALGlelprsPLLGRlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGG 144
Cdd:PRK11264 77 kglirqlrqhvGFVFQNFNLFPHRTVLENIIEG------PVIVK--GEPKEEATARARELLAKVGLAGKETSYPRRLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 145 MQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-203 |
4.23e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 147.63 E-value: 4.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQ 80
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALglelprsplLGRLFGsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:COG4133 83 ADGLKPELTVRENLRF---------WAALYG--LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLAlWRETRLTVFMVTHDLSE 203
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQPLE 193
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
8-201 |
1.25e-43 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 146.61 E-value: 1.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 8 NVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--------GVVF 79
Cdd:TIGR03608 3 NISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKAskfrreklGYLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGLELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:TIGR03608 83 QNFALIENETVEENLDLGLKYKKLS---------KKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDL 201
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDP 194
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-216 |
7.23e-43 |
|
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: 144.96 E-value: 7.23e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD--QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVV 78
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARqslGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:cd03263 81 PQFDALFDELTVREHLRF---------YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALwRETRlTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV-RKGR-SIILTTHSMDEAEALCDRIAIMSD 207
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-216 |
7.46e-43 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 146.42 E-value: 7.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY--GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDASR------ 75
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL---DEENlweirk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 --GVVFQRysvfPH-----LTVLDNVALGLE---LPRSPLlgrlfgsakhhaREQAAALLRKVGLDHALDKYPAQLSGGM 145
Cdd:TIGR04520 78 kvGMVFQN----PDnqfvgATVEDDVAFGLEnlgVPREEM------------RKRVDEALKLVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGfSLGTRLLVFDK 216
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-217 |
3.57e-42 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 143.98 E-value: 3.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD-------ASR 75
Cdd:TIGR02315 2 LEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklrklrRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGlELPRSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHG-RLGYKPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLL-------VFDKV 217
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVglkageiVFDGA 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-202 |
3.94e-42 |
|
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: 145.97 E-value: 3.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY--GDQVV--LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG---QETASKGQILLDGQALAAEPDAS-- 74
Cdd:COG0444 2 LEVRNLKVYFptRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLSEKElr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 75 --RG----VVFQR-YSVF-PHLTVLDNVALGLelprspllgRLFGSAKHH-AREQAAALLRKVGLDHA---LDKYPAQLS 142
Cdd:COG0444 82 kiRGreiqMIFQDpMTSLnPVMTVGDQIAEPL---------RIHGGLSKAeARERAIELLERVGLPDPerrLDRYPHELS 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 143 GGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLG 212
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
4-201 |
2.72e-41 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 141.66 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL-----LGQETASKGQILLDGQAL------AAEPD 72
Cdd:TIGR00972 2 IEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLnrmndLVPGVRIEGKVLFDGQDIydkkidVVELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 73 ASRGVVFQRYSVFPhLTVLDNVALGLelprspllgRLFG-SAKHHAREQAAALLRKVGLDHA----LDKYPAQLSGGMQQ 147
Cdd:TIGR00972 82 RRVGMVFQKPNPFP-MSIYDNIAYGP---------RLHGiKDKKELDEIVEESLKKAALWDEvkdrLHDSALGLSGGQQQ 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDP----GIRKDMHQLllalwrETRLTVFMVTHDL 201
Cdd:TIGR00972 152 RLCIARALAVEPEVLLLDEPTSALDPiatgKIEELIQEL------KKKYTIVIVTHNM 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-224 |
4.73e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 141.64 E-value: 4.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQ--ALAAEPDASRGV---- 77
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtiNLVRDKDGQLKVadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 -----------VFQRYSVFPHLTVLDNValgLELPRspllgRLFGSAKHHAREQAAALLRKVGLDH-ALDKYPAQLSGGM 145
Cdd:PRK10619 86 qlrllrtrltmVFQHFNLWSHMTVLENV---MEAPI-----QVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHAP 224
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGA 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
19-219 |
3.35e-40 |
|
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: 141.78 E-value: 3.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVD----EGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDASRGV-----------VFQRYS 83
Cdd:COG4148 11 RGGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ---DSARGIflpphrrrigyVFQEAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VFPHLTVLDNVALGLElprspllgRLFGSAKHHAREQAAALLrkvGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:COG4148 88 LFPHLSVRGNLLYGRK--------RAPRAERRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 164 LDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRV 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
4-213 |
3.43e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 142.86 E-value: 3.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR-------- 75
Cdd:PRK10070 29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrrkki 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGLELPrspllgrlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELA---------GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:PRK10070 180 AINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAI 237
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
4-219 |
3.66e-40 |
|
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: 137.69 E-value: 3.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVwqRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGV--VFQR 81
Cdd:TIGR01277 1 LALDKV--RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVsmLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALGLElprspllgrlfGSAKHHA--REQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:TIGR01277 79 NNLFAHLTVRQNIGLGLH-----------PGLKLNAeqQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR01277 148 PILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-200 |
5.14e-40 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 137.84 E-value: 5.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD----QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---- 75
Cdd:TIGR02982 2 ISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLvqlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ---GVVFQRYSVFPHLTVLDNVALGLELprSPLLGRLfgsakhHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:TIGR02982 82 rriGYIFQAHNLLGFLTARQNVQMALEL--QPNLSYQ------EARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHD 200
Cdd:TIGR02982 154 RALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-219 |
6.66e-40 |
|
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: 137.50 E-value: 6.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQ 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRrriGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:cd03265 81 DLSVDDELTGWENLYI---------HARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-219 |
1.11e-39 |
|
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: 139.06 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 11 QRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQRYSVFPH 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRrsiGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 88 LTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEP 167
Cdd:TIGR01188 81 LTGRENLEM---------MGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 921961068 168 FGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRAL-KEEGVTILLTTHYMEEADKLCDRIAIIDHGRI 202
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-201 |
1.22e-39 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.86 E-value: 1.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL-----LGQETASKGQILLDGQ---ALAAEPDASR 75
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndLIPGARVEGEILLDGEdiyDPDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ---GVVFQRYSVFPHlTVLDNVALGLELprsplLGRLFGSAKHHAREQAaalLRKVGL-----DHaLDKYPAQLSGGMQQ 147
Cdd:COG1117 92 rrvGMVFQKPNPFPK-SIYDNVAYGLRL-----HGIKSKSELDEIVEES---LRKAALwdevkDR-LKKSALGLSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwREtRLTVFMVTHDL 201
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KK-DYTIVIVTHNM 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-219 |
1.96e-39 |
|
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: 135.78 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFcTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGVVF---Q 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGylpQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:cd03264 80 EFGVYPNFTVREFLDY---------IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALwRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSEL-GEDR-IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-219 |
3.51e-39 |
|
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: 135.64 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD---ASRGVVF- 79
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPherARAGIGYv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 -QRYSVFPHLTVLDNVALGlelprspllgrlfGSAKHHAREQAAallrkvgLDHALDKYPA----------QLSGGMQQR 148
Cdd:cd03224 81 pEGRRIFPELTVEENLLLG-------------AYARRRAKRKAR-------LERVYELFPRlkerrkqlagTLSGGEQQM 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 149 LAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRV 210
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-199 |
4.63e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.40 E-value: 4.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 3 FISVNNVWQRYGDQVV-LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA-------S 74
Cdd:PRK11153 4 LKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrkarrQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 75 RGVVFQRYSVFPHLTVLDNVALGLELPrspllgrlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQA 154
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELA---------GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 155 LIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTH 199
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-203 |
1.53e-38 |
|
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: 133.50 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--GVVFQR 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRriGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREqaaaLLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:cd03268 81 PGFYPNLTARENLRL---------LARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 921961068 162 LLLDEPFGALDP-GIrKDMHQLLLALwRETRLTVFMVTHDLSE 203
Cdd:cd03268 148 LILDEPTNGLDPdGI-KELRELILSL-RDQGITVLISSHLLSE 188
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-202 |
2.45e-38 |
|
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: 141.51 E-value: 2.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV--VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA-EPDASR---GV 77
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRrqiGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFpHLTVLDNVALGlelprspllgrlfgsAKHHAREQAAALLRKVGLDHALDKYP-----------AQLSGGMQ 146
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLG---------------DPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQR 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDLS 202
Cdd:COG2274 618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLS 671
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-219 |
6.84e-38 |
|
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: 132.41 E-value: 6.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD---ASRGV 77
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhriARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VF--QRYSVFPHLTVLDNVALGLELPRspllgrlfGSAKHHAReqaaallrkvgLDHALDKYP----------AQLSGGM 145
Cdd:COG0410 81 GYvpEGRRIFPSLTVEENLLLGAYARR--------DRAEVRAD-----------LERVYELFPrlkerrrqraGTLSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRI 214
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-216 |
1.30e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 129.29 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAsrgvvfqrysv 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 85 fphltvldnvalglelprspllgrlfgsakhhareqaaALLRKVGLDHaldkypaQLSGGMQQRLAIAQALIMKPRVLLL 164
Cdd:cd00267 70 --------------------------------------ELRRRIGYVP-------QLSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 921961068 165 DEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:cd00267 105 DEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-202 |
2.37e-37 |
|
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: 129.04 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD--QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----GV 77
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFpHLTVLDNValglelprspllgrlfgsakhhareqaaallrkvgldhaldkypaqLSGGMQQRLAIAQALIM 157
Cdd:cd03228 81 VPQDPFLF-SGTIRENI----------------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRlTVFMVTHDLS 202
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRAL-AKGK-TVIVIAHRLS 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-213 |
3.55e-37 |
|
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: 129.09 E-value: 3.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAepdasrgvvfqrysv 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 85 FPHLTVLDNVALgleLPrspllgrlfgsakhhareQAaalLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLL 164
Cdd:cd03214 66 LSPKELARKIAY---VP------------------QA---LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 921961068 165 DEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVIL 170
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-245 |
7.15e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 130.59 E-value: 7.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 17 VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----GVVFQRYSV--FPHLTV 90
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRakyiGRVFQDPMMgtAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 91 LDNVALGLELPRSPLLGRLFGSA-KHHAREQAAALlrKVGLDHALDKYPAQLSGGmqQRLAIaqALIM----KPRVLLLD 165
Cdd:COG1101 100 EENLALAYRRGKRRGLRRGLTKKrRELFRELLATL--GLGLENRLDTKVGLLSGG--QRQAL--SLLMatltKPKLLLLD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 166 EPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKvrvdphapgaygARITYDIplNSERRKAL 245
Cdd:COG1101 174 EHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHE------------GRIILDV--SGEEKKKL 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-202 |
4.93e-36 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 133.66 E-value: 4.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 9 VWQRYGDQVV-LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQEtASKGQILLDGQALAAEPDASR-------GVVFQ 80
Cdd:COG4172 291 LFRRTVGHVKaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALrplrrrmQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 R-YSVF-PHLTVLDNVALGLELPRSPLlgrlfgSAKHHaREQAAALLRKVGLDHA-LDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:COG4172 370 DpFGSLsPRMTVGQIIAEGLRVHGPGL------SAAER-RARVAEALEEVGLDPAaRHRYPHEFSGGQRQRIAIARALIL 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLA 487
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
11-219 |
5.17e-36 |
|
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: 130.62 E-value: 5.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 11 QRYGDQVVleGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDASRGV-----------VF 79
Cdd:TIGR02142 7 KRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF---DSRKGIflppekrrigyVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGLELPRSPLLGRLFgsakhhareqaAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:TIGR02142 82 QEARLFPHLSVRGNLRYGMKRARPSERRISF-----------ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-200 |
5.47e-36 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 127.59 E-value: 5.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--------GVVFQRYSVFPHLT 89
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklrakhvGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 90 VLDNVALglelprsPLLGRlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFG 169
Cdd:PRK10584 105 ALENVEL-------PALLR--GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190
....*....|....*....|....*....|.
gi 921961068 170 ALDPGIRKDMHQLLLALWRETRLTVFMVTHD 200
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-248 |
1.09e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 128.31 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYG---DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEP--DASR 75
Cdd:PRK13650 2 SNIIEVKNLTFKYKedqEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 --GVVFQRY-SVFPHLTVLDNVALGLE---LPRSPLLGRLfgsakhharEQAAALlrkVGLDHALDKYPAQLSGGMQQRL 149
Cdd:PRK13650 82 kiGMVFQNPdNQFVGATVEDDVAFGLEnkgIPHEEMKERV---------NEALEL---VGMQDFKEREPARLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 150 AIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEgFSLGTRLLVFDKVRVDPHA-PGAYG 228
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-VALSDRVLVMKNGQVESTStPRELF 228
|
250 260
....*....|....*....|....*.
gi 921961068 229 AR------ITYDIPLNSERRKALAAE 248
Cdd:PRK13650 229 SRgndllqLGLDIPFTTSLVQSLRQN 254
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-202 |
2.25e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 128.31 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-----RGV--VFQR-YSVF-PHLT 89
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrRRMqmVFQDpYASLnPRMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 90 VLDNVALGLelprspllgRLFGSAKHHAR-EQAAALLRKVGL--DHAlDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDE 166
Cdd:COG4608 114 VGDIIAEPL---------RIHGLASKAERrERVAELLELVGLrpEHA-DRYPHEFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 921961068 167 PFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:COG4608 184 PVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-199 |
3.32e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 126.11 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 8 NVWqrYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLR-----LLLGQETASKGQILLDGQALAAE---PDASR---G 76
Cdd:PRK14267 11 RVY--YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPdvdPIEVRrevG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHLTVLDNVALGLELPRspllgrlFGSAKHHAREQAAALLRKVGL----DHALDKYPAQLSGGMQQRLAIA 152
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNG-------LVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWREtrLTVFMVTH 199
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTH 206
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-214 |
4.71e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 130.52 E-value: 4.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 3 FISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA-AEPDASR----GV 77
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQaagiAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHLTVLDNVALGLELPRSPLLGRlfgsakHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGGLIDW------RAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVF 214
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-202 |
2.41e-34 |
|
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: 129.49 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD-QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----GVV 78
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWrrqiAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRySVFPHLTVLDNVALGlelprspllgrlfgsaKHHA-REQAAALLRKVGLDHALDKYP-----------AQLSGGMQ 146
Cdd:COG4988 417 PQN-PYLFAGTIRENLRLG----------------RPDAsDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQA 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDLS 202
Cdd:COG4988 480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA 533
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-250 |
2.64e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.36 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 2 SFISVNNVWQRYGDQ--VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEP--DASR-- 75
Cdd:PRK13635 4 EIIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwDVRRqv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRY-SVFPHLTVLDNVALGLE---LPRSPLLGRLfgsakhhareQAAalLRKVGLDHALDKYPAQLSGGMQQRLAI 151
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDDVAFGLEnigVPREEMVERV----------DQA--LRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSlGTRLLVFDKVRVdpHAPG------ 225
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEI--LEEGtpeeif 228
|
250 260
....*....|....*....|....*...
gi 921961068 226 AYGA---RITYDIPLnSERRKALAAELG 250
Cdd:PRK13635 229 KSGHmlqEIGLDVPF-SVKLKELLKRNG 255
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-201 |
5.31e-34 |
|
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: 128.26 E-value: 5.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 11 QRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKS----TFLRLLLGQETASKGQILLDGQALAAEPDAS----RG----VV 78
Cdd:COG4172 18 QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGnriaMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQR--YSVFPHLTVLDNVALGLELPRspllgrlfGSAKHHAREQAAALLRKVGLDHA---LDKYPAQLSGGMQQRLAIAQ 153
Cdd:COG4172 98 FQEpmTSLNPLHTIGKQIAEVLRLHR--------GLSGAAARARALELLERVGIPDPerrLDAYPHQLSGGQRQRVMIAM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 921961068 154 ALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL 217
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-201 |
5.35e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 122.92 E-value: 5.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS----RGVVF 79
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrRAVLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSV-FPhLTVLDNVALGlelpRSPLlgrlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI-- 156
Cdd:COG4559 82 QHSSLaFP-FTVEEVVALG----RAPH-----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAql 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 921961068 157 -----MKPRVLLLDEPFGALDPGirkdmHQL----LLALWRETRLTVFMVTHDL 201
Cdd:COG4559 152 wepvdGGPRWLFLDEPTSALDLA-----HQHavlrLARQLARRGGGVVAVLHDL 200
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-219 |
1.48e-33 |
|
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: 120.46 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGVVFQRYS 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:cd03269 81 LYPKMKVIDQLVY---------LAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 164 LDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRA 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-219 |
1.78e-33 |
|
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: 121.34 E-value: 1.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQ-ILLDGQALAAE--PDASR-- 75
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEdvWELRKri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVV----FQRYSvfPHLTVLDNVALGL----ELPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQ 147
Cdd:COG1119 81 GLVspalQLRFP--RDETVLDVVLSGFfdsiGLYREP---------TDEQRERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRV 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-219 |
2.67e-33 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 121.45 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 2 SFISVNNVWQRY---------GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD 72
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 73 ASR-------GVVFQRY--SVFPHLTVLdnvalglELPRSPL--LGRLFGSAKhhaREQAAALLRKVGL-DHALDKYPAQ 140
Cdd:TIGR02769 81 KQRrafrrdvQLVFQDSpsAVNPRMTVR-------QIIGEPLrhLTSLDESEQ---KARIAELLDMVGLrSEDADKLPRQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 141 LSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR02769 151 LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
3.16e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 121.64 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV--VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAE--PDASR--GV 77
Cdd:PRK13632 8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlKEIRKkiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRY-SVFPHLTVLDNVALGLE---LPRSPLLGRLFGSAKhhareqaaallrKVGLDHALDKYPAQLSGGMQQRLAIAQ 153
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIAFGLEnkkVPPKKMKDIIDDLAK------------KVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 154 ALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFsLGTRLLVFDKVRV 219
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKL 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-219 |
5.31e-33 |
|
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: 125.65 E-value: 5.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY--GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----GV 77
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrrriAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFpHLTVLDNVALglelprspllgrlfgsAKHHA-REQAAALLRKVGLDHALDKYP-----------AQLSGGM 145
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRL----------------ARPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDLSeGFSLGTRLLVFDKVRV 219
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLA-GLERMDRILVLEDGRI 547
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-202 |
1.11e-32 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 124.89 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-R---GVV 78
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlRrqiGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFpHLTVLDNVALGlelprspllgrlfgsAKHHAREQAAALLRKVGLDHALDKYP-----------AQLSGGMQQ 147
Cdd:COG1132 420 PQDTFLF-SGTIRENIRYG---------------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQ 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDLS 202
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS 536
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-201 |
1.21e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.49 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA----SRGVVF 79
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAelarRRAVLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSV-FPhLTVLDNVALGlelpRSPLlgrlfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI-- 156
Cdd:PRK13548 83 QHSSLsFP-FTVEEVVAMG----RAPH-----GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 921961068 157 ----MKPRVLLLDEPFGALDPGirkdmHQLLL-----ALWRETRLTVFMVTHDL 201
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLA-----HQHHVlrlarQLAHERGLAVIVVLHDL 201
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-218 |
2.28e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 120.30 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQ 80
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARqrvGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:PRK13537 88 FDNLDPDFTVRENLLV---------FGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVR 218
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-227 |
2.39e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.55 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD---ASRGVV-- 78
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiARMGVVrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDN--VALGLELpRSPLLGRLFGS-----AKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAI 151
Cdd:PRK11300 86 FQHVRLFREMTVIENllVAQHQQL-KTGLFSGLLKTpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVF-----------DKVRVD 220
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVnqgtplangtpEEIRNN 244
|
....*..
gi 921961068 221 PHAPGAY 227
Cdd:PRK11300 245 PDVIKAY 251
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-201 |
4.53e-32 |
|
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: 122.99 E-value: 4.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY-----GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQI---LLDGQALAAEPD--- 72
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrVGDEWVDMTKPGpdg 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 73 ---ASR--GVVFQRYSVFPHLTVLDNV--ALGLELPrspllgrlfgsaKHHAREQAAALLRKVGLDHA-----LDKYPAQ 140
Cdd:TIGR03269 360 rgrAKRyiGILHQEYDLYPHRTVLDNLteAIGLELP------------DELARMKAVITLKMVGFDEEkaeeiLDKYPDE 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 141 LSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDM 488
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
4-224 |
5.88e-32 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 117.99 E-value: 5.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD----QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQA-----LAAEPDAS 74
Cdd:COG4107 9 LSVRGLSKRYGPgcgtVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDggprdLFALSEAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 75 R--------GVVFQrysvfphltvldNVALGLELPRS-------PLLGrlfGSAKHHA--REQAAALLRKVGLDHA-LDK 136
Cdd:COG4107 89 RrrlrrtdwGMVYQ------------NPRDGLRMDVSaggniaeRLMA---AGERHYGdiRARALEWLERVEIPLErIDD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 137 YPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVF-- 214
Cdd:COG4107 154 LPRTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMkn 233
|
250
....*....|....*....
gi 921961068 215 ---------DKVRVDPHAP 224
Cdd:COG4107 234 grvvesgltDQVLEDPQHP 252
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-199 |
7.23e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.20 E-value: 7.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 23 NLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--------GVVFQrysvFPHL-----T 89
Cdd:PRK13634 27 NVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkplrkkvGIVFQ----FPEHqlfeeT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 90 VLDNVALGlelPRSpllgrlFGSAKHHAREQAAALLRKVGLDHA-LDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPF 168
Cdd:PRK13634 103 VEKDICFG---PMN------FGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190
....*....|....*....|....*....|.
gi 921961068 169 GALDPGIRKDMHQLLLALWRETRLTVFMVTH 199
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEKGLTTVLVTH 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-203 |
8.89e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 121.67 E-value: 8.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA-AEP-DASR---GVV 78
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPrDAIAlgiGMV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLELPRSPLLGRlfgsakHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:COG3845 86 HQHFMLVPNLTVAENIVLGLEPTKGGRLDR------KAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSE 203
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLRE 203
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
7-200 |
1.28e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 122.53 E-value: 1.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 7 NNVWQRY--GDQ--VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL--LGQETASK----GQIL--LDGQALAAEPDAS 74
Cdd:PRK10535 8 KDIRRSYpsGEEqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcLDKPTSGTyrvaGQDVatLDADALAQLRREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 75 RGVVFQRYSVFPHLTVLDNValglELPrspllGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQA 154
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNV----EVP-----AVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 155 LIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHD 200
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-202 |
1.85e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 115.68 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--------GVVFQRYSVFPHLT 89
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnqklGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 90 VLDNVALglelprsPLLgrLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFG 169
Cdd:PRK11629 104 ALENVAM-------PLL--IGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190
....*....|....*....|....*....|...
gi 921961068 170 ALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-199 |
2.43e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 116.17 E-value: 2.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL-----LGQETASKGQILLDGQALAAEP--DA 73
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrlieLYPEARVSGEVYLDGQDIFKMDviEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 74 SRGV--VFQRYSVFPHLTVLDNVALGLELPRspllgrlFGSAKHHAREQAAALLRKVGL----DHALDKYPAQLSGGMQQ 147
Cdd:PRK14247 81 RRRVqmVFQIPNPIPNLSIFENVALGLKLNR-------LVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWREtrLTVFMVTH 199
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTH 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-202 |
5.51e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 116.36 E-value: 5.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-------RG 76
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpeeRG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 vvfqrysVFPHLTVLDNVAlglelprspLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI 156
Cdd:COG4152 82 -------LYPKMKVGEQLV---------YLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLS 202
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQME 190
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
10-213 |
7.79e-31 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 116.73 E-value: 7.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 10 WQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR-------GVVFQR- 81
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsdiQMIFQDp 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 -YSVFPHLTVLDNVALGLELPRSPLlgrlfgsAKHHAREQAAALLRKVGL-DHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:PRK15079 108 lASLNPRMTIGEIIAEPLRTYHPKL-------SRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:PRK15079 181 KLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLV 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-203 |
1.14e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.75 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL-----LGQETASKGQILLDGQAL-AAEPDASR-- 75
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrmneLESEVRVEGRVEFFNQNIyERRVNLNRlr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ---GVVFQRYSVFPhLTVLDNVALGLEL----PRSPLLGRLFGSAKhhareqAAALLRKVglDHALDKYPAQLSGGMQQR 148
Cdd:PRK14258 88 rqvSMVHPKPNLFP-MSVYDNVAYGVKIvgwrPKLEIDDIVESALK------DADLWDEI--KHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 149 LAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSE 203
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQ 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-219 |
1.61e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.05 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA-----AEPDASR--GVVFQRYSVFP 86
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknrEVPFLRRqiGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 87 HLTVLDNVALglelprsPLLgrLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDE 166
Cdd:PRK10908 93 DRTVYDNVAI-------PLI--IAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 921961068 167 PFGALDPGIRKDMHQLLLALWReTRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-173 |
3.52e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.43 E-value: 3.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEP---DASRGV 77
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VF--QRYSVFPHLTVLDNVALGLELprspllgrlFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:COG1137 81 GYlpQEASIFRKLTVEDNILAVLEL---------RKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|....*...
gi 921961068 156 IMKPRVLLLDEPFGALDP 173
Cdd:COG1137 152 ATNPKFILLDEPFAGVDP 169
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-207 |
3.86e-30 |
|
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: 112.25 E-value: 3.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEP---DASRGVVF- 79
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhkRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 -QRYSVFPHLTVLDNVALGLELprspllgrlFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:cd03218 81 pQEASIFRKLTVEENILAVLEI---------RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSL 207
Cdd:cd03218 152 PKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSI 199
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-215 |
4.20e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 113.24 E-value: 4.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRY---------GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 72 DASRG-------VVFQRY--SVFPHLTVLDNValglelpRSPLLgRLFGSAKHHAREQAAALLRKVGLDHA-LDKYPAQL 141
Cdd:PRK10419 81 RAQRKafrrdiqMVFQDSisAVNPRKTVREII-------REPLR-HLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 142 SGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFD 215
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMD 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
18-201 |
1.37e-29 |
|
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: 110.04 E-value: 1.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDG-QALAAEPDASRGVVFQ--RYSVFPHlTVLDNV 94
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkPIKAKERRKSIGYVMQdvDYQLFTD-SVREEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 95 ALGLELPrspllgrlfgsakHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPG 174
Cdd:cd03226 94 LLGLKEL-------------DAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180
....*....|....*....|....*..
gi 921961068 175 IRKDMHQLLLALWRETRlTVFMVTHDL 201
Cdd:cd03226 161 NMERVGELIRELAAQGK-AVIVITHDY 186
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
17-176 |
1.41e-29 |
|
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: 110.60 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 17 VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQA----LA-AEPD---ASR----GVVFQRYSV 84
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAqASPReilALRrrtiGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 85 FPHLTVLDNVAlglelprSPLLGRlfGSAKHHAREQAAALLRKVGLDHAL-DKYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:COG4778 105 IPRVSALDVVA-------EPLLER--GVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLL 175
|
170
....*....|...
gi 921961068 164 LDEPFGALDPGIR 176
Cdd:COG4778 176 LDEPTASLDAANR 188
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-202 |
2.23e-29 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 112.75 E-value: 2.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRG-------VVFQR-Y-SVFPHLT 89
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllrqkiqIVFQNpYgSLNPRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 90 VLDNVAlglelprSPLLGRLFGSAKHHaREQAAALLRKVGL--DHAlDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEP 167
Cdd:PRK11308 111 VGQILE-------EPLLINTSLSAAER-REKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170 180 190
....*....|....*....|....*....|....*
gi 921961068 168 FGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:PRK11308 182 VSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLS 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-224 |
2.70e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 110.79 E-value: 2.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQA-----LAAEPDASR---- 75
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALSEAERrrll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ----GVVFQrysvfphltvldNVALGLELPRSPllG-----RLFGS-AKHHA--REQAAALLRKVGLDHA-LDKYPAQLS 142
Cdd:PRK11701 88 rtewGFVHQ------------HPRDGLRMQVSA--GgnigeRLMAVgARHYGdiRATAGDWLERVEIDAArIDDLPTTFS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 143 GGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVF-------- 214
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMkqgrvves 233
|
250
....*....|...
gi 921961068 215 ---DKVRVDPHAP 224
Cdd:PRK11701 234 gltDQVLDDPQHP 246
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-203 |
3.90e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 108.48 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGqilldgqALAAEPDASRGVVFQRYSV---FPhL 88
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSG-------TVRRAGGARVAYVPQRSEVpdsLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNVALGLeLPRSPLLGRLfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPF 168
Cdd:NF040873 73 TVRDLVAMGR-WARRGLWRRL----TRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|....*
gi 921961068 169 GALDPGIRKDMHQlLLALWRETRLTVFMVTHDLSE 203
Cdd:NF040873 148 TGLDAESRERIIA-LLAEEHARGATVVVVTHDLEL 181
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-223 |
4.46e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.07 E-value: 4.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--------GVVFQrysvFPHL-- 88
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNlkklrkkvSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 ---TVLDNVALGlelPRSpllgrlFGSAKHHAREQAAALLRKVGLDHAL-DKYPAQLSGGMQQRLAIAQALIMKPRVLLL 164
Cdd:PRK13641 99 fenTVLKDVEFG---PKN------FGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 165 DEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHA 223
Cdd:PRK13641 170 DEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHA 227
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-219 |
5.96e-29 |
|
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: 109.38 E-value: 5.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 21 GLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG----QETASKGQILLDGQALAAEPDASR--GVVFQ--RYSVFPHLTVLD 92
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGllppGLTQTSGEILLDGRPLLPLSIRGRhiATIMQnpRTAFNPLFTMGN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 93 NVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHA---LDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFG 169
Cdd:TIGR02770 84 HAIETL---------RSLGKLSKQARALILEALEAVGLPDPeevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 921961068 170 ALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
17-219 |
9.19e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 9.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 17 VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAE----PDASR--GVVFQ--RYSVFPHl 88
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvklSDIRKkvGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNVALGlelPRSpllgrlFGSAKHHAREQAAALLRKVGLDHA--LDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDE 166
Cdd:PRK13637 100 TIEKDIAFG---PIN------LGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 921961068 167 PFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK13637 171 PTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-200 |
2.01e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.47 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 6 VNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDgqalaaePDASRGVVFQRYSVF 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-------KGLRIGYLPQEPPLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 86 PHLTVLDNVALGL---------------ELPRSPLLGRLFGSAKHH--------AREQAAALLRKVGLDHA-LDKYPAQL 141
Cdd:COG0488 74 DDLTVLDTVLDGDaelraleaeleeleaKLAEPDEDLERLAELQEEfealggweAEARAEEILSGLGFPEEdLDRPVSEL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 142 SGGMQQRLAIAQALIMKPRVLLLDEPFGALD-PGIRkdmhqlllalWRETRL-----TVFMVTHD 200
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDlESIE----------WLEEFLknypgTVLVVSHD 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-219 |
2.43e-28 |
|
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: 107.45 E-value: 2.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQ----VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---G 76
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARrrlG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI 156
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEY---------FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
6-203 |
3.11e-28 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 107.10 E-value: 3.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 6 VNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGVVFQRYSVF 85
Cdd:TIGR03740 3 TKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLIESPPLY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 86 PHLTVLDN---VALGLELPRSPLLgrlfgsakhhareqaaALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVL 162
Cdd:TIGR03740 83 ENLTARENlkvHTTLLGLPDSRID----------------EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 163 LLDEPFGALDP-GIrKDMHQLLLALwRETRLTVFMVTHDLSE 203
Cdd:TIGR03740 147 ILDEPTNGLDPiGI-QELRELIRSF-PEQGITVILSSHILSE 186
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-202 |
3.37e-28 |
|
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: 107.31 E-value: 3.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 2 SFISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----G 76
Cdd:cd03254 1 GEIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrsmiG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHlTVLDNVALGLELPRspllgrlfgsakhhaREQAAALLRKVGLDHALDKYP-----------AQLSGGM 145
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGRPNAT---------------DEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGE 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRlTVFMVTHDLS 202
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGR-TSIIIAHRLS 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-218 |
4.28e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 109.54 E-value: 4.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQ 80
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARariGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:PRK13536 122 FDNLDLEFTVRENLLV---------FGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVR 218
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-216 |
5.69e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 107.96 E-value: 5.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 2 SFISVNNVWQRYGD--QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRL---LLGQETASKGQILLDGQALAAEP----D 72
Cdd:PRK13640 4 NIVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTvwdiR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 73 ASRGVVFQRY-SVFPHLTVLDNVALGLE---LPRSPLLgrlfgsakhharEQAAALLRKVGLDHALDKYPAQLSGGMQQR 148
Cdd:PRK13640 84 EKVGIVFQNPdNQFVGATVGDDVAFGLEnraVPRPEMI------------KIVRDVLADVGMLDYIDSEPANLSGGQKQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 149 LAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGfSLGTRLLVFDK 216
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDD 218
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-224 |
7.70e-28 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 106.84 E-value: 7.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQA-----LAAEPDASRGVV 78
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEAERRRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLD----NVALGLELPRSPL-LGrlfgsAKHHA--REQAAALLRKVGLDHA-LDKYPAQLSGGMQQRLA 150
Cdd:TIGR02323 84 MRTEWGFVHQNPRDglrmRVSAGANIGERLMaIG-----ARHYGniRATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 151 IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV----------- 219
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVvesgltdqvld 238
|
....*
gi 921961068 220 DPHAP 224
Cdd:TIGR02323 239 DPQHP 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-201 |
1.47e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.18 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKST----FLRLLlgqetASKGQILLDGQAL------AAEPDASR-GVVFQ-- 80
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLhnlnrrQLLPVRHRiQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALGLELPRSPLlgrlfgsAKHHAREQAAALLRKVGLDHAL-DKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:PRK15134 372 NSSLNPRLNVLQIIEEGLRVHQPTL-------SAAQREQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKP 444
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDL 486
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
19-199 |
1.70e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.75 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--------GVVFQrysvFPHL-- 88
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDikqirkkvGLVFQ----FPESql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 ---TVLDNVALGlelPRSpllgrlFGSAKHHAREQAAALLRKVGLDHAL-DKYPAQLSGGMQQRLAIAQALIMKPRVLLL 164
Cdd:PRK13649 99 feeTVLKDVAFG---PQN------FGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 921961068 165 DEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTH 199
Cdd:PRK13649 170 DEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTH 203
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-201 |
2.08e-27 |
|
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: 109.76 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDASRGVVFQRYSVF---PHL-- 88
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVS---SLDQDEVRRRVSVCaqdAHLfd 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 -TVLDNVALGlelprspllgrlfgsAKHHAREQAAALLRKVGLDHALDKYP-----------AQLSGGMQQRLAIAQALI 156
Cdd:TIGR02868 423 tTVRENLRLA---------------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALwrETRLTVFMVTHDL 201
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHHL 530
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-214 |
4.21e-27 |
|
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: 102.51 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepdasrgvvfqrys 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 vfphltvldnvalglelPRSPllgrlfgsakhhareqAAALLRKVGLDHaldkypaQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:cd03216 66 -----------------FASP----------------RDARRAGIAMVY-------QLSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 164 LDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVF 214
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVL 155
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
14-200 |
5.67e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 102.89 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEpdaSRGVVFQRYSVFPHL----- 88
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYS---RKGLLERRQRVGLVFqdpdd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 -----TVLDNVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:TIGR01166 80 qlfaaDVDQDVAFGP---------LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 921961068 164 LDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHD 200
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRL-RAEGMTVVISTHD 186
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-212 |
2.84e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 103.14 E-value: 2.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 13 YGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDG---QALAAEPDASR-GVVFQRYSVFPHL 88
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiQHYASKEVARRiGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNVALGlELPRSPLLGRLfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPF 168
Cdd:PRK10253 97 TVQELVARG-RYPHQPLFTRW----RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 921961068 169 GALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLL 212
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLI 215
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-207 |
3.06e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALaaePDASRG---- 76
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRSrlyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 ------VVFQRYSVFPHLTVLDNVALGL----ELPrSPLLgrlfgsakhhaREQAAALLRKVGLDHALDKYPAQLSGGMQ 146
Cdd:PRK11831 82 vrkrmsMLFQSGALFTDMNVFDNVAYPLrehtQLP-APLL-----------HSTVMMKLEAVGLRGAAKLMPSELSGGMA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSL 207
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSI 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-201 |
3.89e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 106.45 E-value: 3.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQ--VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-RG---V 77
Cdd:PRK11160 339 LTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQaisV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHlTVLDNVALglelprspllgrlfgsAKHHAR-EQAAALLRKVGLDHALDKYPA----------QLSGGMQ 146
Cdd:PRK11160 419 VSQRVHLFSA-TLRDNLLL----------------AAPNASdEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQ 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDpgirKDMHQLLLALWRE--TRLTVFMVTHDL 201
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLD----AETERQILELLAEhaQNKTVLMITHRL 534
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
18-219 |
4.55e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 103.24 E-value: 4.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQI--LLDGQALAAEPDASR-------------------- 75
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEkvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ------GVVFQ--RYSVFPHlTVLDNVALGlelPRSpllgrlFGSAKHHAREQAAALLRKVGLDHA-LDKYPAQLSGGMQ 146
Cdd:PRK13651 102 eirrrvGVVFQfaEYQLFEQ-TIEKDIIFG---PVS------MGVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQK 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKI 243
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
4-219 |
9.56e-26 |
|
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: 101.02 E-value: 9.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYG--DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA-AEPDASR---GV 77
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlADPAWLRrqvGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFpHLTVLDNVALGLElprSPLLGRLFGSAKhhaREQAAALLRKV--GLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:cd03252 81 VLQENVLF-NRSIRDNIALADP---GMSMERVIEAAK---LAGAHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 156 IMKPRVLLLDEPFGALD----PGIRKDMHQLLLAlwretrLTVFMVTHDLSEgFSLGTRLLVFDKVRV 219
Cdd:cd03252 154 IHNPRILIFDEATSALDyeseHAIMRNMHDICAG------RTVIIIAHRLST-VKNADRIIVMEKGRI 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
7-203 |
1.54e-25 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 100.17 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 7 NNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA-EPDASRGVV---FQRY 82
Cdd:PRK10247 11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVsycAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 83 SVFPHlTVLDNVALGLELPRspllgrlfgsaKHHAREQAAALLRKVGL-DHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRN-----------QQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSE 203
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-202 |
1.67e-25 |
|
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: 104.29 E-value: 1.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQ-VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA-AEPDASR---GVV 78
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdADADSWRdqiAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHlTVLDNVALGLelprspllgrlfGSAKHHAREQA---AALLRKV-----GLDHALDKYPAQLSGGMQQRLA 150
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLAR------------PDASDAEIREAlerAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 921961068 151 IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRlTVFMVTHDLS 202
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGR-TVLLVTHRLA 518
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
10-245 |
4.42e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.17 E-value: 4.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 10 WQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEP--DASR--GVVFQRY-SV 84
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENvwNLRRkiGMVFQNPdNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 85 FPHLTVLDNVALGLE---LPRSPLLGRLfgsakhhareqAAALLRKVGLDHAlDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:PRK13642 94 FVGATVEDDVAFGMEnqgIPREEMIKRV-----------DEALLAVNMLDFK-TREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 162 LLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHAPGAYGA------RITYDI 235
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAtsedmvEIGLDV 241
|
250
....*....|
gi 921961068 236 PLNSERRKAL 245
Cdd:PRK13642 242 PFSSNLMKDL 251
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-199 |
4.64e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 103.67 E-value: 4.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQRYSVFPHL 88
Cdd:NF033858 275 RFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRrrvGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNvalgLELPrspllGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPF 168
Cdd:NF033858 355 TVRQN----LELH-----ARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190
....*....|....*....|....*....|.
gi 921961068 169 GALDPGIRKDMHQLLLALWRETRLTVFMVTH 199
Cdd:NF033858 426 SGVDPVARDMFWRLLIELSREDGVTIFISTH 456
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-219 |
8.73e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.41 E-value: 8.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA-----SR 75
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkimreAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVAlglelprsplLGRLFGSakhhaREQAAALLRKV-GLDHALDKYPAQ----LSGGMQQRLA 150
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLA----------MGGFFAE-----RDQFQERIKWVyELFPRLHERRIQragtMSGGEQQMLA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 151 IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK11614 148 IGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-201 |
9.25e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 98.93 E-value: 9.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 2 SFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASK---------GQILLDGQALAAEPD 72
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 73 ASR---GVVFQRYSVFPHLTVLDNVALGlELPRSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRL 149
Cdd:PRK09984 83 KSRantGYIFQQFNLVNRLSVLENVLIG-ALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 921961068 150 AIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQV 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
22-199 |
1.16e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 99.42 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 22 LNLQVDEGEFCTLVGTSGCGKSTFLRLLLG-----QETASKGQILLDGQALAAEPDASR---GVVFQrysvFPHL----- 88
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRkkvGVVFQ----FPESqlfee 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNVALGlelPRSpllgrlFGSAKHHAREQAAALLRKVGLDHAL-DKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEP 167
Cdd:PRK13643 101 TVLKDVAFG---PQN------FGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
170 180 190
....*....|....*....|....*....|..
gi 921961068 168 FGALDPGIRKDMHQLLLALwRETRLTVFMVTH 199
Cdd:PRK13643 172 TAGLDPKARIEMMQLFESI-HQSGQTVVLVTH 202
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
4-172 |
1.32e-24 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 98.00 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY---GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA-EPDASR---G 76
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRsqiG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRysvfPHL---TVLDNVALGLElprspllgrlfgSAKHHAREQAAallRKVGLDHALDKYP-----------AQLS 142
Cdd:cd03249 81 LVSQE----PVLfdgTIAENIRYGKP------------DATDEEVEEAA---KKANIHDFIMSLPdgydtlvgergSQLS 141
|
170 180 190
....*....|....*....|....*....|
gi 921961068 143 GGMQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:cd03249 142 GGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-201 |
1.51e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALaaepDASR------- 75
Cdd:PRK13636 6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI----DYSRkglmklr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 ---GVVFQR--YSVFPhLTVLDNVALG---LELPrspllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQ 147
Cdd:PRK13636 82 esvGMVFQDpdNQLFS-ASVYQDVSFGavnLKLP------------EDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDI 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-203 |
1.53e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 2 SFISVNNV-WQRYGDQ-VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA----EPDASR 75
Cdd:PRK13648 6 SIIVFKNVsFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDdnfeKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQR-YSVFPHLTVLDNVALGLELPRSPllgrlfgSAKHHarEQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQA 154
Cdd:PRK13648 86 GIVFQNpDNQFVGSIVKYDVAFGLENHAVP-------YDEMH--RRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 921961068 155 LIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSE 203
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSE 205
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
8-219 |
2.22e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 99.56 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 8 NVWQRYGDqvvlegLNLQVDE----GEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDASRGV------ 77
Cdd:PRK11144 5 NFKQQLGD------LCLTVNLtlpaQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF---DAEKGIclppek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 -----VFQRYSVFPHLTVLDNVALGLelprspllgrlfgsaKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:PRK11144 76 rrigyVFQDARLFPHYKVRGNLRYGM---------------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIG 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK11144 141 RALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKV 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-199 |
2.76e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.04 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLdgqalaaePDASRgVVF--QR-YsvFPHLTVL 91
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR--------PAGAR-VLFlpQRpY--LPLGTLR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 92 DNVALglelPRSPllgrlfgsaKHHAREQAAALLRKVGLDHALDKY------PAQLSGGMQQRLAIAQALIMKPRVLLLD 165
Cdd:COG4178 444 EALLY----PATA---------EAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190
....*....|....*....|....*....|....
gi 921961068 166 EPFGALDPGIRKDMHQLLLALWRETrlTVFMVTH 199
Cdd:COG4178 511 EATSALDEENEAALYQLLREELPGT--TVISVGH 542
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-219 |
3.14e-24 |
|
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: 96.50 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQ--VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDG----QALAAEPDASRGV 77
Cdd:cd03245 3 IEFRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirQLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFpHLTVLDNVALGLelprspllgrlfGSAKHHAREQAAALLrkvGLDHALDKYP-----------AQLSGGMQ 146
Cdd:cd03245 83 VPQDVTLF-YGTLRDNITLGA------------PLADDERILRAAELA---GVTDFVNKHPngldlqigergRGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDPGI-RKDMHQllLALWRETRlTVFMVTHDLSEgFSLGTRLLVFDKVRV 219
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMDMNSeERLKER--LRQLLGDK-TLIIITHRPSL-LDLVDRIIVMDSGRI 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-201 |
4.37e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 99.53 E-value: 4.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAepdASRGVVFQ 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEA---LSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLD---NVALGLELPRSPLLGRL--FGSAKHHAREQAaalLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:PRK09536 78 RVASVPQDTSLSfefDVRQVVEMGRTPHRSRFdtWTETDRAAVERA---MERTGVAQFADRPVTSLSGGERQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 921961068 156 IMKPRVLLLDEPFGALDPGirkdmHQL-LLALWR---ETRLTVFMVTHDL 201
Cdd:PRK09536 155 AQATPVLLLDEPTASLDIN-----HQVrTLELVRrlvDDGKTAVAAIHDL 199
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-219 |
5.42e-24 |
|
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: 96.06 E-value: 5.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQaLAAEPDAsrGVVFQrysvfPHLTVL 91
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLLGL--GGGFN-----PELTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 92 DNVAlglelprspLLGRLFGsakhHAREQAAALLRKV----GLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEP 167
Cdd:cd03220 103 ENIY---------LNGRLLG----LSRKEIDEKIDEIiefsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 921961068 168 FGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-200 |
6.22e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 6.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD-QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA------SRG 76
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSllevrkTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRY--SVF-PhlTVLDNVALGlelprsPLLgrlFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQ 153
Cdd:PRK13639 82 IVFQNPddQLFaP--TVEEDVAFG------PLN---LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 921961068 154 ALIMKPRVLLLDEPFGALDP-GIRKDMhQLLLALWRETrLTVFMVTHD 200
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPmGASQIM-KLLYDLNKEG-ITIIISTHD 196
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-215 |
7.40e-24 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 94.30 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQ--VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVV 78
Cdd:cd03247 1 LSINNVSFSYPEQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSsliSVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRysvfPHL---TVLDNvalglelprsplLGRlfgsakhhareqaaallrkvgldhaldkypaQLSGGMQQRLAIAQAL 155
Cdd:cd03247 81 NQR----PYLfdtTLRNN------------LGR-------------------------------RFSGGERQRLALARIL 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDLSeGFSLGTRLLVFD 215
Cdd:cd03247 114 LQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLT-GIEHMDKILFLE 170
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
4-203 |
7.92e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.24 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA--SRGVVF-- 79
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlARRLALlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGlelpRSPLL---GRLfgSAKHHAREQAAalLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI 156
Cdd:PRK11231 83 QHHLTPEGITVRELVAYG----RSPWLslwGRL--SAEDNARVNQA--MEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 157 MKPRVLLLDEPFGALDPGirkdmHQL-LLALWRETRL---TVFMVTHDLSE 203
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDIN-----HQVeLMRLMRELNTqgkTVVTVLHDLNQ 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-199 |
9.19e-24 |
|
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: 93.82 E-value: 9.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD--QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA-EPDASR---GV 77
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGdhvGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHlTVLDNValglelprspllgrlfgsakhhareqaaallrkvgldhaldkypaqLSGGMQQRLAIAQALIM 157
Cdd:cd03246 81 LPQDDELFSG-SIAENI----------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTH 199
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAH 154
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-219 |
9.28e-24 |
|
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: 100.09 E-value: 9.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 9 VWQRYGDQVVlEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVFQRYSVF 85
Cdd:TIGR01257 937 IFEPSGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqslGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 86 PHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLD 165
Cdd:TIGR01257 1016 HHLTVAEHILF---------YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 921961068 166 EPFGALDPGIRKDMHQLLLAlWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLK-YRSGR-TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-200 |
1.16e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.88 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR----------GVVFQRYSV 84
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQidaiklrkevGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 85 FPHLTVLDNVALglelprsPLLGRLFgSAKHHAREQAAALLRKVGL----DHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:PRK14246 102 FPHLSIYDNIAY-------PLKSHGI-KEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALWREtrLTVFMVTHD 200
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHN 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-219 |
1.37e-23 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 93.65 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYgdqvVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVF-- 79
Cdd:cd03215 6 EVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiraGIAYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 ---QRYSVFPHLTVLDNVALglelprspllgrlfgsakhhareqaaallrkvgldhaldkyPAQLSGGMQQRLAIAQALI 156
Cdd:cd03215 82 edrKREGLVLDLSVAENIAL-----------------------------------------SSLLSGGNQQKVVLARWLA 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03215 121 RDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-224 |
1.61e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 95.54 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 13 YGDQVVLEGLNLQVDEGEFCTLVGTSGCGKS----TFLRLLLGQETASKGQILLDGQALAaePDASRGVvfqrysvfphl 88
Cdd:PRK10418 13 QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA--PCALRGR----------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 tvldNVALGLELPRS---PLLgrlfgSAKHHARE------------QAAALLRKVGLDHA---LDKYPAQLSGGMQQRLA 150
Cdd:PRK10418 80 ----KIATIMQNPRSafnPLH-----TMHTHAREtclalgkpaddaTLTAALEAVGLENAarvLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 151 IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHAP 224
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGD 224
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
5-202 |
2.54e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 95.24 E-value: 2.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS--RGVVF--Q 80
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfaRKVAYlpQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALGlELPRSPLLGRlFGSAKHHAREQAAALlrkVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:PRK10575 93 QLPAAEGMTVRELVAIG-RYPWHGALGR-FGAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDIN 209
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
2.74e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.19 E-value: 2.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD----ASRGVV 78
Cdd:PRK13647 5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkwvrSKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRY--SVFPhLTVLDNVALGlelPRSpllgrlFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALI 156
Cdd:PRK13647 85 FQDPddQVFS-STVWDDVAFG---PVN------MGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 157 MKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRV 216
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-218 |
2.83e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.84 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL-----LGQETASKGQILLDGQALAA------EPD 72
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndLNPEVTITGSIVYNGHNIYSprtdtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 73 ASRGVVFQRYSVFPhLTVLDNVALGLelprspllgRLFGSAKHHAREQA-------AALLRKVGlDHALDKYPAqLSGGM 145
Cdd:PRK14239 86 KEIGMVFQQPNPFP-MSIYENVVYGL---------RLKGIKDKQVLDEAvekslkgASIWDEVK-DRLHDSALG-LSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwrETRLTVFMVTHDLSE--------GFSLGTRLLVFDKV 217
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQasrisdrtGFFLDGDLIEYNDT 231
|
.
gi 921961068 218 R 218
Cdd:PRK14239 232 K 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-219 |
3.19e-23 |
|
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: 94.07 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 3 FISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA------------- 69
Cdd:cd03248 14 FQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyehkylhskvslv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 70 --EPdasrgVVFQRysvfphlTVLDNVALGLelPRSPLLGRLFGSAKHHAREQAAALlrKVGLDHALDKYPAQLSGGMQQ 147
Cdd:cd03248 94 gqEP-----VLFAR-------SLQDNIAYGL--QSCSFECVKEAAQKAHAHSFISEL--ASGYDTEVGEKGSQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLAlWRETRlTVFMVTHDLSEgFSLGTRLLVFDKVRV 219
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERR-TVLVIAHRLST-VERADQILVLDGGRI 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-224 |
5.30e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 94.39 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 13 YGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL--LGQETAS---KGQILLDGQALAAEPDASR-----GVVFQRY 82
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrMNDKVSGyrySGDVLLGGRSIFNYRDVLEfrrrvGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 83 SVFPhLTVLDNVALGLE----LPRSPLLGrlfgsakhhareQAAALLRKVGLDHA----LDKYPAQLSGGMQQRLAIAQA 154
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRahklVPRKEFRG------------VAQARLTEVGLWDAvkdrLSDSPFRLSGGQQQLLCLART 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 155 LIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwrETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHAP 224
Cdd:PRK14271 178 LAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-203 |
1.26e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.31 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 13 YGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLL-----LGQETASKGQILLDGQALAA---EPDASR---GVVFQR 81
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrlndLIPGFRVEGKVTFHGKNLYApdvDPVEVRrriGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHlTVLDNVALGlelprspllGRLFGsAKHHAREQAAALLRKVGL-DHALDKYPAQ---LSGGMQQRLAIAQALIM 157
Cdd:PRK14243 100 PNPFPK-SIYDNIAYG---------ARING-YKGDMDELVERSLRQAALwDEVKDKLKQSglsLSGGQQQRLCIARAIAV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 921961068 158 KPRVLLLDEPFGALDP----GIRKDMHQLllalwrETRLTVFMVTHDLSE 203
Cdd:PRK14243 169 QPEVILMDEPCSALDPistlRIEELMHEL------KEQYTIIIVTHNMQQ 212
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-210 |
1.32e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEP---DASRGV 77
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VF--QRYSVFPHLTVLDNVALGLELpRSPLlgrlfgsAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL 155
Cdd:PRK10895 81 GYlpQEASIFRRLSVYDNLMAVLQI-RDDL-------SAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTR 210
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCER 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-202 |
6.52e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.00 E-value: 6.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYGDQV--VLEGLNLQVDEGEFCTLVGTSGCGKS----TFLRLLLGQETA-SKGQILLDGQALAAEPDAS-RGV------ 77
Cdd:PRK15134 16 RQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQTlRGVrgnkia 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 -VFQR--YSVFPHLTVLDNVALGLELPRspllgrlfGSAKHHAREQAAALLRKVGLDHA---LDKYPAQLSGGMQQRLAI 151
Cdd:PRK15134 96 mIFQEpmVSLNPLHTLEKQLYEVLSLHR--------GMRREAARGEILNCLDRVGIRQAakrLTDYPHQLSGGERQRVMI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLS 218
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-201 |
9.44e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 90.53 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFL----RLLlgqeTASKGQILLDGQALAAEPDAsrgVVF 79
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLsmisRLL----PPDSGEVLVDGLDVATTPSR---ELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVF---PH----LTVLDNVALGlelpRSPL-LGRLfGSAKHHAREQAAALLrkvGLDHALDKYPAQLSGGMQQRLAI 151
Cdd:COG4604 75 KRLAILrqeNHinsrLTVRELVAFG----RFPYsKGRL-TAEDREIIDEAIAYL---DLEDLADRYLDELSGGQRQRAFI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDI 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
29-247 |
1.65e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.00 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 29 GEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-----RGV--VFQR--YSVFPHLTVLDNVAlgle 99
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIqfIFQDpyASLDPRQTVGDSIM---- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 100 lprSPLL--GRLFGSAkhhAREQAAALLRKVGL--DHALdKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGI 175
Cdd:PRK10261 426 ---EPLRvhGLLPGKA---AAARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 176 RKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVDPHAPgaygARITYDIPLNSERRKALAA 247
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGP----RRAVFENPQHPYTRKLMAA 566
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.96e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 90.25 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA----EPDASR 75
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKenirEVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRY--SVFPHlTVLDNVALGlelprsPL-LGRLFGSAKHHAREqaaaLLRKVGLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:PRK13652 81 GLVFQNPddQIFSP-TVEQDIAFG------PInLGLDEETVAHRVSS----ALHMLGLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-219 |
4.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.38 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD------QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD----- 72
Cdd:PRK13633 5 IKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwdir 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 73 ASRGVVFQRysvfPH-----LTVLDNVALGLELprspllgrlFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQ 147
Cdd:PRK13633 85 NKAGMVFQN----PDnqivaTIVEEDVAFGPEN---------LGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 148 RLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSlGTRLLVFDKVRV 219
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKV 222
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-202 |
5.11e-21 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 91.70 E-value: 5.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS--RGV-VF 79
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlrQGVaMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGLELPRSPLLGRLfgsakhhAREQAAALLRKV--GLDHALDKYPAQLSGGMQQRLAIAQALIM 157
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRDISEEQVWQAL-------ETVQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVfmVTHDLS 202
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALAAVREHTTLVV--IAHRLS 536
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-199 |
6.02e-21 |
|
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: 91.40 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQET--ASKGQIL-----------LDGQALAAE 70
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 71 P-------------------DASR-------GVVFQR-YSVFPHLTVLDNVALGLELprspllgrlFGSAKHHAREQAAA 123
Cdd:TIGR03269 81 PcpvcggtlepeevdfwnlsDKLRrrirkriAIMLQRtFALYGDDTVLDNVLEALEE---------IGYEGKEAVGRAVD 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 124 LLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTH 199
Cdd:TIGR03269 152 LIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
5-219 |
1.67e-20 |
|
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: 87.00 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQR-YGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVF- 79
Cdd:cd03267 22 SLKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLrriGVVFg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:cd03267 102 QKTQLWWDLPVIDSFYL---------LAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 160 RVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-202 |
1.77e-20 |
|
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: 85.98 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNV---WQRYGDQ--VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGqalaaepdaSRGVV 78
Cdd:cd03250 1 ISVEDAsftWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG---------SIAYV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQrysvFPHL---TVLDNValglelprspllgrLFGSAKHHAREQAAalLRKVGLDHALDKYPAQ-----------LSGG 144
Cdd:cd03250 72 SQ----EPWIqngTIRENI--------------LFGKPFDEERYEKV--IKACALEPDLEILPDGdlteigekginLSGG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 145 MQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKD-MHQLLLALWRETRlTVFMVTHDLS 202
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHiFENCILGLLLNNK-TRILVTHQLQ 189
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-202 |
1.95e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 86.52 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV--VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-R---GV 77
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlRrqiGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFpHLTVLDNVALGlelprspllgrlfgsaKHHA-REQAAALLRKVGLDHALDKYP-----------AQLSGGM 145
Cdd:cd03251 81 VSQDVFLF-NDTVAENIAYG----------------RPGAtREEVEEAARAANAHEFIMELPegydtvigergVKLSGGQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALDPG----IRKDMHQLLlalwrETRlTVFMVTHDLS 202
Cdd:cd03251 144 RQRIAIARALLKDPPILILDEATSALDTEserlVQAALERLM-----KNR-TTFVIAHRLS 198
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-213 |
1.99e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.84 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 3 FISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQA-------LAAEpdASR 75
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkldhkLAAQ--LGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGlELPRSPLLG-RLFGSAKhhAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQA 154
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIG-RHLTKKVCGvNIIDWRE--MRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 155 LIMKPRVLLLDEPFGALdpgIRKDMHQLLL---ALWRETRLTVFmVTHDLSEGFSLGTRLLV 213
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL---TNKEVDYLFLimnQLRKEGTAIVY-ISHKLAEIRRICDRYTV 217
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
4-203 |
2.46e-20 |
|
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: 86.52 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD-QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA-AEPDASR---GVV 78
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIReVTLDSLRraiGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFpHLTVLDNVAlglelprsplLGRLfgSAKHHAREQAAallrKVGLDHAL-----DKYPAQ-------LSGGMQ 146
Cdd:cd03253 81 PQDTVLF-NDTIGYNIR----------YGRP--DATDEEVIEAA----KAAQIHDKimrfpDGYDTIvgerglkLSGGEK 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwrETRLTVFMVTHDLSE 203
Cdd:cd03253 144 QRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLST 198
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
18-217 |
3.55e-20 |
|
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: 84.91 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQ--ETASKGQILLDGQALaaEPDASR---GVVFQRYSVFPHLTVLD 92
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL--DKRSFRkiiGYVPQDDILHPTLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 93 NVALglelprspllgrlfgsakhhareqaAALLRkvgldhaldkypaQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:cd03213 102 TLMF-------------------------AAKLR-------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 173 PGIRKDMHQLLLALWRETRlTVFMVTHDLS-EGFSLgtrllvFDKV 217
Cdd:cd03213 144 SSSALQVMSLLRRLADTGR-TIICSIHQPSsEIFEL------FDKL 182
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
18-201 |
3.69e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 87.65 E-value: 3.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG------QETASKgqILLDGQALAAEPDASR--------GVVFQRys 83
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkdnwHVTADR--FRWNGIDLLKLSPRERrkiigreiAMIFQE-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 vfPhLTVLD-NVALGLEL----PRSPLLGRlFGSAKHHAREQAAALLRKVGL-DHA--LDKYPAQLSGGMQQRLAIAQAL 155
Cdd:COG4170 98 --P-SSCLDpSAKIGDQLieaiPSWTFKGK-WWQRFKWRKKRAIELLHRVGIkDHKdiMNSYPHELTEGECQKVMIAMAI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDL 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-202 |
3.76e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.29 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 11 QRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQ--ALAAepdasRGVVFQrysvfPHL 88
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsALLE-----LGAGFH-----PEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNVALGlelprspllGRLFGsakhHAREQAAALLRKV----GLDHALDK----YpaqlSGGMQQRLAIAQALIMKPR 160
Cdd:COG1134 104 TGRENIYLN---------GRLLG----LSRKEIDEKFDEIvefaELGDFIDQpvktY----SSGMRARLAFAVATAVDPD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLS 202
Cdd:COG1134 167 ILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMG 207
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-202 |
5.03e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 87.10 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVV----LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG----QETASKGQILLDGQALAAEPD 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGlidyPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 73 ASR--------GVVFQ--RYSVFPHLTVLDNVALGLELPRspllgrlfGSAKHHAREQAAALLRKVGL-DHA--LDKYPA 139
Cdd:PRK11022 81 KERrnlvgaevAMIFQdpMTSLNPCYTVGFQIMEAIKVHQ--------GGNKKTRRQRAIDLLNQVGIpDPAsrLDVYPH 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 140 QLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLA 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
5.16e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.21 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 17 VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR--------------------G 76
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHElitnpyskkiknfkelrrrvS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQ--RYSVFPHlTVLDNVALGlelprsPLLgrlFGSAKHHAREQAAALLRKVGLDHA-LDKYPAQLSGGMQQRLAIAQ 153
Cdd:PRK13631 120 MVFQfpEYQLFKD-TIEKDIMFG------PVA---LGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 154 ALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDK 251
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
15-202 |
7.34e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 7.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAL---------------AAEPdasrgVVF 79
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvqydhhylhrqvalvGQEP-----VLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRysvfphlTVLDNVALGLElpRSPLLGRLFGSAKHHAREQAAALLRkvGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:TIGR00958 568 SG-------SVRENIAYGLT--DTPDEEIMAAAKAANAHDFIMEFPN--GYDTEVGEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 921961068 160 RVLLLDEPFGALDPGIrkdmhQLLLALWRETR-LTVFMVTHDLS 202
Cdd:TIGR00958 637 RVLILDEATSALDAEC-----EQLLQESRSRAsRTVLLIAHRLS 675
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-219 |
1.48e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 85.44 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSF---ISVNNVWQRYGDQV-----VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAE-- 70
Cdd:PRK13645 1 FDFskdIILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 71 -----PDASR--GVVFQ--RYSVFPHlTVLDNVALGlelprsPLLgrlFGSAKHHAREQAAALLRKVGL-DHALDKYPAQ 140
Cdd:PRK13645 81 kikevKRLRKeiGLVFQfpEYQLFQE-TIEKDIAFG------PVN---LGENKQEAYKKVPELLKLVQLpEDYVKRSPFE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 141 LSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-216 |
2.14e-19 |
|
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: 83.86 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFL----RLLLGQETASkGQILLDGQALaaEPDASR---GVVFQRYSVFPHLTV 90
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLdaisGRVEGGGTTS-GQILFNGQPR--KPDQFQkcvAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 91 LDNVALGLELPrsplLGRLFGSAKHHAREqAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGA 170
Cdd:cd03234 99 RETLTYTAILR----LPRKSSDAIRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 171 LDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSS 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
14-201 |
2.48e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.55 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKS-TFLRL--LLGQETASKGQILLDGQALAAEPDAS----RG----VVFQ-- 80
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREILNLPEKElnklRAeqisMIFQdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALGLELPRspllgrlfGSAKHHAREQAAALLRKVGLDHALDK---YPAQLSGGMQQRLAIAQALIM 157
Cdd:PRK09473 107 MTSLNPYMRVGEQLMEVLMLHK--------GMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLC 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 921961068 158 KPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:PRK09473 179 RPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-227 |
2.77e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 86.27 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLdGQALaaepdaSRGVVFQRYS 83
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------KIGYFDQHQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VF-PHLTVLDNVALGL----ELPRSPLLGR-LFGSAKHHareqaaallRKVGldhaldkypaQLSGGMQQRLAIAQALIM 157
Cdd:COG0488 389 ELdPDKTVLDELRDGApggtEQEVRGYLGRfLFSGDDAF---------KPVG----------VLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 158 KPRVLLLDEPFGALDPgirkDMHQLLLALWRETRLTVFMVTHDlsEGF--SLGTRLLVFDKVRVDPHaPGAY 227
Cdd:COG0488 450 PPNVLLLDEPTNHLDI----ETLEALEEALDDFPGTVLLVSHD--RYFldRVATRILEFEDGGVREY-PGGY 514
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-214 |
4.16e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQR-YGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVF- 79
Cdd:COG3845 259 EVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrrlGVAYi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 ----QRYSVFPHLTVLDNVALGlELPRSPLLGRLF---GSAKHHAREQAAAL-LRKVGLDHALdkypAQLSGGMQQRLAI 151
Cdd:COG3845 339 pedrLGRGLVPDMSVAENLILG-RYRRPPFSRGGFldrKAIRAFAEELIEEFdVRTPGPDTPA----RSLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 921961068 152 AQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLVF 214
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVM 475
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-171 |
1.08e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.60 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 7 NNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG--QETASKGQILLDGQALAAE--PDASR-GVV--F 79
Cdd:PRK13549 9 KNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEGEELQASniRDTERaGIAiiH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVFPHLTVLDNVALGLELPRSpllGRLFGSAKHHareQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKP 159
Cdd:PRK13549 89 QELALVKELSVLENIFLGNEITPG---GIMDYDAMYL---RAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170
....*....|..
gi 921961068 160 RVLLLDEPFGAL 171
Cdd:PRK13549 163 RLLILDEPTASL 174
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-182 |
1.68e-18 |
|
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: 80.87 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDA-SRGVVF--Q 80
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYlgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVLDNVALglelprsplLGRLFGSAkhhaREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPR 160
Cdd:TIGR01189 81 LPGLKPELSALENLHF---------WAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147
|
170 180
....*....|....*....|...
gi 921961068 161 VLLLDEPFGALDP-GIRKDMHQL 182
Cdd:TIGR01189 148 LWILDEPTTALDKaGVALLAGLL 170
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-230 |
1.78e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.36 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAepdASRGV------ 77
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY---SKRGLlalrqq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 ---VFQRYSVFPHLTVLD-NVALGLelprspllgRLFGSAKHHAREQAAALLRKVGLDHaLDKYPAQ-LSGGMQQRLAIA 152
Cdd:PRK13638 79 vatVFQDPEQQIFYTDIDsDIAFSL---------RNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRVDPH-APGAYGAR 230
Cdd:PRK13638 149 GALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHgAPGEVFAC 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-214 |
2.43e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 2.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGE---FCTLVGtsgCGKSTFLRLLLGQETASKGQILLDGQALAAE--PDA-SRGVVF-----QRYSVFP 86
Cdd:COG1129 267 VVRDVSFSVRAGEilgIAGLVG---AGRTELARALFGADPADSGEIRLDGKPVRIRspRDAiRAGIAYvpedrKGEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 87 HLTVLDNVALGLeLPRSPLLGRLfgsakHHAREQAAA--LLRKVGLdhaldKYP------AQLSGGMQQRLAIAQALIMK 158
Cdd:COG1129 344 DLSIRENITLAS-LDRLSRGGLL-----DRRRERALAeeYIKRLRI-----KTPspeqpvGNLSGGNQQKVVLAKWLATD 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALWREtRLTVFMVTHDLSEGFSLGTRLLVF 214
Cdd:COG1129 413 PKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVM 467
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-203 |
4.03e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 83.36 E-value: 4.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQeTASKGQILLDGQALAA-EPDASR---GVVFQRySVFPHLTV 90
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRElDPESWRkhlSWVGQN-PQLPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 91 LDNVALGlelprspllgrlfgsaKHHAR-EQAAALLRKV-----------GLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:PRK11174 440 RDNVLLG----------------NPDASdEQLQQALENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQP 503
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 159 PRVLLLDEPFGALDpgiRKDMHQLLLALWRETR-LTVFMVTHDLSE 203
Cdd:PRK11174 504 CQLLLLDEPTASLD---AHSEQLVMQALNAASRrQTTLMVTHQLED 546
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-200 |
4.63e-18 |
|
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: 77.87 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQIlldgqalaaepdasrgvvfqrys 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 vfphlTVLDNVALGlelprspllgrlfgsakhhareqaaallrkvgldhaldkYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:cd03221 58 -----TWGSTVKIG---------------------------------------YFEQLSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190
....*....|....*....|....*....|....*...
gi 921961068 164 LDEPFGALD-PGIrkdmhQLLLALWRETRLTVFMVTHD 200
Cdd:cd03221 94 LDEPTNHLDlESI-----EALEEALKEYPGTVILVSHD 126
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-230 |
6.77e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 82.49 E-value: 6.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGVVF----QRYSVFPHlT 89
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIgylpQDVELFDG-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 90 VLDNVAlglelpRspllgrlFGSAKHHAREQAAallRKVGLDHALDKYP-----------AQLSGGMQQRLAIAQALIMK 158
Cdd:COG4618 422 IAENIA------R-------FGDADPEKVVAAA---KLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSeGFSLGTRLLVFDKVRVDphapgAYGAR 230
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQ-----AFGPR 550
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-202 |
7.29e-18 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 82.46 E-value: 7.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYG--DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA----AEPDASRGV 77
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdytlASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHlTVLDNVALGLelprspllGRLFGSAKHHAREQAAALLRKV-----GLDHALDKYPAQLSGGMQQRLAIA 152
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGR--------TEQADRAEIERALAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAIA 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDLS 202
Cdd:TIGR02203 482 RALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLS 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-203 |
1.68e-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: 81.41 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG--QETASKGQILLDGQALAAE--PDASRG--- 76
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASniRDTERAgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 VVFQRYSVFPHLTVLDNVALGLELPRSPllGRLFGSAKHHareQAAALLRKVGLDHALDKYP-AQLSGGMQQRLAIAQAL 155
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPG--GRMAYNAMYL---RAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 156 IMKPRVLLLDEPFGALdpgIRKDMhQLLLALWRETR---LTVFMVTHDLSE 203
Cdd:TIGR02633 157 NKQARLLILDEPSSSL---TEKET-EILLDIIRDLKahgVACVYISHKLNE 203
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-199 |
1.70e-17 |
|
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: 77.95 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQE--TASKGQILLDGQAL-AAEPD--ASRGV- 77
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDItDLPPEerARLGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 -VFQRYSVFPHLTVLDnvalglelprspllgrlfgsakhhareqaaaLLRKVGldhaldkypAQLSGGMQQRLAIAQALI 156
Cdd:cd03217 81 lAFQYPPEIPGVKNAD-------------------------------FLRYVN---------EGFSGGEKKRNEILQLLL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 157 MKPRVLLLDEPfgalDPGIRKDMHQLL---LALWRETRLTVFMVTH 199
Cdd:cd03217 121 LEPDLAILDEP----DSGLDIDALRLVaevINKLREEGKSVLIITH 162
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-212 |
2.31e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.79 E-value: 2.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEG-LNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAE-PDASR---GVV 78
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRklfSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLtvldnvalglelprspllgrLFGSAKHHAREQAAALLRKVGLDHALDK-----YPAQLSGGMQQRLAIAQ 153
Cdd:PRK10522 403 FTDFHLFDQL--------------------LGPEGKPANPALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLL 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 154 ALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDlSEGFSLGTRLL 212
Cdd:PRK10522 463 ALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLL 520
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-219 |
3.00e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.88 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDASR------- 75
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTG---DFSKlqgirkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 -GVVFQR-YSVFPHLTVLDNVALGLE---LPRSPLlgrlfgsakhhaREQAAALLRKVGLDHALDKYPAQLSGGMQQRLA 150
Cdd:PRK13644 79 vGIVFQNpETQFVGRTVEEDLAFGPEnlcLPPIEI------------RKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 151 IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEgFSLGTRLLVFDKVRV 219
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEE-LHDADRIIVMDRGKI 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-203 |
3.17e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA-AEPDASRG----VV 78
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArLTPAKAHQlgiyLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGleLPRSPLlgrlfgsakhhAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFG--LPKRQA-----------SMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSE 203
Cdd:PRK15439 159 SRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPE 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-203 |
3.28e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 79.05 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 17 VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAE-------PDASR-GVVFQrysvFPHL 88
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyirPVRKRiGMVFQ----FPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVL-DNVAlglelpRSPLLG-RLFGSAKHHAREQAAALLRKVGLD-HALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLD 165
Cdd:PRK13646 97 QLFeDTVE------REIIFGpKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 921961068 166 EPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSE 203
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNE 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-213 |
3.52e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 3.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKS----TFLRLL--LGQETASKG--------QILLDGQALAAEPDASRG----VVFQ 80
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKmllrrrsrQVIELSEQSAAQMRHVRGadmaMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 R--YSVFPHLTVLDNVALGLELPRspllgrlfGSAKHHAREQAAALLRKVGLDHA---LDKYPAQLSGGMQQRLAIAQAL 155
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQ--------GASREEAMVEAKRMLDQVRIPEAqtiLSRYPHQLSGGMRQRVMIAMAL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:PRK10261 184 SCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLV 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-171 |
4.14e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.05 E-value: 4.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA-AEPDASR----GVVFQRYSVFPHLTVLDN 93
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQeagiGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 94 VALGLElPRSPllgrlFGSAKHHA-REQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGAL 171
Cdd:PRK10762 100 IFLGRE-FVNR-----FGRIDWKKmYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
4-201 |
4.31e-17 |
|
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: 77.37 E-value: 4.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV-VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDgQALAAEPDASRGVVFQRY 82
Cdd:cd03290 1 VQVTNGYFSWGSGLaTLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS-NKNESEPSFEATRSRNRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 83 SVF-----PHL---TVLDNVALGlelprSPllgrlFGSAKHHAREQAAAL-----LRKVGLDHALDKYPAQLSGGMQQRL 149
Cdd:cd03290 80 SVAyaaqkPWLlnaTVEENITFG-----SP-----FNKQRYKAVTDACSLqpdidLLPFGDQTEIGERGINLSGGQRQRI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 921961068 150 AIAQALIMKPRVLLLDEPFGALDPGIRKD-MHQLLLALWRETRLTVFMVTHDL 201
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTHKL 202
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
4-172 |
9.15e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAlAAEPDASRGVVF--QR 81
Cdd:PRK13539 3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYlgHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAAllrkVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRV 161
Cdd:PRK13539 82 NAMKPALTVAENLEF---------WAAFLGGEELDIAAALEA----VGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170
....*....|.
gi 921961068 162 LLLDEPFGALD 172
Cdd:PRK13539 149 WILDEPTAALD 159
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
22-216 |
1.28e-16 |
|
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: 79.29 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 22 LNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAepdaSRGVVFQRYSVFPHLTVLDNVALGLElp 101
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCPQFDAIDDLLTGRE-- 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 102 RSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQ 181
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180 190
....*....|....*....|....*....|....*
gi 921961068 182 LLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDK 216
Cdd:TIGR01257 2112 TIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVK 2145
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-173 |
1.55e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDAS-RGVVFQR- 81
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DARhRRAVCPRi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 -Y-------SVFPHLTVLDNVALglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKyPA-QLSGGMQQRLAIA 152
Cdd:NF033858 79 aYmpqglgkNLYPTLSVFENLDF---------FGRLFGQDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLC 148
|
170 180
....*....|....*....|.
gi 921961068 153 QALIMKPRVLLLDEPFGALDP 173
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDP 169
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
5-167 |
2.09e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 75.87 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQE--TASKGQILLDGQA-LAAEPD--ASRGV-- 77
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDiLELSPDerARAGIfl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPHLTVLD--NVALGlELPRSPLLGRLFgsakhhaREQAAALLRKVGLDHA-LDKYPAQ-LSGGMQQRLAIAQ 153
Cdd:COG0396 82 AFQYPVEIPGVSVSNflRTALN-ARRGEELSAREF-------LKLLKEKMKELGLDEDfLDRYVNEgFSGGEKKRNEILQ 153
|
170
....*....|....
gi 921961068 154 ALIMKPRVLLLDEP 167
Cdd:COG0396 154 MLLLEPKLAILDET 167
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-203 |
3.80e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.14 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETAS--KGQILLDGQAL------AAEpdaSRGVVF--QRYSVFPHL 88
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCrfkdirDSE---ALGIVIihQELALIPYL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNVALGLELPRSPLLGRlfgsakHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPF 168
Cdd:NF040905 94 SIAENIFLGNERAKRGVIDW------NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190
....*....|....*....|....*....|....*
gi 921961068 169 GALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSE 203
Cdd:NF040905 168 AALNEEDSAALLDLLLEL-KAQGITSIIISHKLNE 201
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-172 |
5.13e-16 |
|
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: 74.07 E-value: 5.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepdasrgvvFQRYSVFPHLTVLDN 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD----------FQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 94 VAlGLELPRSPLLGRLFGSAKHhAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:cd03231 81 AP-GIKTTLSVLENLRFWHADH-SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-185 |
7.67e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.68 E-value: 7.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGVVFqrY-----SVFPHL 88
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLL--YlghqpGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNVAlglelprspLLGRLFGSAKhhaREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPF 168
Cdd:PRK13538 90 TALENLR---------FYQRLHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170
....*....|....*..
gi 921961068 169 GALDPGIRKDMHQLLLA 185
Cdd:PRK13538 158 TAIDKQGVARLEALLAQ 174
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-202 |
9.11e-16 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 76.32 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYG-DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDASRGVVFQRY 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK---DIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 83 SVFPHL------TVLDNVALGlelprspllgrlfgsAKHHAREQ---AAALLRKV---------GLDHALDKYPAQLSGG 144
Cdd:TIGR01193 551 NYLPQEpyifsgSILENLLLG---------------AKENVSQDeiwAACEIAEIkddienmplGYQTELSEEGSSISGG 615
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 145 MQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwreTRLTVFMVTHDLS 202
Cdd:TIGR01193 616 QKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL---QDKTIIFVAHRLS 670
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
28-201 |
1.47e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 74.06 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 28 EGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRG----VVFQRYSVfpHLTVLDNVALGLELPRs 103
Cdd:PRK15112 38 EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSqrirMIFQDPST--SLNPRQRISQILDFPL- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 104 pllgRLFGSAKHHAREQAA-ALLRKVGL--DHAlDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMH 180
Cdd:PRK15112 115 ----RLNTDLEPEQREKQIiETLRQVGLlpDHA-SYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189
|
170 180
....*....|....*....|.
gi 921961068 181 QLLLALWRETRLTVFMVTHDL 201
Cdd:PRK15112 190 NLMLELQEKQGISYIYVTQHL 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-201 |
2.37e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.22 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepdasrGVVFQ 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI-------GYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPH--LTVLDNVALGLELPRSPLLGRLfgsakhhAREQAAALLrkvglDHALDKypaqLSGGMQQRLAIAQALIMK 158
Cdd:PRK09544 75 KLYLDTTlpLTVNRFLRLRPGTKKEDILPAL-------KRVQAGHLI-----DAPMQK----LSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-222 |
2.42e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAL-----AAEPDASR 75
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfastTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVFQRYSVFPHLTVLDNVALGlELPRSpllgrlFGSA-KHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQA 154
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLG-QLPHK------GGIVnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 155 LIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLtVFMVTHDLSEGFSLGTRLLVF-DKVRVDPH 222
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFkDGRYVATF 222
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-219 |
2.94e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 74.61 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-R---GVVFQRYSVFPHlTVLDNV 94
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlRrniAVVFQDAGLFNR-SIEDNI 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 95 ALGLElprspllgrlfgSAK----HHAREQAAAL---LRKV-GLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDE 166
Cdd:PRK13657 430 RVGRP------------DATdeemRAAAERAQAHdfiERKPdGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 921961068 167 PFGALDPGIRKDMHQLLLALwRETRlTVFMVTHDLSEgFSLGTRLLVFDKVRV 219
Cdd:PRK13657 498 ATSALDVETEAKVKAALDEL-MKGR-TTFIIAHRLST-VRNADRILVFDNGRV 547
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-172 |
3.59e-15 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 74.60 E-value: 3.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAE-----PDASR 75
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdpPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 76 GVVF--------------QRYSVFPHLTVLDnvalglelPRSPLLGRLfgsakhhAREQA--------------AALLRK 127
Cdd:PRK11147 81 GTVYdfvaegieeqaeylKRYHDISHLVETD--------PSEKNLNEL-------AKLQEqldhhnlwqlenriNEVLAQ 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 128 VGLDHalDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:PRK11147 146 LGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-199 |
3.78e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.03 E-value: 3.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLdgqalaaePdASRGVVFqrysvfphltvldnv 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------P-EGEDLLF--------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 95 algleLPRSPLL--GRLfgsakhhaREQAAallrkvgldhaldkYP--AQLSGGMQQRLAIAQALIMKPRVLLLDEPFGA 170
Cdd:cd03223 69 -----LPQRPYLplGTL--------REQLI--------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
|
170 180
....*....|....*....|....*....
gi 921961068 171 LDPGIRKDMHQLLlalwRETRLTVFMVTH 199
Cdd:cd03223 122 LDEESEDRLYQLL----KELGITVISVGH 146
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-202 |
7.92e-15 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 73.59 E-value: 7.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAA-EPDASRG---VVFQRYSVFPHlTV 90
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSrlaVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 91 LDNVALGlelprSPllgrlfgSAKHHAREQAAAL-------LR-KVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVL 162
Cdd:PRK10789 406 ANNIALG-----RP-------DATQQEIEHVARLasvhddiLRlPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 163 LLDEPFGALDPgirKDMHQLL--LALWRETRlTVFMVTHDLS 202
Cdd:PRK10789 474 ILDDALSAVDG---RTEHQILhnLRQWGEGR-TVIISAHRLS 511
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-200 |
1.83e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 1.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 17 VVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETAS--------KGQILLDGQALAAePDASRgvVFQRYSVFPH- 87
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAA-IDAPR--LARLRAVLPQa 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 88 ------LTVLDNVALGlelpRSPlLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQAL------ 155
Cdd:PRK13547 92 aqpafaFSAREIVLLG----RYP-HARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpp 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 156 ---IMKPRVLLLDEPFGALDPGirkDMHQLL---LALWRETRLTVFMVTHD 200
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLA---HQHRLLdtvRRLARDWNLGVLAIVHD 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-243 |
3.35e-14 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 3.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDG-------QALAAEPdasrGVVF-QRYSVFPHLTV 90
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrrKEFARRI----GVVFgQRSQLWWDLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 91 LDNVAlglelprspLLGRLFGSAKHHAREQAAALLRKVGLDHALDKyPA-QLSGGMQQRLAIAQALIMKPRVLLLDEPFG 169
Cdd:COG4586 114 IDSFR---------LLKAIYRIPDAEYKKRLDELVELLDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTI 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 921961068 170 ALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKvrvdphapGaygaRITYDIPLNSERRK 243
Cdd:COG4586 184 GLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH--------G----RIIYDGSLEELKER 245
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-201 |
5.33e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 69.48 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGqETASKGQILLDGQALAAEPDAS----RGVVFQRYSVFPHLTVLDNV 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAElarhRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 95 ALGLElprspllgrlfGSAKHHAREQA-AALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIM-------KPRVLLLDE 166
Cdd:COG4138 91 ALHQP-----------AGASSEAVEQLlAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 921961068 167 PFGALDpgIRkdmHQL----LLALWRETRLTVFMVTHDL 201
Cdd:COG4138 160 PMNSLD--VA---QQAaldrLLRELCQQGITVVMSSHDL 193
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-202 |
5.36e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 71.20 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY--GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-R---GV 77
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlRnqvAL 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFpHLTVLDNVAlglelprspllgrlFGSAKHHAREQ--AAA-------LLRKV--GLDHALDKYPAQLSGGMQ 146
Cdd:PRK11176 422 VSQNVHLF-NDTIANNIA--------------YARTEQYSREQieEAArmayamdFINKMdnGLDTVIGENGVLLSGGQR 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRlTVFMVTHDLS 202
Cdd:PRK11176 487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNR-TSLVIAHRLS 540
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
105-219 |
5.57e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 70.53 E-value: 5.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 105 LLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLL 184
Cdd:NF000106 109 MIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVR 188
|
90 100 110
....*....|....*....|....*....|....*
gi 921961068 185 ALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:NF000106 189 SMVRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRV 222
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
4-172 |
9.43e-14 |
|
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: 70.23 E-value: 9.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDAS-R---GVV 78
Cdd:COG5265 358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASlRaaiGIV 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 fqrysvfPHLTVL------DNVAlglelprsplLGRLfgSAKHHAREQAAallRKVGLDH---AL-DKYPAQ-------L 141
Cdd:COG5265 438 -------PQDTVLfndtiaYNIA----------YGRP--DASEEEVEAAA---RAAQIHDfieSLpDGYDTRvgerglkL 495
|
170 180 190
....*....|....*....|....*....|.
gi 921961068 142 SGGMQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-214 |
1.02e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.20 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 6 VNNVWQRYGDQVvlEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA--AEPDA-SRGVVFQRY 82
Cdd:PRK09700 268 VRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAvKKGMAYITE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 83 S-----VFPHLTVLDNVALGlelpRSPLLGRLFGSAK--HHAREQAAALLRKVGLD---HALDKYPAQLSGGMQQRLAIA 152
Cdd:PRK09700 346 SrrdngFFPNFSIAQNMAIS----RSLKDGGYKGAMGlfHEVDEQRTAENQRELLAlkcHSVNQNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 153 QALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVF 214
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVF 482
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-228 |
2.49e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 25 QVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDgQALAAEPdasrgvvfQRYSVFPHLTV---LDNVAlglelp 101
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKISYKP--------QYIKPDYDGTVedlLRSIT------ 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 102 rspllgRLFGSAKHHAReqaaaLLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALD--------P 173
Cdd:PRK13409 426 ------DDLGSSYYKSE-----IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavaK 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 174 GIRKDMhqlllalwRETRLTVFMVTHD------LSEgfslgtRLLVFDKVrvdphaPGAYG 228
Cdd:PRK13409 495 AIRRIA--------EEREATALVVDHDiymidyISD------RLMVFEGE------PGKHG 535
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
19-228 |
3.62e-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: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVD-----EGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLD------GQALaaEPDASRGVVfqrysvfph 87
Cdd:COG1245 351 YGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYI--SPDYDGTVE--------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 88 lTVLDNVAlglelprspllGRLFGSAKHHAReqaaaLLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEP 167
Cdd:COG1245 420 -EFLRSAN-----------TDDFGSSYYKTE-----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 168 FGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL------SEgfslgtRLLVFDKVrvdphaPGAYG 228
Cdd:COG1245 483 SAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIylidyiSD------RLMVFEGE------PGVHG 537
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-219 |
4.79e-13 |
|
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: 66.36 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD--QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPdasRGVVFQR 81
Cdd:cd03244 3 IEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSVfphltvldnvalgleLPRSPLLgrLFGSAKH-------HAREQAAALLRKVGLDHALDKYP-----------AQLSG 143
Cdd:cd03244 80 ISI---------------IPQDPVL--FSGTIRSnldpfgeYSDEELWQALERVGLKEFVESLPggldtvveeggENLSV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 144 GMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDLSegfslgT-----RLLVFDKVR 218
Cdd:cd03244 143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLD------TiidsdRILVLDKGR 214
|
.
gi 921961068 219 V 219
Cdd:cd03244 215 V 215
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
12-202 |
4.83e-13 |
|
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: 66.62 E-value: 4.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYG-DQVVLEGLNLqVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQilldgqaLAAEPD------ASRGVVFQRYsv 84
Cdd:cd03236 9 RYGpNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-------FDDPPDwdeildEFRGSELQNY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 85 fphLTVLDNValGLELPRSP----LLGRLF-GSA-----KHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQA 154
Cdd:cd03236 79 ---FTKLLEG--DVKVIVKPqyvdLIPKAVkGKVgellkKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 921961068 155 LIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLS 202
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDLA 200
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-200 |
6.36e-13 |
|
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: 67.90 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 22 LNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAL-AAEPDASR---GVVFQRYSVFPHLtvldnvaLG 97
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYRqlfSAVFSDFHLFDRL-------LG 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 98 LELPRSPllgrlfgsakhharEQAAALLRKVGLDHAL----DKY-PAQLSGGMQQRLAIAQALIMKPRVLLLDEpFGA-L 171
Cdd:COG4615 424 LDGEADP--------------ARARELLERLELDHKVsvedGRFsTTDLSQGQRKRLALLVALLEDRPILVFDE-WAAdQ 488
|
170 180
....*....|....*....|....*....
gi 921961068 172 DPGIRKDMHQLLLALWRETRLTVFMVTHD 200
Cdd:COG4615 489 DPEFRRVFYTELLPELKARGKTVIAISHD 517
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
8-199 |
8.40e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 8 NVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASrgvvfqrysvfph 87
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREAS------------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 88 ltVLDNVALGLELPrspllgrlfgsakhhareQAAALLRKVGLDHA--LDKYPAQLSGGMQQRLAIAQALIMKPRVLLLD 165
Cdd:COG2401 102 --LIDAIGRKGDFK------------------DAVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190
....*....|....*....|....*....|....*
gi 921961068 166 EpFGA-LDPGIRKDMHQLLLALWRETRLTVFMVTH 199
Cdd:COG2401 162 E-FCShLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-213 |
1.88e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEP--DA-SRGVVF-----QRYSVFPHLTV 90
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpqDGlANGIVYisedrKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 91 LDNVALGLELPRSPLLGRLfgsakHHAREQAAAllrkvglDHALD----KYPAQ------LSGGMQQRLAIAQALIMKPR 160
Cdd:PRK10762 348 KENMSLTALRYFSRAGGSL-----KHADEQQAV-------SDFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 921961068 161 VLLLDEPFGALDPGIRKDMHQLLLALWRETrLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSEMPEVLGMSDRILV 467
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
26-219 |
2.24e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.00 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 26 VDEGEFCTLVGTSGCGKSTFLRLLLGQ-ETASKGQILLDGQALAAEPDA---SRGVVF-----QRYSVFPHLTVLDNVAL 96
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAqaiRAGIAMvpedrKRHGIVPILGVGKNITL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 97 GLeLPRSPLLGRLFGSAKHHAREQAAALLrKVGLDHAlDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIR 176
Cdd:TIGR02633 363 SV-LKSFCFKMRIDAAAELQIIGSAIQRL-KVKTASP-FLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 921961068 177 KDMHQLLLALWRETrLTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR02633 440 YEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
19-215 |
2.59e-12 |
|
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: 64.74 E-value: 2.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEF-----CTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPdasrgvvfQRYSVFPHLTVLDn 93
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP--------QYIKADYEGTVRD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 94 valgleLPRSPLLGrlFGSAKHHAREqaaaLLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDP 173
Cdd:cd03237 81 ------LLSSITKD--FYTHPYFKTE----IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 174 GIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFD 215
Cdd:cd03237 149 EQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
15-172 |
2.73e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.06 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG--QETASKGQILLDGQALAAEPDASRGVVFQRYSVFPHLTVLD 92
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 93 NVALG--LELPRSpllgrLFGSAKHHAREQAAALLRKVGLDHAL--DKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPF 168
Cdd:PLN03211 160 TLVFCslLRLPKS-----LTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
....
gi 921961068 169 GALD 172
Cdd:PLN03211 235 SGLD 238
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-172 |
2.79e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGvvfqryS 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRD------A 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VFPHLTVLDNVALGLELPRspllgrlFGSAKHHAREQAAALLRKvGLDHalDKYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:TIGR03719 397 LDPNKTVWEEISGGLDIIK-------LGKREIPSRAYVGRFNFK-GSDQ--QKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
....*....
gi 921961068 164 LDEPFGALD 172
Cdd:TIGR03719 467 LDEPTNDLD 475
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-213 |
3.45e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 20 EGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAL--AAEPDASR-GVVF-----QRYSVFPHLTVL 91
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdiRSPRDAIRaGIMLcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 92 DNVALGLElpRSPLLGRLFGSAKHHArEQAAALLRKVGLdhaldKYPA------QLSGGMQQRLAIAQALIMKPRVLLLD 165
Cdd:PRK11288 350 DNINISAR--RHHLRAGCLINNRWEA-ENADRFIRSLNI-----KTPSreqlimNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 921961068 166 EPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVV 468
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-213 |
1.49e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.79 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 26 VDEGEFCTLVGTSGCGKSTFLRLLLGQ-ETASKGQILLDGQALAAEP--DASR-GVVF-----QRYSVFPHLTVLDNVAL 96
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNpqQAIAqGIAMvpedrKRDGIVPVMGVGKNITL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 97 GLeLPRSPLLGRLFGSAKHHAREQAAALLrKVGLDHALDKYpAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIR 176
Cdd:PRK13549 365 AA-LDRFTGGSRIDDAAELKTILESIQRL-KVKTASPELAI-ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAK 441
|
170 180 190
....*....|....*....|....*....|....*..
gi 921961068 177 KDMHQLLLALWRETrLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:PRK13549 442 YEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLV 477
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
22-201 |
1.56e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 22 LNLQVDEGEFCTLVGTSGCGKSTFLRLLLG------QETASKGQiLLDGQALAAEPDASRGVVFQRYSVF---PHLTVLD 92
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdnwRVTADRMR-FDDIDLLRLSPRERRKLVGHNVSMIfqePQSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 93 NVALGLEL----PRSPLLGRL---FGSAKHHAREqaaaLLRKVGL-DH--ALDKYPAQLSGGMQQRLAIAQALIMKPRVL 162
Cdd:PRK15093 105 SERVGRQLmqniPGWTYKGRWwqrFGWRKRRAIE----LLHRVGIkDHkdAMRSFPYELTEGECQKVMIAIALANQPRLL 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 921961068 163 LLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDL 201
Cdd:PRK15093 181 IADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDL 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
4-202 |
1.62e-11 |
|
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: 63.81 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNN---VWQRyGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAlaaepdasrgvvfq 80
Cdd:TIGR00957 637 ITVHNatfTWAR-DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV-------------- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 rySVFPHLTVLDNVALglelPRSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYP-----AQLSGGMQQRLAIAQAL 155
Cdd:TIGR00957 702 --AYVPQQAWIQNDSL----RENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEigekgVNLSGGQKQRVSLARAV 775
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 156 IMKPRVLLLDEPFGALDPGIRKDMHQLLLA----LWRETRLtvfMVTHDLS 202
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVGKHIFEHVIGpegvLKNKTRI---LVTHGIS 823
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
4-201 |
1.63e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGD-QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAL-AAEPDASRGVVFQR 81
Cdd:PRK15056 7 IVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTrQALQKNLVAYVPQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 YSV---FPHLtVLDNVALGlelpRSPLLGRLfGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:PRK15056 87 EEVdwsFPVL-VEDVVMMG----RYGHMGWL-RRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQ 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 921961068 159 PRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDL 201
Cdd:PRK15056 161 GQVILLDEPFTGVDVKTEARIISLLRELRDEGK-TMLVSTHNL 202
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-173 |
3.45e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAlAAEPDASRGVVFQRY--SVFPHLTVLD 92
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRSRFMAYLGHlpGLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 93 NvalglelprsplLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:PRK13543 102 N------------LHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
.
gi 921961068 173 P 173
Cdd:PRK13543 170 L 170
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-199 |
3.68e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 3.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQ--ETASKGQILLDGQALAAEP--DASRGVVF 79
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpQGYSNDLTLFGRRRGSGETiwDIKKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 QRYSVfpHLTVLDNVALglelpRSPLLGRLFGS---------AKHHAREQAAALLrkvGLDHALDKYPAQ-LSGGmQQRL 149
Cdd:PRK10938 341 VSSSL--HLDYRVSTSV-----RNVILSGFFDSigiyqavsdRQQKLAQQWLDIL---GIDKRTADAPFHsLSWG-QQRL 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 921961068 150 A-IAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTH 199
Cdd:PRK10938 410 AlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
19-201 |
4.39e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 4.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQeTASKGQILLDGQALAAEPDAS----RGVVFQRYS------VFPHL 88
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAElarhRAYLSQQQTppfampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TvldnvalglelprspllgrLFGSAKHHAREQAAAL---LRKVGLDHALDKYPAQLSGGMQQRLAIAQALI-----MKP- 159
Cdd:PRK03695 91 T-------------------LHQPDKTRTEAVASALnevAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPa 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 921961068 160 -RVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDL 201
Cdd:PRK03695 152 gQLLLLDEPMNSLDVAQQAALDRLLSELCQQGI-AVVMSSHDL 193
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-219 |
6.30e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.99 E-value: 6.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 28 EGEFCTLVGTSGCGKSTFLRLLLG-QETASKGQ--ILLDGQALAAEPDASR-GVVFQRYSVFPHLTVLD--NVALGLELP 101
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFrSPKGVKGSgsVLLNGMPIDAKEMRAIsAYVQQDDLFIPTLTVREhlMFQAHLRMP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 102 RSpllgrlfgSAKHHAREQAAALLRKVGLDHALDK---YPAQ---LSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGI 175
Cdd:TIGR00955 130 RR--------VTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 921961068 176 RKDMHQLLLALWRETRlTVFMVTHD-LSEGFSLGTRLLVFDKVRV 219
Cdd:TIGR00955 202 AYSVVQVLKGLAQKGK-TIICTIHQpSSELFELFDKIILMAEGRV 245
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-172 |
7.61e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 7.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 13 YGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRG---VVFQRYSVFPHLT 89
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKqlcFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 90 VLDNVALGLELPRSPLlgrlfgsakhhareQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFG 169
Cdd:PRK13540 91 LRENCLYDIHFSPGAV--------------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
...
gi 921961068 170 ALD 172
Cdd:PRK13540 157 ALD 159
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-213 |
1.17e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.22 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 22 LNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASR---GVVF-----QRYSVFPHLTVLDN 93
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarGLVYlpedrQSSGLYLDAPLAWN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 94 ValglelprSPLLGRLFGSAKHHAREQA------AALLRKvgLDHAlDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEP 167
Cdd:PRK15439 362 V--------CALTHNRRGFWIKPARENAvleryrRALNIK--FNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 168 FGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLLV 213
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMADRVLV 475
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-172 |
1.37e-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: 59.35 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQV--VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPdasrgvvfqr 81
Cdd:cd03369 7 IEVENLSVRYAPDLppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 82 ysvfphLTVLDNvALGLeLPRSPLLgrLFGSAK-------HHAREQAAALLR--KVGLDhaldkypaqLSGGMQQRLAIA 152
Cdd:cd03369 77 ------LEDLRS-SLTI-IPQDPTL--FSGTIRsnldpfdEYSDEEIYGALRvsEGGLN---------LSQGQRQLLCLA 137
|
170 180
....*....|....*....|
gi 921961068 153 QALIMKPRVLLLDEPFGALD 172
Cdd:cd03369 138 RALLKRPRVLVLDEATASID 157
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-200 |
2.77e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.95 E-value: 2.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 5 SVNNVWQRY-GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASkgqillDGQALAAePDASRGVVFQRYS 83
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDF------NGEARPQ-PGIKVGYLPQEPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VFPHLTVLDNVALGLELPRSpLLGRLFGSAKHHAREQA--AALLRKVG-------------LDHALD------KYP---- 138
Cdd:TIGR03719 79 LDPTKTVRENVEEGVAEIKD-ALDRFNEISAKYAEPDAdfDKLAAEQAelqeiidaadawdLDSQLEiamdalRCPpwda 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 139 --AQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDpgirkdmhqlllA---LWRETRL-----TVFMVTHD 200
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD------------AesvAWLERHLqeypgTVVAVTHD 217
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
29-172 |
1.39e-09 |
|
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: 56.10 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 29 GEFCTLVGTSGCGKSTFLRLLLGQETAS--KGQILLDGQALAAEPDASRGVVFQRYSVFPHLTVldnvalglelpRSPLl 106
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTV-----------REAL- 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 107 grLFgsakhhareqaAALLRKVGLDHaldkypaqlsggmQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:cd03232 101 --RF-----------SALLRGLSVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-200 |
1.57e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.65 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 6 VNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGVvfqrysVF 85
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHRAE------LD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 86 PHLTVLDNVALGLE------LPRSpLLGRL--FGSAKHHAREQAAAllrkvgldhaldkypaqLSGGMQQRLAIAQaLIM 157
Cdd:PRK11147 396 PEKTVMDNLAEGKQevmvngRPRH-VLGYLqdFLFHPKRAMTPVKA-----------------LSGGERNRLLLAR-LFL 456
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 921961068 158 KPRVLL-LDEPFGALDpgirKDMHQLLLALWRETRLTVFMVTHD 200
Cdd:PRK11147 457 KPSNLLiLDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-172 |
3.45e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.06 E-value: 3.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNN---VWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQ-ETASKGQILLDGqALAAEPDASRgvvf 79
Cdd:PLN03130 615 ISIKNgyfSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGElPPRSDASVVIRG-TVAYVPQVSW---- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 qrysVFpHLTVLDNValglelprspllgrLFGSAKHHAREQAAalLRKVGLDHALDKYPA-----------QLSGGMQQR 148
Cdd:PLN03130 690 ----IF-NATVRDNI--------------LFGSPFDPERYERA--IDVTALQHDLDLLPGgdlteigergvNISGGQKQR 748
|
170 180
....*....|....*....|....
gi 921961068 149 LAIAQALIMKPRVLLLDEPFGALD 172
Cdd:PLN03130 749 VSMARAVYSNSDVYIFDDPLSALD 772
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
12-216 |
3.69e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 56.88 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAaepDASRGVVFQRYSVFPHLTVL 91
Cdd:TIGR00957 1295 REDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA---KIGLHDLRFKITIIPQDPVL 1371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 92 DNVALGLEL-PRSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGA 170
Cdd:TIGR00957 1372 FSGSLRMNLdPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 171 LDPGIrKDMHQLLLALWRETrLTVFMVTHDLSEGFSLgTRLLVFDK 216
Cdd:TIGR00957 1452 VDLET-DNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDK 1494
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-212 |
4.57e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 6 VNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLdgqalaAEpDASRGVVFQ-RYSV 84
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SE-NANIGYYAQdHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 85 FPH-LTVLDNVAL-----GLELPRSPLLGRLFGSAKHhareqaaallrkvgldhaLDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:PRK15064 395 FENdLTLFDWMSQwrqegDDEQAVRGTLGRLLFSQDD------------------IKKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 921961068 159 PRVLLLDEPFGALDpgiRKDMHQLLLALwRETRLTVFMVTHDLSEGFSLGTRLL 212
Cdd:PRK15064 457 PNVLVMDEPTNHMD---MESIESLNMAL-EKYEGTLIFVSHDREFVSSLATRII 506
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-172 |
5.65e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 5.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDgqalaaePDASRGVVFQRYS 83
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-------PNERLGKLRQDQF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VFPHLTVLDNVALGLE--------------LP--------RSPLLGRLFGSAKHHARE-QAAALLRKVGLDhaLDkypaQ 140
Cdd:PRK15064 75 AFEEFTVLDTVIMGHTelwevkqerdriyaLPemseedgmKVADLEVKFAEMDGYTAEaRAGELLLGVGIP--EE----Q 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 921961068 141 LSGGMQQ-------RLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:PRK15064 149 HYGLMSEvapgwklRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-181 |
6.11e-09 |
|
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: 55.25 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY--GDQVVLEGLNLQVDEGEFCTLVGTSGCGKST----FLRLLlgqetASKGQILLDGQALAAEP----DA 73
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLL-----NTEGDIQIDGVSWNSVPlqkwRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 74 SRGVVFQRYSVFphltvldnvalglelprSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQL-----------S 142
Cdd:cd03289 78 AFGVIPQKVFIF-----------------SGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlS 140
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 921961068 143 GGMQQRLAIAQALIMKPRVLLLDEPFGALDP----GIRKDMHQ 181
Cdd:cd03289 141 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPityqVIRKTLKQ 183
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-194 |
6.14e-09 |
|
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: 56.07 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQaLAAEPDASRgvvfqrysVFPHlTVLDNVALG 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-ISFSPQTSW--------IMPG-TIKDNIIFG 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 98 LElprspllgrlFGSAKHHAREQAAALLRKVGLDHALDKYP-----AQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:TIGR01271 511 LS----------YDEYRYTSVIKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180
....*....|....*....|....
gi 921961068 173 PGIRKDMHQLLLA--LWRETRLTV 194
Cdd:TIGR01271 581 VVTEKEIFESCLCklMSNKTRILV 604
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-181 |
7.59e-09 |
|
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: 56.07 E-value: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY--GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLgQETASKGQILLDGQALAA----EPDASRGV 77
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSvtlqTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VFQRYSVFPhltvldnvalglelprspllGRLFGSAKHHAR---EQAAALLRKVGLDHALDKYPAQL-----------SG 143
Cdd:TIGR01271 1297 IPQKVFIFS--------------------GTFRKNLDPYEQwsdEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSN 1356
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 921961068 144 GMQQRLAIAQALIMKPRVLLLDEPFGALDPG----IRKDMHQ 181
Cdd:TIGR01271 1357 GHKQLMCLARSILSKAKILLLDEPSAHLDPVtlqiIRKTLKQ 1398
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-172 |
1.07e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 6 VNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQE--TASKGQILLDGQA-LAAEPD--ASRGV--V 78
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESiLDLEPEerAHLGIflA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQrysvFPhltvldnvalgLELP---RSPLLgRLFGSAKHHAREQAAA-----------LLRKVGLD-HALDKYPAQ-LS 142
Cdd:CHL00131 90 FQ----YP-----------IEIPgvsNADFL-RLAYNSKRKFQGLPELdplefleiineKLKLVGMDpSFLSRNVNEgFS 153
|
170 180 190
....*....|....*....|....*....|
gi 921961068 143 GGMQQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLD 183
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-221 |
1.13e-08 |
|
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: 52.76 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 29 GEFCTLVGTSGCGKSTFLRLLLGQ-ETASKGQILLDGQALAAEPDASRgvvfqrysvfphltvldnvalglelprspllg 107
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARElGPPGGGVIYIDGEDILEEVLDQL-------------------------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 108 rlfgsakhhareqaaallrkvgLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKD-----MHQL 182
Cdd:smart00382 50 ----------------------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALlllleELRL 107
|
170 180 190
....*....|....*....|....*....|....*....
gi 921961068 183 LLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKVRVDP 221
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLL 146
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-200 |
1.37e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.87 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAlaaepdasRGVVFQRYSVFphltvldn 93
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKV--------RMAVFSQHHVD-------- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 94 valGLELPRSPLL--GRLFGSAkhhAREQAAALLRKVGLDHALDKYPA-QLSGGMQQRLAIAQALIMKPRVLLLDEPFGA 170
Cdd:PLN03073 584 ---GLDLSSNPLLymMRCFPGV---PEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNH 657
|
170 180 190
....*....|....*....|....*....|
gi 921961068 171 LDPGIRKDMHQLLLALwretRLTVFMVTHD 200
Cdd:PLN03073 658 LDLDAVEALIQGLVLF----QGGVLMVSHD 683
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-200 |
2.88e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQ-ALAAepdasrgvVFQRYsvfPHLTV 90
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwQLAW--------VNQET---PALPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 91 --LDNVALGLELPR------------------SPLLGRLFGSAKHHAREQAAALLRKVGLDH-ALDKYPAQLSGGMQQRL 149
Cdd:PRK10636 79 paLEYVIDGDREYRqleaqlhdanerndghaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 150 AIAQALIMKPRVLLLDEPFGALDpgirkdmhqLLLALWRETRL-----TVFMVTHD 200
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLD---------LDAVIWLEKWLksyqgTLILISHD 205
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-172 |
3.47e-08 |
|
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: 52.94 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 18 VLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQaLAAEPDASRgvvfqrysVFPHlTVLDNValg 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-ISFSSQFSW--------IMPG-TIKENI--- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 98 lelprspllgrLFGSAKHHAREQaaALLRKVGLDHALDKYPAQ-----------LSGGMQQRLAIAQALIMKPRVLLLDE 166
Cdd:cd03291 119 -----------IFGVSYDEYRYK--SVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
....*.
gi 921961068 167 PFGALD 172
Cdd:cd03291 186 PFGYLD 191
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-171 |
4.42e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.19 E-value: 4.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQAL-------AAEPDASrgVVFQRYSVFPHLTVL 91
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskeALENGIS--MVHQELNLVLQRSVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 92 DNVALGlelpRSPLLGRLFGSAKHHarEQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGAL 171
Cdd:PRK10982 92 DNMWLG----RYPTKGMFVDQDKMY--RDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
12-201 |
4.71e-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: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 12 RYG-DQVVLEGLNlQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQIlldgqalAAEPDASRgvVFQRYS---VFPH 87
Cdd:COG1245 82 RYGeNGFRLYGLP-VPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-------DEEPSWDE--VLKRFRgteLQDY 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 88 LTVLDN----VALGLE----LPR------SPLLgrlfgsAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQ 153
Cdd:COG1245 152 FKKLANgeikVAHKPQyvdlIPKvfkgtvRELL------EKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAA 225
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 921961068 154 ALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDL 201
Cdd:COG1245 226 ALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDL 272
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
11-228 |
6.78e-08 |
|
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: 51.03 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 11 QRYGDQVVLEGLNlQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPdasrgvvfQRYSvfphltv 90
Cdd:cd03222 8 KRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP--------QYID------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 91 ldnvalglelprspllgrlfgsakhhareqaaallrkvgldhaldkypaqLSGGMQQRLAIAQALIMKPRVLLLDEPFGA 170
Cdd:cd03222 72 --------------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 171 LDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEGFSLGTRLLVFDKvrvdphAPGAYG 228
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG------EPGVYG 153
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-200 |
8.58e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 14 GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASkgqillDGQALAAePDASRGVVFQRYSVFPHLTVLDN 93
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEF------EGEARPA-PGIKVGYLPQEPQLDPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 94 VALGLElPRSPLLGRLFGSAKHHAREQAA--ALLRKVG-------------LDHAL------------DKYPAQLSGGMQ 146
Cdd:PRK11819 91 VEEGVA-EVKAALDRFNEIYAAYAEPDADfdALAAEQGelqeiidaadawdLDSQLeiamdalrcppwDAKVTKLSGGER 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 147 QRLAIAQALIMKPRVLLLDEPFGALDpgirkdmhqlllA---LWRETRL-----TVFMVTHD 200
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLD------------AesvAWLEQFLhdypgTVVAVTHD 219
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-212 |
8.70e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.59 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQA-LAAepdASRGVVFQrysvfphLTVLDNVALG 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAaLIA---ISSGLNGQ-------LTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 98 lelprspllGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEpfgALDPGIRK 177
Cdd:PRK13545 110 ---------GLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQT 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 921961068 178 DMHQLLLAL--WRETRLTVFMVTHDLSEGFSLGTRLL 212
Cdd:PRK13545 178 FTKKCLDKMneFKEQGKTIFFISHSLSQVKSFCTKAL 214
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-172 |
1.77e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNN---VWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQ----ETASkgqILLDGqALAAEPDASRg 76
Cdd:PLN03232 615 ISIKNgyfSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGElshaETSS---VVIRG-SVAYVPQVSW- 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 77 vvfqrysVFpHLTVLDNValglelprspllgrLFGSAKHHAREQAAalLRKVGLDHALDKYPAQ-----------LSGGM 145
Cdd:PLN03232 690 -------IF-NATVRENI--------------LFGSDFESERYWRA--IDVTALQHDLDLLPGRdlteigergvnISGGQ 745
|
170 180
....*....|....*....|....*..
gi 921961068 146 QQRLAIAQALIMKPRVLLLDEPFGALD 172
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-199 |
1.83e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.67 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 16 QVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLG--------QETASKGQILLDGQalaaEPDASRGVV--------- 78
Cdd:TIGR00954 465 DVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGElwpvyggrLTKPAKGKLFYVPQ----RPYMTLGTLrdqiiypds 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 ---FQR--YSVFPHLTVLDNVALglelprspllgrlfgsakHHAreqaaaLLRKVGLDhALDKYPAQLSGGMQQRLAIAQ 153
Cdd:TIGR00954 541 sedMKRrgLSDKDLEQILDNVQL------------------THI------LEREGGWS-AVQDWMDVLSGGEKQRIAMAR 595
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 154 ALIMKPRVLLLDEPFGALDPgirkDMHQLLLALWRETRLTVFMVTH 199
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSV----DVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
141-219 |
2.24e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 2.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 141 LSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRlTVFMVTHDLSEGFSLGTRLLVFDKVRV 219
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
131-202 |
2.75e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.75e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 921961068 131 DHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLS 202
Cdd:PTZ00265 1349 DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1420
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
19-219 |
3.34e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 49.57 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQ--ETAS-KGQILLDGqaLAAEPDASRgvvFQRYSVF--------PH 87
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRteGNVSvEGDIHYNG--IPYKEFAEK---YPGEIIYvseedvhfPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 88 LTVldnvalglelprspllGRLFGSAkhhAREQAAALLRKVgldhaldkypaqlSGGMQQRLAIAQALIMKPRVLLLDEP 167
Cdd:cd03233 98 LTV----------------RETLDFA---LRCKGNEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 921961068 168 FGALDPGIRKDMHQLLLALWRETRLTVFMVTHDLSEG-FSLgtrllvFDKVRV 219
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEiYDL------FDKVLV 192
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
4-202 |
3.79e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.74 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRY--GDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALA--AEPDASRGVvf 79
Cdd:PLN03232 1235 IKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGLTDLRRVL-- 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 80 qrySVFPHLTVLDNVALGLEL-PRSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMK 158
Cdd:PLN03232 1313 ---SIIPQSPVLFSGTVRFNIdPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 159 PRVLLLDEPFGALDpgIRKDmhQLLLALWRE--TRLTVFMVTHDLS 202
Cdd:PLN03232 1390 SKILVLDEATASVD--VRTD--SLIQRTIREefKSCTMLVIAHRLN 1431
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-189 |
4.35e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 1 MSFISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQilldgqalaaepdasrgvvfq 80
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 RYSVFPHLTVL--------------DNVALGLElPRSPLLGR-----LFGSAKHHAR-EQAAALLrkvGLDHALDKYPAQ 140
Cdd:PRK10938 60 RQSQFSHITRLsfeqlqklvsdewqRNNTDMLS-PGEDDTGRttaeiIQDEVKDPARcEQLAQQF---GITALLDRRFKY 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 921961068 141 LSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRE 189
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS 184
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-172 |
4.71e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGvvfqryS 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRD------A 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 84 VFPHLTVLDNVALGLELPRspllgrlFGSAKHHAREQAAALLRKvGLDHalDKYPAQLSGGMQQRLAIAQALIMKPRVLL 163
Cdd:PRK11819 399 LDPNKTVWEEISGGLDIIK-------VGNREIPSRAYVGRFNFK-GGDQ--QKKVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
....*....
gi 921961068 164 LDEPFGALD 172
Cdd:PRK11819 469 LDEPTNDLD 477
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-200 |
1.71e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.63 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 13 YGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLdgqalaaepdaSRGVvfqRYSVFPHLTvld 92
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-----------AKGI---KLGYFAQHQ--- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 93 nvalgLELPR---SPL--LGRLfgsAKHHAREQAAALLRKVGL--DHALDKyPAQLSGGMQQRLAIAQALIMKPRVLLLD 165
Cdd:PRK10636 385 -----LEFLRadeSPLqhLARL---APQELEQKLRDYLGGFGFqgDKVTEE-TRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....*
gi 921961068 166 EPFGALDPGIRKDMHQLLLALwrETRLTVfmVTHD 200
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALIDF--EGALVV--VSHD 486
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-202 |
1.79e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 15 DQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPD-----ASRGVVFQ--------- 80
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINlkwwrSKIGVVSQdpllfsnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 81 ----RYSVFphlTVLDNVALGLELPRSPLLGRLFGSAKHHAREQAAALLRKV-------GLDHAL--------------- 134
Cdd:PTZ00265 477 knniKYSLY---SLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMsnttdsnELIEMRknyqtikdsevvdvs 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 135 -------------DKY-------PAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPG----IRKDMHQLllaLWRET 190
Cdd:PTZ00265 554 kkvlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseylVQKTINNL---KGNEN 630
|
250
....*....|..
gi 921961068 191 RLTVfMVTHDLS 202
Cdd:PTZ00265 631 RITI-IIAHRLS 641
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
124-201 |
3.29e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.50 E-value: 3.29e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 124 LLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALWRETrlTVFMVTHDL 201
Cdd:PRK13409 196 VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDL 271
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-219 |
5.53e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.41 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 29 GEFCTLVGTSGCGKSTFLRLLLGQETASK----GQILLDGQALAAEPDASRGVVFqrYSV-----FPHLTV---LDNVAL 96
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFHigveGVITYDGITPEEIKKHYRGDVV--YNAetdvhFPHLTVgetLDFAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 97 gLELPRSPLLGRlfgSAKHHAREQAAALLRKVGLDHALD-----KYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGAL 171
Cdd:TIGR00956 165 -CKTPQNRPDGV---SREEYAKHIADVYMATYGLSHTRNtkvgnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGL 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 921961068 172 DPGIRKDMHQLLLALWRETRLTVFMVTHDLSE-GFSLgtrllvFDKVRV 219
Cdd:TIGR00956 241 DSATALEFIRALKTSANILDTTPLVAIYQCSQdAYEL------FDKVIV 283
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
34-199 |
5.71e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 34 LVGTSGCGKSTFLR----------------LLLGQETA----SKGQILLDG-----QALAAEpdaSRGVVFQRYSVFPHL 88
Cdd:PLN03073 208 LVGRNGTGKTTFLRymamhaidgipkncqiLHVEQEVVgddtTALQCVLNTdiertQLLEEE---AQLVAQQRELEFETE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 89 TVLDNVALGLELPRSPLLGRLFGSAK-------HHAREQAAALLrkVGLDHALD---KYPAQLSGGMQQRLAIAQALIMK 158
Cdd:PLN03073 285 TGKGKGANKDGVDKDAVSQRLEEIYKrlelidaYTAEARAASIL--AGLSFTPEmqvKATKTFSGGWRMRIALARALFIE 362
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 921961068 159 PRVLLLDEPFGALDpgirkdmhqLLLALWRETRL-----TVFMVTH 199
Cdd:PLN03073 363 PDLLLLDEPTNHLD---------LHAVLWLETYLlkwpkTFIVVSH 399
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-199 |
1.58e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.78 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNVWQRYGDQVVLEGLNLQVDEGEFCTLVGTSGCGKSTFLRLLLGQE--TASKGQILLDGQ---ALAAEPDASRGV- 77
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKdllELSPEDRAGEGIf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 -VFQrYSVfphltvldnvalglELPrspllgrlfGSAKHHAREQAAALLRKVGLDHALDKY---------------PAQL 141
Cdd:PRK09580 82 mAFQ-YPV--------------EIP---------GVSNQFFLQTALNAVRSYRGQEPLDRFdfqdlmeekiallkmPEDL 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 921961068 142 ---------SGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTH 199
Cdd:PRK09580 138 ltrsvnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
4-201 |
3.01e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 43.85 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 4 ISVNNvWQRYGDQVVLE---GLNLqvdegefctLVGTSGCGKSTFL---RLLLGQETASKGQILLDgQALAAEPDASRGV 77
Cdd:COG0419 5 LRLEN-FRSYRDTETIDfddGLNL---------IVGPNGAGKSTILeaiRYALYGKARSRSKLRSD-LINVGSEEASVEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 78 VF----QRYSVFPHLTVLDNVALGLELPRSPLLGRLFG-----SAKHHAREQAAALLRKVGLDHALDKY----------- 137
Cdd:COG0419 74 EFehggKRYRIERRQGEFAEFLEAKPSERKEALKRLLGleiyeELKERLKELEEALESALEELAELQKLkqeilaqlsgl 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 921961068 138 --PAQLSGGMQQRLAIAQALimkprVLLLDepFGALDPGIRKDMHQLLLALwretrltvFMVTHDL 201
Cdd:COG0419 154 dpIETLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALEEL--------AIITHVI 204
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-183 |
3.87e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 36 GTSGCGKSTFLRLLLGQETASKGQILLDGQALAAEPDASRGVVFQRYSVFPHLTVLDNVAlglelprspllgrlFGSAKH 115
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLK--------------FWSEIY 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 921961068 116 HAREQAAALLRKVGLDHALDKYPAQLSGGMQQRLAIAQALIMKPRVLLLDEPFGALDPGIRKDMHQLL 183
Cdd:PRK13541 99 NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
79-202 |
1.20e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 42.38 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 79 FQRYSVFPHLTVLDNVALGLELPRSPLLGRLFGSAKHHAREQAAALLRKVGLDHALDKYP---AQLSGGMQQRLAIAQAL 155
Cdd:pfam13304 172 AADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGElpaFELSDGTKRLLALLAAL 251
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 921961068 156 I---MKPRVLLLDEPFGALDPGIRKDMHQLLLALwRETRLTVFMVTHDLS 202
Cdd:pfam13304 252 LsalPKGGLLLIDEPESGLHPKLLRRLLELLKEL-SRNGAQLILTTHSPL 300
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-202 |
9.56e-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: 38.84 E-value: 9.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 19 LEGLNLQVDEGEFCTLVGTSGCGKSTFLrlllgQETaskgqilldgqaLAAEPDASRGVVFQRYSvfPHLTVLdnvalgl 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEG------------LYASGKARLISFLPKFS--RNKLIF------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 99 elprsplLGRLfgsakhhareqaaALLRKVGLDH-ALDKYPAQLSGGMQQRLAIAQALI--MKPRVLLLDEPFGALDPgi 175
Cdd:cd03238 65 -------IDQL-------------QFLIDVGLGYlTLGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQ-- 122
|
170 180
....*....|....*....|....*....
gi 921961068 176 rKDMHQLLLALWRETRL--TVFMVTHDLS 202
Cdd:cd03238 123 -QDINQLLEVIKGLIDLgnTVILIEHNLD 150
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
138-200 |
1.06e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 39.13 E-value: 1.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 921961068 138 PAQLSGGmQQ-------RLAIAQALIMKPRVLLLDEPFGALDPG-IRKDMHQLLLALWRETRLTVFMVTHD 200
Cdd:cd03240 113 RGRCSGG-EKvlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
123-200 |
1.38e-03 |
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ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.78 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 921961068 123 ALLRKVGLDH-ALDKYPAQLSGGMQQRLAIAQALIMKPRVLL--LDEPFGALDPgirKDMHQLLLALWRETRL--TVFMV 197
Cdd:cd03270 119 GFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHP---RDNDRLIETLKRLRDLgnTVLVV 195
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gi 921961068 198 THD 200
Cdd:cd03270 196 EHD 198
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| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
140-201 |
2.80e-03 |
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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: 37.34 E-value: 2.80e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 921961068 140 QLSGGMQQRLAIAQALI---MKPRVL-LLDEPFGALDPGIRkdmhQLLLALWRETRL---TVFMVTHDL 201
Cdd:cd03227 77 QLSGGEKELSALALILAlasLKPRPLyILDEIDRGLDPRDG----QALAEAILEHLVkgaQVIVITHLP 141
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