|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-172 |
2.66e-89 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 262.33 E-value: 2.66e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------AFVFQEPRLMPWLTVEQNIGFS-DDVGYDKA----WVAQLIDEVGLT 68
Cdd:COG1116 50 KSTLLRLIAGLEKPTSGEVLVDGKPVtgpgpdrGVVFQEPALLPWLTVLDNVALGlELRGVPKAerreRARELLELVGLA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRV 148
Cdd:COG1116 130 GFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRV 209
|
170 180
....*....|....*....|....
gi 1864955972 149 LVMDNRPSSIRQELAVELVHPRDR 172
Cdd:COG1116 210 VVLSARPGRIVEEIDVDLPRPRDR 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1-166 |
1.01e-75 |
|
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: 226.58 E-value: 1.01e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------AFVFQEPRLMPWLTVEQNIGFSDDV-GYDKA----WVAQLIDEVGLT 68
Cdd:cd03293 43 KSTLLRIIAGLERPTSGEVLVDGEPVtgpgpdrGYVFQQDALLPWLTVLDNVALGLELqGVPKAeareRAEELLELVGLS 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRV 148
Cdd:cd03293 123 GFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRV 202
|
170
....*....|....*...
gi 1864955972 149 LVMDNRPSSIRQELAVEL 166
Cdd:cd03293 203 VVLSARPGRIVAEVEVDL 220
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1-174 |
2.47e-52 |
|
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: 167.26 E-value: 2.47e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA-------FVFQEPRLMPWLTVEQNIGFS-DDVGYD------KAWVAQLIDEVG 66
Cdd:TIGR01184 24 KSTLLNLISGLAQPTSGGVILEGKQITepgpdrmVVFQNYSLLPWLTVRENIALAvDRVLPDlskserRAIVEEHIALVG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 67 LTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSD 146
Cdd:TIGR01184 104 LTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSD 183
|
170 180
....*....|....*....|....*....
gi 1864955972 147 RVLVMDNRPSS-IRQELAVELVHPRDRRD 174
Cdd:TIGR01184 184 RVVMLTNGPAAnIGQILEVPFPRPRDRLE 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-153 |
3.35e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 170.66 E-value: 3.35e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------FVFQEPRLMPWLTVEQNIGFSDDV-GYDKA----WVAQLIDEV 65
Cdd:COG3842 44 KTTLLRMIAGFETPDSGRILLDGRDVTglppekrnvgMVFQDYALFPHLTVAENVAFGLRMrGVPKAeiraRVAELLELV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:COG3842 124 GLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALA 203
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:COG3842 204 DRIAVMND 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1-153 |
4.55e-50 |
|
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: 161.15 E-value: 4.55e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG----------GEVAFVFQEPRLMPWLTVEQNIGFSDDVGYDK-----AWVAQLIDEV 65
Cdd:cd03259 39 KTTLLRLIAGLERPDSGEILIDGrdvtgvpperRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPkaeirARVRELLELV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:cd03259 119 GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALA 198
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:cd03259 199 DRIAVMNE 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-153 |
6.16e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 164.55 E-value: 6.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE-----------VAFVFQEPRLMPWLTVEQNIGFSDDV-----GYDKAWVAQLIDE 64
Cdd:COG1118 41 KTTLLRIIAGLETPDSGRIVLNGRDlftnlpprerrVGFVFQHYALFPHMTVAENIAFGLRVrppskAEIRARVEELLEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYL 144
Cdd:COG1118 121 VQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALEL 200
|
....*....
gi 1864955972 145 SDRVLVMDN 153
Cdd:COG1118 201 ADRVVVMNQ 209
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1-172 |
2.23e-47 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 155.61 E-value: 2.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA-------FVFQEPRLMPWLTVEQNIGfsddVGYDKAWVA---QLIDEVGLTGF 70
Cdd:PRK11247 51 KSTLLRLLAGLETPSAGELLAGTAPLAearedtrLMFQDARLLPWKKVIDNVG----LGLKGQWRDaalQALAAVGLADR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 71 GQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLV 150
Cdd:PRK11247 127 ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLL 206
|
170 180
....*....|....*....|..
gi 1864955972 151 MDNrpSSIRQELAVELVHPRDR 172
Cdd:PRK11247 207 IEE--GKIGLDLTVDLPRPRRR 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-165 |
1.66e-46 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 153.48 E-value: 1.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------AFVFQEPRLMPWLTVEQNIGFSDDV-GYDKA----WVAQLIDEVGLT 68
Cdd:COG4525 46 KTTLLNLIAGFLAPSSGEITLDGVPVtgpgadrGVVFQKDALLPWLNVLDNVAFGLRLrGVPKAerraRAEELLALVGLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRV 148
Cdd:COG4525 126 DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRL 205
|
170
....*....|....*..
gi 1864955972 149 LVMDNRPSSIRQELAVE 165
Cdd:COG4525 206 VVMSPGPGRIVERLELD 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1-153 |
3.41e-43 |
|
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: 142.33 E-value: 3.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA--------------FVFQEPRLMPWLTVEQNIGFsddvgydkawvaqlidevg 66
Cdd:cd03229 39 KSTLLRCIAGLEEPDSGSILIDGEDLTdledelpplrrrigMVFQDFALFPHLTVLENIAL------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 67 ltgfgqalpkALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSD 146
Cdd:cd03229 100 ----------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLAD 169
|
....*..
gi 1864955972 147 RVLVMDN 153
Cdd:cd03229 170 RVVVLRD 176
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
1-153 |
6.76e-43 |
|
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: 146.72 E-value: 6.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------FVFQEPRLMPWLTVEQNIGFS-DDVGYDKAWVAQLIDE----V 65
Cdd:TIGR03265 43 KTTLLRIIAGLERQTAGTIYQGGRDITrlppqkrdygIVFQSYALFPNLTVADNIAYGlKNRGMGRAEVAERVAElldlV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:TIGR03265 123 GLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMA 202
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:TIGR03265 203 DRIVVMNH 210
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-153 |
4.28e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 138.73 E-value: 4.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE----------VAFVFQEPRLMPWLTVEQNI--GFSDDVGY---DKAWVAQLIDEV 65
Cdd:COG3840 38 KSTLLNLIAGFLPPDSGRILWNGQDltalppaerpVSMLFQENNLFPHLTVAQNIglGLRPGLKLtaeQRAQVEQALERV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:COG3840 118 GLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIA 197
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:COG3840 198 DRVLLVAD 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-158 |
6.63e-41 |
|
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: 137.81 E-value: 6.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG----------------EVAFVFQEPRLMPWLTVEQNIGF---SDDVGYDKAWVAQL 61
Cdd:cd03297 36 KSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkkinlppqqrKIGLVFQQYALFPHLNVRENLAFglkRKRNREDRISVDEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEA 141
Cdd:cd03297 116 LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEA 195
|
170
....*....|....*...
gi 1864955972 142 LYLSDRVLVM-DNRPSSI 158
Cdd:cd03297 196 EYLADRIVVMeDGRLQYI 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-151 |
1.15e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 137.48 E-value: 1.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------------FVFQEPRLMPWLTVEQNI-------GFSDDVgyDKAW 57
Cdd:COG1136 47 KSTLLNILGGLDRPTSGEVLIDGQDISslserelarlrrrhigFVFQFFNLLPELTALENValplllaGVSRKE--RRER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:COG1136 125 ARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD 204
|
170
....*....|....
gi 1864955972 138 vDEALYLSDRVLVM 151
Cdd:COG1136 205 -PELAARADRVIRL 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1-153 |
1.29e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 137.50 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA-----------FVFQEPRLMPWLTVEQNIGF-----SDDVGYDKAWVAQLIDE 64
Cdd:COG1131 39 KTTTIRMLLGLLRPTSGEVRVLGEDVArdpaevrrrigYVPQEPALYPDLTVRENLRFfarlyGLPRKEARERIDELLEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYL 144
Cdd:COG1131 119 FGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERL 197
|
....*....
gi 1864955972 145 SDRVLVMDN 153
Cdd:COG1131 198 CDRVAIIDK 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-153 |
2.66e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 139.82 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV----------AFVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDEV---- 65
Cdd:COG3839 42 KSTLLRMIAGLEDPTSGEILIGGRDVtdlppkdrniAMVFQSYALYPHMTVYENIAFPLKLrKVPKAEIDRRVREAaell 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:COG3839 122 GLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLA 201
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:COG3839 202 DRIAVMND 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1-152 |
4.74e-40 |
|
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: 135.83 E-value: 4.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------FVFQEPRLMPWLTVEQNIGF--------SDDVgydKAWVAQLI 62
Cdd:cd03300 39 KTTLLRLIAGFETPTSGEILLDGKDITnlpphkrpvnTVFQNYALFPHLTVFENIAFglrlkklpKAEI---KERVAEAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEAL 142
Cdd:cd03300 116 DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAL 195
|
170
....*....|
gi 1864955972 143 YLSDRVLVMD 152
Cdd:cd03300 196 TMSDRIAVMN 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-153 |
1.27e-39 |
|
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: 135.32 E-value: 1.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPR--LMPWLTVEQNI-------GFSDDvgydKAWVA 59
Cdd:COG1124 44 KSTLLRALAGLERPWSGEVTFDGrpvtrrrrkafrRRVQMVFQDPYasLHPRHTVDRILaeplrihGLPDR----EERIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLT-GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDV 138
Cdd:COG1124 120 ELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDL 199
|
170
....*....|....*
gi 1864955972 139 DEALYLSDRVLVMDN 153
Cdd:COG1124 200 AVVAHLCDRVAVMQN 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-153 |
4.91e-39 |
|
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: 136.77 E-value: 4.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQG------ELLQGGGE----------VAFVFQEPRLMPWLTVEQNIGFsddvGYDKAWVA----- 59
Cdd:COG4148 38 KTTLLRAIAGLERPDSGrirlggEVLQDSARgiflpphrrrIGYVFQEARLFPHLSVRGNLLY----GRKRAPRAerris 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 --QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:COG4148 114 fdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHS 193
|
170
....*....|....*.
gi 1864955972 138 VDEALYLSDRVLVMDN 153
Cdd:COG4148 194 LDEVARLADHVVLLEQ 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-153 |
1.26e-38 |
|
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: 132.46 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------FVFQEPRLMPWLTVEQNIGF------------SDDVgydKAWV 58
Cdd:cd03296 41 KTTLLRLIAGLERPDSGTILFGGEDATdvpvqernvgFVFQHYALFRHMTVFDNVAFglrvkprserppEAEI---RAKV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDV 138
Cdd:cd03296 118 HELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQ 197
|
170
....*....|....*
gi 1864955972 139 DEALYLSDRVLVMDN 153
Cdd:cd03296 198 EEALEVADRVVVMNK 212
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
1-153 |
4.92e-38 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 131.08 E-value: 4.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG----------EVAFVFQEPRLMPWLTVEQNIGFSDDV-----GYDKAWVAQLIDEV 65
Cdd:TIGR00968 39 KSTLLRIIAGLEQPDSGRIRLNGQdatrvhardrKIGFVFQHYALFKHLTVRDNIAFGLEIrkhpkAKIKARVEELLELV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:TIGR00968 119 QLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVA 198
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:TIGR00968 199 DRIVVMSN 206
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1-151 |
9.65e-38 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 131.23 E-value: 9.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------------FVFQEPRLMPWLTVEQNIGFSDDV-GYDKA----WVA 59
Cdd:cd03294 63 KSTLLRCINRLIEPTSGKVLIDGQDIAamsrkelrelrrkkisMVFQSFALLPHRTVLENVAFGLEVqGVPRAereeRAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:cd03294 143 EALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLD 222
|
170
....*....|..
gi 1864955972 140 EALYLSDRVLVM 151
Cdd:cd03294 223 EALRLGDRIAIM 234
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-153 |
1.56e-37 |
|
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: 135.42 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG---------------GEVAFVFQEPR--LMPWLTVEQNIGFSDDV--GYDKAW---- 57
Cdd:COG1123 304 KSTLARLLLGLLRPTSGSILFDGkdltklsrrslrelrRRVQMVFQDPYssLNPRMTVGDIIAEPLRLhgLLSRAErrer 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:COG1123 384 VAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISH 463
|
170
....*....|....*..
gi 1864955972 137 DVDEALYLSDRVLVMDN 153
Cdd:COG1123 464 DLAVVRYIADRVAVMYD 480
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1-151 |
2.36e-37 |
|
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: 128.76 E-value: 2.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------------FVFQEPRLMPWLTVEQNI-----GFSDDVGYDKAWVA 59
Cdd:cd03255 43 KSTLLNILGGLDRPTSGEVRVDGTDISklsekelaafrrrhigFVFQSFNLLPDLTALENVelpllLAGVPKKERRERAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:cd03255 123 ELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE 202
|
170
....*....|..
gi 1864955972 140 EALYlSDRVLVM 151
Cdd:cd03255 203 LAEY-ADRIIEL 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-152 |
7.43e-37 |
|
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: 127.62 E-value: 7.43e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGE-LLQG--------------GGEVAFVFQEPR--LMPWLTVEQNI-------GFSDDVGYDKA 56
Cdd:cd03257 44 KSTLARAILGLLKPTSGSiIFDGkdllklsrrlrkirRKEIQMVFQDPMssLNPRMTIGEQIaeplrihGKLSKKEARKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 WVAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVT 135
Cdd:cd03257 124 AVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFIT 203
|
170
....*....|....*..
gi 1864955972 136 HDVDEALYLSDRVLVMD 152
Cdd:cd03257 204 HDLGVVAKIADRVAVMY 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-165 |
2.40e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 124.43 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL-LQG------GGEVAFVFQEPRLMPWLTVEQNIGFSDDV-GYDKAW----VAQLIDEVGLT 68
Cdd:PRK11248 40 KTTLLNLIAGFVPYQHGSItLDGkpvegpGAERGVVFQNEGLLPWRNVQDNVAFGLQLaGVEKMQrleiAHQMLKKVGLE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRV 148
Cdd:PRK11248 120 GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATEL 199
|
170
....*....|....*..
gi 1864955972 149 LVMDNRPSSIRQELAVE 165
Cdd:PRK11248 200 VLLSPGPGRVVERLPLN 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1-153 |
2.88e-35 |
|
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: 123.60 E-value: 2.88e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPR---LMPwlTVEQNIGFSD-DVGYDKAWVAQLIDE 64
Cdd:COG1122 40 KSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrRKVGLVFQNPDdqlFAP--TVEEDVAFGPeNLGLPREEIRERVEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 ----VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHhGIALLLVTHDVDE 140
Cdd:COG1122 118 alelVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDL 196
|
170
....*....|...
gi 1864955972 141 ALYLSDRVLVMDN 153
Cdd:COG1122 197 VAELADRVIVLDD 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1-153 |
3.75e-35 |
|
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: 122.58 E-value: 3.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELL------------QGGGEVAFVFQEPR---LMPwlTVEQNIGFS-DDVGYDKAWVAQLIDE 64
Cdd:cd03225 40 KSTLLRLLNGLLGPTSGEVLvdgkdltklslkELRRKVGLVFQNPDdqfFGP--TVEEEVAFGlENLGLPEEEIEERVEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 ----VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDE 140
Cdd:cd03225 118 alelVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDL 196
|
170
....*....|...
gi 1864955972 141 ALYLSDRVLVMDN 153
Cdd:cd03225 197 LLELADRVIVLED 209
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-153 |
5.40e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 125.97 E-value: 5.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------FVFQEPRLMPWLTVEQNIGFSDDV---------GYDKAWVAQL 61
Cdd:PRK10851 41 KTTLLRIIAGLEHQTSGHIRFHGTDVSrlhardrkvgFVFQHYALFRHMTVFDNIAFGLTVlprrerpnaAAIKAKVTQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEA 141
Cdd:PRK10851 121 LEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
|
170
....*....|..
gi 1864955972 142 LYLSDRVLVMDN 153
Cdd:PRK10851 201 MEVADRVVVMSQ 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1-153 |
1.52e-34 |
|
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: 122.02 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA------------FVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDE--- 64
Cdd:cd03295 40 KTTTMKMINRLIEPTSGEIFIDGEDIReqdpvelrrkigYVIQQIGLFPHMTVEENIALVPKLlKWPKEKIRERADElla 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 -VGL--TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEA 141
Cdd:cd03295 120 lVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEA 199
|
170
....*....|..
gi 1864955972 142 LYLSDRVLVMDN 153
Cdd:cd03295 200 FRLADRIAIMKN 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1-153 |
1.65e-34 |
|
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: 121.06 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF----------VFQEPRLMPWLTVEQNIGFSDDVGY-----DKAWVAQLIDEV 65
Cdd:cd03298 37 KSTLLNLIAGFETPQSGRVLINGVDVTAappadrpvsmLFQENNLFAHLTVEQNVGLGLSPGLkltaeDRQAIEVALARV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:cd03298 117 GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLA 196
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:cd03298 197 QRVVFLDN 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-153 |
5.46e-34 |
|
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: 120.73 E-value: 5.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG-----------GEVAFVFQEPRLMPWLTVEQNIGF-----SDDVGYDKAWVAQLIDE 64
Cdd:COG4555 40 KTTLLRMLAGLLKPDSGSILIDGedvrkeprearRQIGVLPDERGLYDRLTVRENIRYfaelyGLFDEELKKRIEELIEL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYL 144
Cdd:COG4555 120 LGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEAL 198
|
....*....
gi 1864955972 145 SDRVLVMDN 153
Cdd:COG4555 199 CDRVVILHK 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-153 |
8.17e-34 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 123.13 E-value: 8.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------FVFQEPRLMPWLTVEQNIGF--------SDDVgydKAWVAQLI 62
Cdd:PRK09452 53 KTTVLRLIAGFETPDSGRIMLDGQDIThvpaenrhvnTVFQSYALFPHMTVFENVAFglrmqktpAAEI---TPRVMEAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEAL 142
Cdd:PRK09452 130 RMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEAL 209
|
170
....*....|.
gi 1864955972 143 YLSDRVLVMDN 153
Cdd:PRK09452 210 TMSDRIVVMRD 220
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-151 |
1.15e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 122.90 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV----------------AFVFQEPRLMPWLTVEQNIGFSDDV-GYDKA----WVA 59
Cdd:COG4175 66 KSTLVRCLNRLIEPTAGEVLIDGEDItklskkelrelrrkkmSMVFQHFALLPHRTVLENVAFGLEIqGVPKAerreRAR 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:COG4175 146 EALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVFITHDLD 225
|
170
....*....|..
gi 1864955972 140 EALYLSDRVLVM 151
Cdd:COG4175 226 EALRLGDRIAIM 237
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1-153 |
1.38e-33 |
|
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: 118.90 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV----------AFVFQEPRLMPWLTVEQNIGFSDDV-GYDKA-------WVAQLI 62
Cdd:cd03301 39 KTTTLRMIAGLEEPTSGRIYIGGRDVtdlppkdrdiAMVFQNYALYPHMTVYDNIAFGLKLrKVPKDeidervrEVAELL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 devGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEAL 142
Cdd:cd03301 119 ---QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAM 195
|
170
....*....|.
gi 1864955972 143 YLSDRVLVMDN 153
Cdd:cd03301 196 TMADRIAVMND 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1-154 |
1.52e-33 |
|
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: 119.14 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA---------------FVFQEPRLMPWLTVEQNIGF--------SDDVGYDKaw 57
Cdd:cd03261 39 KSTLLRLIVGLLRPDSGEVLIDGEDISglseaelyrlrrrmgMLFQSGALFDSLTVFENVAFplrehtrlSEEEIREI-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:cd03261 117 VLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHD 196
|
170
....*....|....*..
gi 1864955972 138 VDEALYLSDRVLVMDNR 154
Cdd:cd03261 197 LDTAFAIADRIAVLYDG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-154 |
2.36e-33 |
|
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: 118.93 E-value: 2.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA---------------FVFQEPRLMPWLTVEQNIGF-----SDdvgYDKAWVAQ 60
Cdd:COG1127 44 KSVLLKLIIGLLRPDSGEILVDGQDITglsekelyelrrrigMLFQGGALFDSLTVFENVAFplrehTD---LSEAEIRE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDE----VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:COG1127 121 LVLEklelVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTH 200
|
170
....*....|....*...
gi 1864955972 137 DVDEALYLSDRVLVMDNR 154
Cdd:COG1127 201 DLDSAFAIADRVAVLADG 218
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1-153 |
3.23e-33 |
|
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: 116.73 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG-----------GEVAFVFQEPRLMPWLTVEQNIgfsddvgydkawvaqlidevgltg 69
Cdd:cd03230 39 KTTLIKIILGLLKPDSGEIKVLGkdikkepeevkRRIGYLPEEPSLYENLTVRENL------------------------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 70 fgqalpkALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVL 149
Cdd:cd03230 95 -------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERLCDRVA 166
|
....
gi 1864955972 150 VMDN 153
Cdd:cd03230 167 ILNN 170
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
1-153 |
1.11e-32 |
|
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: 119.14 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------FVFQEPRLMPWLTVEQNIGFS---DDVGYD--KAWVAQLIDEV 65
Cdd:TIGR01187 9 KTTLLRLLAGFEQPDSGSIMLDGEDVTnvpphlrhinMVFQSYALFPHMTVEENVAFGlkmRKVPRAeiKPRVLEALRLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:TIGR01187 89 QLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQEEAMTMS 168
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:TIGR01187 169 DRIAIMRK 176
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1-152 |
8.62e-32 |
|
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: 114.16 E-value: 8.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG--------------GEVAFVFQEPRLMPWLTVEQNI--------GFSDDVGYDKAwv 58
Cdd:cd03262 39 KSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrQKVGMVFQQFNLFPHLTVLENItlapikvkGMSKAEAEERA-- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAeHHGIALLLVTHDV 138
Cdd:cd03262 117 LELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEM 195
|
170
....*....|....
gi 1864955972 139 DEALYLSDRVLVMD 152
Cdd:cd03262 196 GFAREVADRVIFMD 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1-153 |
1.37e-31 |
|
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: 114.36 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE----------VAFVFQEPRLMPWLTVEQNIGFS-DDVGYDKAWVAQLIDEV-GLT 68
Cdd:cd03299 38 KSVLLETIAGFIKPDSGKILLNGKDitnlppekrdISYVPQNYALFPHMTVYKNIAYGlKKRKVDKKEIERKVLEIaEML 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQAL---PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:cd03299 118 GIDHLLnrkPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALA 197
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:cd03299 198 DKVAIMLN 205
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-152 |
3.09e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.97 E-value: 3.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------FVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDE----V 65
Cdd:PRK11432 45 KTTVLRLVAGLEKPTEGQIFIDGEDVThrsiqqrdicMVFQSYALFPHMSLGENVGYGLKMlGVPKEERKQRVKEalelV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:PRK11432 125 DLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVS 204
|
....*..
gi 1864955972 146 DRVLVMD 152
Cdd:PRK11432 205 DTVIVMN 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1-153 |
5.07e-31 |
|
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: 115.59 E-value: 5.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL------LQGGGE----------VAFVFQEPRLMPWLTVEQNI--GFSD-DVGYDKAWVAQL 61
Cdd:TIGR02142 36 KTTLIRLIAGLTRPDEGEIvlngrtLFDSRKgiflppekrrIGYVFQEARLFPHLSVRGNLryGMKRaRPSERRISFERV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEA 141
Cdd:TIGR02142 116 IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEV 195
|
170
....*....|..
gi 1864955972 142 LYLSDRVLVMDN 153
Cdd:TIGR02142 196 LRLADRVVVLED 207
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1-153 |
1.16e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 111.06 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPRLMPwLTVEQNIGFSD---DVGYDKAWVAQLIDEV 65
Cdd:COG4619 39 KSTLLRALADLDPPTSGEIYLDGkplsampppewrRQVAYVPQEPALWG-GTVRDNLPFPFqlrERKFDRERALELLERL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLT-GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYL 144
Cdd:COG4619 118 GLPpDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERV 197
|
....*....
gi 1864955972 145 SDRVLVMDN 153
Cdd:COG4619 198 ADRVLTLEA 206
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-154 |
1.72e-30 |
|
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: 110.65 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGE-LLQGGG----------EVAFVFQEPRLMPWLTVEQNIGFS---DDVGYDKAWVAQLIDEVG 66
Cdd:COG4133 41 KTTLLRILAGLLPPSAGEvLWNGEPirdaredyrrRLAYLGHADGLKPELTVRENLRFWaalYGLRADREAIDEALEAVG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 67 LTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIAlLLVTHdvDEALYLSD 146
Cdd:COG4133 121 LAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAV-LLTTH--QPLELAAA 197
|
....*...
gi 1864955972 147 RVLVMDNR 154
Cdd:COG4133 198 RVLDLGDF 205
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-153 |
2.00e-30 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 113.63 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV----------AFVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDEV---- 65
Cdd:NF040840 39 KTVLLELIAGIWPPDSGKIYLDGKDItnlppekrgiAYVYQNYMLFPHKTVFENIAFGLKLrKVPKEEIERKVKEImell 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:NF040840 119 GISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLA 198
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:NF040840 199 DRVGIMLN 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-154 |
2.31e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 110.83 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE----------VAFVFQEPRLMPWLTVEQNIGFSDDVG-----YDKAWVAQLIDEV 65
Cdd:PRK10771 38 KSTLLNLIAGFLTPASGSLTLNGQDhtttppsrrpVSMLFQENNLFSHLTVAQNIGLGLNPGlklnaAQREKLHAIARQM 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:PRK10771 118 GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIA 197
|
170
....*....|
gi 1864955972 146 DR-VLVMDNR 154
Cdd:PRK10771 198 PRsLVVADGR 207
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-154 |
6.11e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.18 E-value: 6.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELL-------QGGGEVAFV---FQEPRLMPwLTVEQNI--GFSDDVGY-------DKAWVAQL 61
Cdd:COG1121 45 KSTLLKAILGLLPPTSGTVRlfgkpprRARRRIGYVpqrAEVDWDFP-ITVRDVVlmGRYGRRGLfrrpsraDREAVDEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEA 141
Cdd:COG1121 124 LERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAV 202
|
170
....*....|...
gi 1864955972 142 LYLSDRVLVMDNR 154
Cdd:COG1121 203 REYFDRVLLLNRG 215
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1-155 |
6.61e-30 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 109.16 E-value: 6.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELL-------QGGGEVAFVFQE---PRLMPwLTVEQ--------NIGFSDDVGY-DKAWVAQL 61
Cdd:cd03235 38 KSTLLKAILGLLKPTSGSIRvfgkpleKERKRIGYVPQRrsiDRDFP-ISVRDvvlmglygHKGLFRRLSKaDKAKVDEA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEA 141
Cdd:cd03235 117 LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLV 195
|
170
....*....|....
gi 1864955972 142 LYLSDRVLVMDNRP 155
Cdd:cd03235 196 LEYFDRVLLLNRTV 209
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-172 |
6.64e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 112.82 E-value: 6.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG----------EVAFVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDEVG--- 66
Cdd:PRK11000 42 KSTLLRMIAGLEDITSGDLFIGEKrmndvppaerGVGMVFQSYALYPHLSVAENMSFGLKLaGAKKEEINQRVNQVAevl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 67 -LTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:PRK11000 122 qLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLA 201
|
170 180
....*....|....*....|....*....
gi 1864955972 146 DRVLVMD-NRPSSIRQELavELVH-PRDR 172
Cdd:PRK11000 202 DKIVVLDaGRVAQVGKPL--ELYHyPANR 228
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-152 |
1.39e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 112.24 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFV----------FQEPRLMPWLTVEQNIGF---SDDVGYD--KAWVAQLIDEV 65
Cdd:PRK11607 58 KSTLLRMLAGFEQPTAGQIMLDGVDLSHVppyqrpinmmFQSYALFPHMTVEQNIAFglkQDKLPKAeiASRVNEMLGLV 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:PRK11607 138 HMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMA 217
|
....*..
gi 1864955972 146 DRVLVMD 152
Cdd:PRK11607 218 GRIAIMN 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1-153 |
2.77e-29 |
|
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: 106.18 E-value: 2.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGgevafvfQEPRLMPWLTVEQNIGFsddvgydkawVAQLidevgltgfgqalpkalSG 80
Cdd:cd00267 38 KSTLLRAIAGLLKPTSGEILIDG-------KDIAKLPLEELRRRIGY----------VPQL-----------------SG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 81 GMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:cd00267 84 GQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKD 155
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-153 |
3.28e-29 |
|
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: 113.39 E-value: 3.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPRLMPwLTVEQNIGFSDDvGYDKAWVAQLIDEVGLT 68
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrRQIGVVLQDVFLFS-GTIRENITLGDP-DATDEEIIEAARLAGLH 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAehHGIALLLVTHD 137
Cdd:COG2274 592 DFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHR 669
|
170
....*....|....*.
gi 1864955972 138 vDEALYLSDRVLVMDN 153
Cdd:COG2274 670 -LSTIRLADRIIVLDK 684
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-153 |
3.52e-29 |
|
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: 108.05 E-value: 3.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV---------------AFVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDE 64
Cdd:cd03258 44 KSTLIRCINGLERPTSGSVLVDGTDLtllsgkelrkarrriGMIFQHFNLLSSRTVFENVALPLEIaGVPKAEIEERVLE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 ----VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDE 140
Cdd:cd03258 124 llelVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEV 203
|
170
....*....|...
gi 1864955972 141 ALYLSDRVLVMDN 153
Cdd:cd03258 204 VKRICDRVAVMEK 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-153 |
3.75e-29 |
|
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: 112.30 E-value: 3.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGL---EKDYQGELLQGG------------GEVAFVFQEPR--LMPwLTVEQNIGFS---DDVGYDKAW--V 58
Cdd:COG1123 45 KSTLALALMGLlphGGRISGEVLLDGrdllelsealrgRRIGMVFQDPMtqLNP-VTVGDQIAEAlenLGLSRAEARarV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDV 138
Cdd:COG1123 124 LELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDL 203
|
170
....*....|....*
gi 1864955972 139 DEALYLSDRVLVMDN 153
Cdd:COG1123 204 GVVAEIADRVVVMDD 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-153 |
5.19e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 107.06 E-value: 5.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG--------GEVAF-------VFQEPRLMPWLTVEQNIGFSDDV-GYDKA----WVAQ 60
Cdd:COG2884 41 KSTLLKLLYGEERPTSGQVLVNGqdlsrlkrREIPYlrrrigvVFQDFRLLPDRTVYENVALPLRVtGKSRKeirrRVRE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDE 140
Cdd:COG2884 121 VLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLEL 199
|
170
....*....|...
gi 1864955972 141 ALYLSDRVLVMDN 153
Cdd:COG2884 200 VDRMPKRVLELED 212
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-151 |
1.18e-28 |
|
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: 108.60 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKD---------YQGELLQG----------GGEVAFVFQEPR--LMPWLTVEQNIG----FSDDVGYDK 55
Cdd:COG0444 44 KSTLARAILGLLPPpgitsgeilFDGEDLLKlsekelrkirGREIQMIFQDPMtsLNPVMTVGDQIAeplrIHGGLSKAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 56 AW--VAQLIDEVGLTGFGQAL---PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIA 130
Cdd:COG0444 124 ARerAIELLERVGLPDPERRLdryPHELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLA 203
|
170 180
....*....|....*....|.
gi 1864955972 131 LLLVTHDVDEALYLSDRVLVM 151
Cdd:COG0444 204 ILFITHDLGVVAEIADRVAVM 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-153 |
1.98e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 106.23 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG--------------GEVAFVFQEPRLMPWLTVEQNI--------GFSDDVGYDKAwv 58
Cdd:COG1126 40 KSTLLRCINLLEEPDSGTITVDGedltdskkdinklrRKVGMVFQQFNLFPHLTVLENVtlapikvkKMSKAEAEERA-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAftRMK---LqDLLLQLAEhHGIALLLVT 135
Cdd:COG1126 118 MELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDP--ELVgevL-DVMRDLAK-EGMTMVVVT 193
|
170
....*....|....*...
gi 1864955972 136 HDVDEALYLSDRVLVMDN 153
Cdd:COG1126 194 HEMGFAREVADRVVFMDG 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1-106 |
2.12e-28 |
|
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: 103.50 E-value: 2.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPRLMPWLTVEQNIGFSDDVGY-----DKAWVAQLID 63
Cdd:pfam00005 24 KSTLLKLIAGLLSPTEGTILLDGqdltdderkslrKEIGYVFQDPQLFPRLTVRENLRLGLLLKGlskreKDARAEEALE 103
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1864955972 64 EVGLTGFG----QALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFS 106
Cdd:pfam00005 104 KLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-153 |
2.65e-28 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.86 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA---------------FVFQEPRLMPWLTVEQNIGFSDDV-GYDKAW----VAQ 60
Cdd:COG1135 44 KSTLIRCINLLERPTSGSVLVDGVDLTalserelraarrkigMIFQHFNLLSSRTVAENVALPLEIaGVPKAEirkrVAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDE 140
Cdd:COG1135 124 LLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDV 203
|
170
....*....|...
gi 1864955972 141 ALYLSDRVLVMDN 153
Cdd:COG1135 204 VRRICDRVAVLEN 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-151 |
4.05e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 105.52 E-value: 4.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG---------------GEVAFVFQEPRLMPWLTVEQNI----------------GFSD 49
Cdd:COG3638 42 KSTLLRCLNGLVEPTSGEILVDGqdvtalrgralrrlrRRIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsllgLFPP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 50 DvgyDKAWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGI 129
Cdd:COG3638 122 E---DRERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGI 198
|
170 180
....*....|....*....|..
gi 1864955972 130 ALLLVTHDVDEALYLSDRVLVM 151
Cdd:COG3638 199 TVVVNLHQVDLARRYADRIIGL 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-153 |
5.75e-28 |
|
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: 105.13 E-value: 5.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPWLTVEQNI---------GFSDDVGYDKAWVA 59
Cdd:COG1120 40 KSTLLRALAGLLKPSSGEVLLDGRDlaslsrrelarrIAYVPQEPPAPFGLTVRELValgryphlgLFGRPSAEDREAVE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:COG1120 120 EALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLN 199
|
170
....*....|....
gi 1864955972 140 EALYLSDRVLVMDN 153
Cdd:COG1120 200 LAARYADRLVLLKD 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1-153 |
6.70e-28 |
|
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: 103.28 E-value: 6.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAfvfqeprLMPWLTVEQNIgfsddvgydkAWVAQLIDEVGLTGFGQALPKALSG 80
Cdd:cd03214 38 KSTLLKTLAGLLKPSSGEILLDGKDLA-------SLSPKELARKI----------AYVPQALELLGLAHLADRPFNELSG 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 81 GMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:cd03214 101 GERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKD 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-154 |
1.02e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 103.33 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAG-LEKD--YQGELLQGGGE----------VAFVFQEPRLMPWLTVEQNIGFS--DDVGYD--KAWVAQLID 63
Cdd:COG4136 40 KSTLLAAIAGtLSPAfsASGEVLLNGRRltalpaeqrrIGILFQDDLLFPHLSVGENLAFAlpPTIGRAqrRARVEQALE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 64 EVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALy 143
Cdd:COG4136 120 EAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAP- 198
|
170
....*....|.
gi 1864955972 144 LSDRVLVMDNR 154
Cdd:COG4136 199 AAGRVLDLGNW 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-153 |
1.78e-27 |
|
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: 103.28 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL-LQG---------------GGEVAFVFQEPRLMPWLTVEQNIG-----FSDDVGYDKAwvA 59
Cdd:COG4181 51 KSTLLGLLAGLDRPTSGTVrLAGqdlfaldedararlrARHVGFVFQSFQLLPTLTALENVMlplelAGRRDARARA--R 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:COG4181 129 ALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA 208
|
170
....*....|....
gi 1864955972 140 EALyLSDRVLVMDN 153
Cdd:COG4181 209 LAA-RCDRVLRLRA 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
1-153 |
8.28e-27 |
|
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: 101.48 E-value: 8.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE----------VAFVFQEPRLMPWLTVEQNIGFSDDVGY-----DKAWVAQLIDEV 65
Cdd:TIGR01277 37 KSTLLNLIAGFIEPASGSIKVNDQShtglapyqrpVSMLFQENNLFAHLTVRQNIGLGLHPGLklnaeQQEKVVDAAQQV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLS 145
Cdd:TIGR01277 117 GIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIA 196
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:TIGR01277 197 SQIAVVSQ 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-153 |
1.47e-26 |
|
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: 105.61 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPWlTVEQNIGFSDDvGYDKAWVAQLIDEVGLT 68
Cdd:COG4988 376 KSTLLNLLLGFLPPYSGSILINGVDlsdldpaswrrqIAWVPQNPYLFAG-TIRENLRLGRP-DASDEELEAALEAAGLD 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHgiALLLVTHD 137
Cdd:COG4988 454 EFVAALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHR 531
|
170
....*....|....*.
gi 1864955972 138 vDEALYLSDRVLVMDN 153
Cdd:COG4988 532 -LALLAQADRILVLDD 546
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
1-152 |
1.74e-26 |
|
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: 100.48 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL------LQGGGE---------VAFVFQEPRLMPWLTVEQNIGFS----DDVGYD--KAWVA 59
Cdd:TIGR02982 44 KTTLLTLIGGLRSVQEGSLkvlgqeLHGASKkqlvqlrrrIGYIFQAHNLLGFLTARQNVQMAlelqPNLSYQeaRERAR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDvD 139
Cdd:TIGR02982 124 AMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-N 202
|
170
....*....|...
gi 1864955972 140 EALYLSDRVLVMD 152
Cdd:TIGR02982 203 RILDVADRILQME 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1-166 |
5.08e-26 |
|
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: 99.95 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE---------------VAFVFQEPRLMPWLTVEQNIgFSDDVGY------------ 53
Cdd:cd03256 40 KSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrqlrrqIGMIFQQFNLIERLSVLENV-LSGRLGRrstwrslfglfp 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 54 --DKAWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIAL 131
Cdd:cd03256 119 keEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITV 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1864955972 132 LLVTHDVDEALYLSDRVL-------VMDNRPSSIRQELAVEL 166
Cdd:cd03256 199 IVSLHQVDLAREYADRIVglkdgriVFDGPPAELTDEVLDEI 240
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1-153 |
1.16e-25 |
|
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: 98.41 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQ-----GELLQGGGE--------------VAFVFQEPRLMPwLTVEQNIGFSDDV-GYDKAWVAQ 60
Cdd:cd03260 39 KSTLLRLLNRLNDLIPgapdeGEVLLDGKDiydldvdvlelrrrVGMVFQKPNPFP-GSIYDNVAYGLRLhGIKLKEELD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGLTGFG-------QALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIalLL 133
Cdd:cd03260 118 ERVEEALRKAAlwdevkdRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VI 195
|
170 180
....*....|....*....|
gi 1864955972 134 VTHDVDEALYLSDRVLVMDN 153
Cdd:cd03260 196 VTHNMQQAARVADRTAFLLN 215
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1-153 |
2.03e-25 |
|
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: 96.30 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPwLTVEQNIgfsddvgydkawvaqlidevglt 68
Cdd:cd03228 41 KSTLLKLLLRLYDPTSGEILIDGVDlrdldleslrknIAYVPQDPFLFS-GTIRENI----------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 gfgqalpkaLSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIalLLVTHDVDEALyLSDRV 148
Cdd:cd03228 97 ---------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGKTV--IVIAHRLSTIR-DADRI 164
|
....*
gi 1864955972 149 LVMDN 153
Cdd:cd03228 165 IVLDD 169
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1-153 |
2.95e-25 |
|
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: 97.44 E-value: 2.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-----------AFVFQEPRLMPWLTVEQNI-------GFSDDVGYDKawVAQLI 62
Cdd:cd03265 39 KTTTIKMLTTLLKPTSGRATVAGHDVvreprevrrriGIVFQDLSVDDELTGWENLyiharlyGVPGAERRER--IDELL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEAL 142
Cdd:cd03265 117 DFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAE 196
|
170
....*....|.
gi 1864955972 143 YLSDRVLVMDN 153
Cdd:cd03265 197 QLCDRVAIIDH 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-153 |
5.48e-25 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.39 E-value: 5.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------------GEVAFVFQEPRLMPWLTVEQNI--------GFSDDVGYD 54
Cdd:COG4161 41 KSSLLRVLNLLETPDSGQLNIAGhqfdfsqkpsekairllrQKVGMVFQQYNLWPHLTVMENLieapckvlGLSKEQARE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 55 KAwvAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAeHHGIALLLV 134
Cdd:COG4161 121 KA--MKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIV 197
|
170
....*....|....*....
gi 1864955972 135 THDVDEALYLSDRVLVMDN 153
Cdd:COG4161 198 THEVEFARKVASQVVYMEK 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-151 |
5.60e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 99.15 E-value: 5.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV----------AFVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDEV---- 65
Cdd:PRK11650 43 KSTLLRMVAGLERITSGEIWIGGRVVnelepadrdiAMVFQNYALYPHMSVRENMAYGLKIrGMPKAEIEERVAEAaril 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTR--MKLQdlLLQLAEHHGIALLLVTHDVDEALY 143
Cdd:PRK11650 123 ELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRvqMRLE--IQRLHRRLKTTSLYVTHDQVEAMT 200
|
....*...
gi 1864955972 144 LSDRVLVM 151
Cdd:PRK11650 201 LADRVVVM 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-153 |
6.56e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.01 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG------------------EVAFVFQEPRLMPWLTVEQNI--------GFSDDVGYD 54
Cdd:PRK11124 41 KSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkairelrrNVGMVFQQYNLWPHLTVQQNLieapcrvlGLSKDQALA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 55 KAwvAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLV 134
Cdd:PRK11124 121 RA--EKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIV 197
|
170
....*....|....*....
gi 1864955972 135 THDVDEALYLSDRVLVMDN 153
Cdd:PRK11124 198 THEVEVARKTASRVVYMEN 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-161 |
3.49e-24 |
|
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: 95.06 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV---------------AFVFQEPRLMPWLTVEQNIgFSDDVGYDKAW-------- 57
Cdd:TIGR02315 41 KSTLLRCINRLVEPSSGSILLEGTDItklrgkklrklrrriGMIFQHYNLIERLTVLENV-LHGRLGYKPTWrsllgrfs 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 ------VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIAL 131
Cdd:TIGR02315 120 eedkerALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITV 199
|
170 180 190
....*....|....*....|....*....|....*..
gi 1864955972 132 LLVTHDVDEALYLSDRVL-------VMDNRPSSIRQE 161
Cdd:TIGR02315 200 IINLHQVDLAKKYADRIVglkageiVFDGAPSELDDE 236
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-153 |
3.90e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.87 E-value: 3.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG----------------EVAFVFQEPRLMPWLTVEQNIGFsddvGYDKAWVAQLIDE 64
Cdd:PRK11144 37 KTSLINAISGLTRPQKGRIVLNGRvlfdaekgiclppekrRIGYVFQDARLFPHYKVRGNLRY----GMAKSMVAQFDKI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 VGLTGFGQAL---PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEA 141
Cdd:PRK11144 113 VALLGIEPLLdryPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEI 192
|
170
....*....|..
gi 1864955972 142 LYLSDRVLVMDN 153
Cdd:PRK11144 193 LRLADRVVVLEQ 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-153 |
9.26e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 9.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG----------------GEVAFVFQEPRLMPWLTVEQNIGFSDDVG-------YDKAW 57
Cdd:PRK10070 67 KSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrKKIAMVFQSFALMPHMTVLDNTAFGMELAginaeerREKAL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAqlIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:PRK10070 147 DA--LRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHD 224
|
170
....*....|....*.
gi 1864955972 138 VDEALYLSDRVLVMDN 153
Cdd:PRK10070 225 LDEAMRIGDRIAIMQN 240
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-153 |
1.55e-23 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 93.56 E-value: 1.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFV-------------FQEPRLMPWLTVEQNI----------GFSDDVGYDKAW 57
Cdd:COG0411 43 KTTLFNLITGFYRPTSGRILFDGRDITGLpphriarlgiartFQNPRLFPELTVLENVlvaaharlgrGLLAALLRLPRA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQ----------LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHH 127
Cdd:COG0411 123 RREereareraeeLLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDER 202
|
170 180
....*....|....*....|....*.
gi 1864955972 128 GIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:COG0411 203 GITILLIEHDMDLVMGLADRIVVLDF 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1-153 |
1.63e-23 |
|
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: 92.53 E-value: 1.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAG-LEKdYQGELlQGGGEVAFVFQEPrlmpWL---TVEQNIGFSDDvgYDKAWVAQLIDEVGLTGFGQALPK 76
Cdd:cd03250 44 KSSLLSALLGeLEK-LSGSV-SVPGSIAYVSQEP----WIqngTIRENILFGKP--FDEERYEKVIKACALEPDLEILPD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 77 -----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVdEALYLS 145
Cdd:cd03250 116 gdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQL-QLLPHA 194
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:cd03250 195 DQIVVLDN 202
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1-153 |
2.21e-23 |
|
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: 92.89 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFV-------------FQEPRLMPWLTVEQNI----------GFSDDVGYDK-- 55
Cdd:cd03219 39 KTTLFNLISGFLRPTSGSVLFDGEDITGLppheiarlgigrtFQIPRLFPELTVLENVmvaaqartgsGLLLARARREer 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 56 ---AWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALL 132
Cdd:cd03219 119 earERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVL 197
|
170 180
....*....|....*....|.
gi 1864955972 133 LVTHDVDEALYLSDRVLVMDN 153
Cdd:cd03219 198 LVEHDMDVVMSLADRVTVLDQ 218
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1-153 |
2.22e-23 |
|
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: 93.67 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG---------------GEVAFVFQEP--RLMPwLTVE-------QNIGFSDDVGYDKa 56
Cdd:TIGR04521 44 KSTLIQHLNGLLKPTSGTVTIDGrditakkkkklkdlrKKVGLVFQFPehQLFE-ETVYkdiafgpKNLGLSEEEAEER- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 wVAQLIDEVGLT-GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVT 135
Cdd:TIGR04521 122 -VKEALELVGLDeEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVT 200
|
170
....*....|....*...
gi 1864955972 136 HDVDEALYLSDRVLVMDN 153
Cdd:TIGR04521 201 HSMEDVAEYADRVIVMHK 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-153 |
4.74e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.08 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG--------------GEVAFVFQEPRLMPWLTVEQNIGF--------SDDVGYDKAwv 58
Cdd:PRK09493 40 KSTLLRCINKLEEITSGDLIVDGlkvndpkvderlirQEAGMVFQQFYLFPHLTALENVMFgplrvrgaSKEEAEKQA-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDV 138
Cdd:PRK09493 118 RELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAE-EGMTMVIVTHEI 196
|
170
....*....|....*
gi 1864955972 139 DEALYLSDRVLVMDN 153
Cdd:PRK09493 197 GFAEKVASRLIFIDK 211
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
1-153 |
4.78e-23 |
|
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: 91.64 E-value: 4.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------------FVFQEPRLMPWLTVEQNI-------GFSDDVGYDKAw 57
Cdd:TIGR02211 44 KSTLLHLLGGLDNPTSGEVLFNGQSLSklssneraklrnkklgFIYQFHHLLPDFTALENVamplligKKSVKEAKERA- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 vAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:TIGR02211 123 -YEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHD 201
|
170
....*....|....*.
gi 1864955972 138 VDEALYLsDRVLVMDN 153
Cdd:TIGR02211 202 LELAKKL-DRVLEMKD 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1-153 |
1.29e-22 |
|
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: 90.35 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE----------VAFVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDEVGLTG 69
Cdd:cd03268 39 KTTTMKIILGLIKPDSGEITFDGKSyqkniealrrIGALIEAPGFYPNLTARENLRLLARLlGIRKKRIDEVLDVVGLKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 70 FGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVL 149
Cdd:cd03268 119 SAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIG 197
|
....
gi 1864955972 150 VMDN 153
Cdd:cd03268 198 IINK 201
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-151 |
1.55e-22 |
|
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: 90.26 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG-----------GEVAFVFQEPRLMPWLTVEQNI-------GFSDDvgYDKAWVAQLI 62
Cdd:cd03263 41 KTTTLKMLTGELRPTSGTAYINGysirtdrkaarQSLGYCPQFDALFDELTVREHLrfyarlkGLPKS--EIKEEVELLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIalLLVTHDVDEAL 142
Cdd:cd03263 119 RVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAE 196
|
....*....
gi 1864955972 143 YLSDRVLVM 151
Cdd:cd03263 197 ALCDRIAIM 205
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1-153 |
2.76e-22 |
|
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: 89.24 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG---------GEVAFVFQEPRLMPWL-TVEQNIGFSDDVGYDKAW-VAQLIDEVGLTG 69
Cdd:cd03226 39 KTTLAKILAGLIKESSGSILLNGkpikakerrKSIGYVMQDVDYQLFTdSVREELLLGLKELDAGNEqAETVLKDLDLYA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 70 FGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVL 149
Cdd:cd03226 119 LKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKVCDRVL 197
|
....
gi 1864955972 150 VMDN 153
Cdd:cd03226 198 LLAN 201
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-151 |
3.10e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.77 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF-------------VFQEPRLMPWLTVEQNI---------GFSDDvGYDKAWV 58
Cdd:COG1129 43 KSTLMKILSGVYQPDSGEILLDGEPVRFrsprdaqaagiaiIHQELNLVPNLSVAENIflgreprrgGLIDW-RAMRRRA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDV 138
Cdd:COG1129 122 RELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKA-QGVAIIYISHRL 200
|
170
....*....|...
gi 1864955972 139 DEALYLSDRVLVM 151
Cdd:COG1129 201 DEVFEIADRVTVL 213
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-153 |
3.44e-22 |
|
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: 90.25 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL---------LQGGGEVAF------VFQEP--RLMPWLTVEQNIG------FSDDVGYDKAW 57
Cdd:TIGR02769 50 KSTLARLLLGLEKPAQGTVsfrgqdlyqLDRKQRRAFrrdvqlVFQDSpsAVNPRMTVRQIIGeplrhlTSLDESEQKAR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:TIGR02769 130 IAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITH 209
|
170
....*....|....*..
gi 1864955972 137 DVDEALYLSDRVLVMDN 153
Cdd:TIGR02769 210 DLRLVQSFCQRVAVMDK 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-153 |
3.75e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.40 E-value: 3.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE---------------VAFVFQEPRLMPWLTVEQNIGF--------SDDVgydKAW 57
Cdd:PRK11153 44 KSTLIRCINLLERPTSGRVLVDGQDltalsekelrkarrqIGMIFQHFNLLSSRTVFDNVALplelagtpKAEI---KAR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVD-AFTRMKLqDLLLQLAEHHGIALLLVTH 136
Cdd:PRK11153 121 VTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSIL-ELLKDINRELGLTIVLITH 199
|
170
....*....|....*..
gi 1864955972 137 DVDEALYLSDRVLVMDN 153
Cdd:PRK11153 200 EMDVVKRICDRVAVIDA 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1-153 |
4.70e-22 |
|
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: 89.80 E-value: 4.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE-------------VAFVFQEP-----RLmpwlTVEQNIGFSDD---VGYDKAW-- 57
Cdd:TIGR04520 41 KSTLAKLLNGLLLPTSGKVTVDGLDtldeenlweirkkVGMVFQNPdnqfvGA----TVEDDVAFGLEnlgVPREEMRkr 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:TIGR04520 117 VDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHD 196
|
170
....*....|....*.
gi 1864955972 138 VDEALyLSDRVLVMDN 153
Cdd:TIGR04520 197 MEEAV-LADRVIVMNK 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-151 |
9.05e-22 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 91.67 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEK-----DYQGELLQGGGEVAF---------VFQEP--RLMPWLTVEQNIG---FSDDVGYDKA----W 57
Cdd:COG4172 325 KSTLGLALLRLIPsegeiRFDGQDLDGLSRRALrplrrrmqvVFQDPfgSLSPRMTVGQIIAeglRVHGPGLSAAerraR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLT-GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:COG4172 405 VAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH 484
|
170
....*....|....*
gi 1864955972 137 DVDEALYLSDRVLVM 151
Cdd:COG4172 485 DLAVVRALAHRVMVM 499
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1-153 |
2.60e-21 |
|
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: 86.86 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-----------AFVFQEPRLMPWLTVEQNI-------GFSDdvGYDKAWVAQLI 62
Cdd:cd03264 38 KTTLMRILATLTPPSSGTIRIDGQDVlkqpqklrrriGYLPQEFGVYPNFTVREFLdyiawlkGIPS--KEVKARVDEVL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIalLLVTHDVDEAL 142
Cdd:cd03264 116 ELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIV--ILSTHIVEDVE 193
|
170
....*....|.
gi 1864955972 143 YLSDRVLVMDN 153
Cdd:cd03264 194 SLCNQVAVLNK 204
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1-152 |
2.88e-21 |
|
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: 88.60 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-----------AFVFQEPRLMPWLTVEQNI-------GFSDDVGYDKAwvAQLI 62
Cdd:TIGR01188 32 KTTTIRMLTTLLRPTSGTARVAGYDVvreprkvrrsiGIVPQYASVDEDLTGRENLemmgrlyGLPKDEAEERA--EELL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEAL 142
Cdd:TIGR01188 110 ELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIRALKE-EGVTILLTTHYMEEAD 188
|
170
....*....|
gi 1864955972 143 YLSDRVLVMD 152
Cdd:TIGR01188 189 KLCDRIAIID 198
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1-153 |
3.79e-21 |
|
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: 86.72 E-value: 3.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------------AFVFQEPRLMPWLTVEQNI------GFSDDVGYDKAWVAQL 61
Cdd:cd03224 39 KTTLLKTIMGLLPPRSGSIRFDGRDItglppheraragiGYVPEGRRIFPELTVEENLllgayaRRRAKRKARLERVYEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEvgLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEA 141
Cdd:cd03224 119 FPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRD-EGVTILLVEQNARFA 195
|
170
....*....|..
gi 1864955972 142 LYLSDRVLVMDN 153
Cdd:cd03224 196 LEIADRAYVLER 207
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-152 |
4.23e-21 |
|
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: 86.15 E-value: 4.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA---------------FVFQEPRLMPWLTVEQNIGFSDDVGYDKA-----WVAQ 60
Cdd:TIGR02673 41 KTTLLKLLYGALTPSRGQVRIAGEDVNrlrgrqlpllrrrigVVFQDFRLLPDRTVYENVALPLEVRGKKEreiqrRVGA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDE 140
Cdd:TIGR02673 121 ALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSL 199
|
170
....*....|..
gi 1864955972 141 ALYLSDRVLVMD 152
Cdd:TIGR02673 200 VDRVAHRVIILD 211
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1-151 |
4.40e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 4.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE-VAFVFQ---EPRLMPwLTVEQ--NIGFSDDVGY-------DKAWVAQLIDEVGL 67
Cdd:NF040873 31 KSTLLKVLAGVLRPTSGTVRRAGGArVAYVPQrseVPDSLP-LTVRDlvAMGRWARRGLwrrltrdDRAAVDDALERVGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 68 TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALyLSDR 147
Cdd:NF040873 110 ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVR-RADP 187
|
....
gi 1864955972 148 VLVM 151
Cdd:NF040873 188 CVLL 191
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-152 |
5.43e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 86.37 E-value: 5.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG----------------EVAFVFQEPRLMPWLTVEQNI-------GFSDDVGYDKAw 57
Cdd:PRK10584 49 KSTLLAILAGLDDGSSGEVSLVGQplhqmdeearaklrakHVGFVFQSFMLIPTLNALENVelpallrGESSRQSRNGA- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 vAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:PRK10584 128 -KALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
170
....*....|....*
gi 1864955972 138 VDEALYLSDRVLVMD 152
Cdd:PRK10584 207 LQLAARCDRRLRLVN 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-153 |
1.07e-20 |
|
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: 84.02 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFvfqeprLMPWLTVEQNIGFsddvgydkawVAQLidevgltgfgqalpkalSG 80
Cdd:cd03216 39 KSTLMKILSGLYKPDSGEILVDGKEVSF------ASPRDARRAGIAM----------VYQL-----------------SV 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 81 GMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:cd03216 86 GERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRA-QGVAVIFISHRLDEVFEIADRVTVLRD 157
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1-151 |
2.30e-20 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 84.90 E-value: 2.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------------AFVFQEPRLMPWLTVEQNI-----GFSDDVGYDKAWVAQLI 62
Cdd:cd03218 39 KTTTFYMIVGLVKPDSGKILLDGQDItklpmhkrarlgiGYLPQEASIFRKLTVEENIlavleIRGLSKKEREEKLEELL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEAL 142
Cdd:cd03218 119 EEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKD-RGIGVLITDHNVRETL 197
|
....*....
gi 1864955972 143 YLSDRVLVM 151
Cdd:cd03218 198 SITDRAYII 206
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-151 |
3.57e-20 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 85.94 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA---------------FVFQEPR--LMPWLTVEQNIGF------SDDVGYDKAW 57
Cdd:COG4608 57 KSTLGRLLLRLEEPTSGEILFDGQDITglsgrelrplrrrmqMVFQDPYasLNPRMTVGDIIAEplrihgLASKAERRER 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:COG4608 137 VAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISH 216
|
170
....*....|....*
gi 1864955972 137 DVDEALYLSDRVLVM 151
Cdd:COG4608 217 DLSVVRHISDRVAVM 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1-153 |
4.13e-20 |
|
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: 83.61 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA---------------FVFQEPRLMPWLTVEQNIGFSDDVGYD--KAW---VAQ 60
Cdd:cd03292 40 KSTLLKLIYKEELPTSGTIRVNGQDVSdlrgraipylrrkigVVFQDFRLLPDRNVYENVAFALEVTGVppREIrkrVPA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDE 140
Cdd:cd03292 120 ALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKEL 198
|
170
....*....|...
gi 1864955972 141 ALYLSDRVLVMDN 153
Cdd:cd03292 199 VDTTRHRVIALER 211
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-153 |
6.78e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 82.48 E-value: 6.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------------AFVFQEPR---LMPWLTVEQNIgfsddvgydkawvaqlide 64
Cdd:cd03215 39 QTELAEALFGLRPPASGEITLDGKPVtrrsprdairagiAYVPEDRKregLVLDLSVAENI------------------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 vgltgfgqALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYL 144
Cdd:cd03215 100 --------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGL 170
|
....*....
gi 1864955972 145 SDRVLVMDN 153
Cdd:cd03215 171 CDRILVMYE 179
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-153 |
1.02e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.89 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF------------VFQEP-RLMPWLTVEQNIGFS-DDVGYD----KAWVAQLI 62
Cdd:PRK13632 48 KSTISKILTGLLKPQSGEIKIDGITISKenlkeirkkigiIFQNPdNQFIGATVEDDIAFGlENKKVPpkkmKDIIDDLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEAL 142
Cdd:PRK13632 128 KKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI 207
|
170
....*....|.
gi 1864955972 143 yLSDRVLVMDN 153
Cdd:PRK13632 208 -LADKVIVFSE 217
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
1-149 |
1.08e-19 |
|
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: 82.28 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE----------------VAFVFQEPRLMPWLTVEQNIgfsdDVG--YDKA------ 56
Cdd:TIGR03608 37 KSTLLNIIGLLEKFDSGQVYLNGQEtpplnskkaskfrrekLGYLFQNFALIENETVEENL----DLGlkYKKLskkekr 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 -WVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVT 135
Cdd:TIGR03608 113 eKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELND-EGKTIIIVT 191
|
170
....*....|....*..
gi 1864955972 136 HDvdeaLYLS---DRVL 149
Cdd:TIGR03608 192 HD----PEVAkqaDRVI 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-153 |
1.12e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.58 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL---------LQGGGEVAF------VFQEP--RLMPWLTVEQNIG------FSDDVGYDKAW 57
Cdd:PRK10419 51 KSTLARLLVGLESPSQGNVswrgeplakLNRAQRKAFrrdiqmVFQDSisAVNPRKTVREIIReplrhlLSLDKAERLAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLT-GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:PRK10419 131 ASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
170
....*....|....*..
gi 1864955972 137 DVDEALYLSDRVLVMDN 153
Cdd:PRK10419 211 DLRLVERFCQRVMVMDN 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1-151 |
1.33e-19 |
|
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: 85.42 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPWlTVEQNIGFSDDVGyDKAWVAQLIDEVGLT 68
Cdd:TIGR02857 361 KSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdqIAWVPQHPFLFAG-TIAENIRLARPDA-SDAEIREALERAGLD 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPKA-----------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTHD 137
Cdd:TIGR02857 439 EFVAALPQGldtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR 516
|
170
....*....|....
gi 1864955972 138 vDEALYLSDRVLVM 151
Cdd:TIGR02857 517 -LALAALADRIVVL 529
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-140 |
1.66e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.45 E-value: 1.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPwLTVEQNIGFSDDVGYDKAWVAQLIDevGLT 68
Cdd:PRK10247 46 KSTLLKIVASLISPTSGTLLFEGEDistlkpeiyrqqVSYCAQTPTLFG-DTVYDNLIFPWQIRNQQPDPAIFLD--DLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGqaLPK--------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDE 140
Cdd:PRK10247 123 RFA--LPDtiltkniaELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-153 |
2.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.86 E-value: 2.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEP-RLMPWLTVEQNIGFS-DDVGYD----KAWVAQLI 62
Cdd:PRK13650 46 KSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhkIGMVFQNPdNQFVGATVEDDVAFGlENKGIPheemKERVNEAL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEaL 142
Cdd:PRK13650 126 ELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE-V 204
|
170
....*....|.
gi 1864955972 143 YLSDRVLVMDN 153
Cdd:PRK13650 205 ALSDRVLVMKN 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
16-152 |
5.62e-19 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 81.33 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 16 QGELLQGGGEVAFVFQEPRLMPWLTVEQNI--------GFSDDVGYDKAwvAQLIDEVGLTGFGQALPKALSGGMAQRVA 87
Cdd:PRK11264 77 KGLIRQLRQHVGFVFQNFNLFPHRTVLENIiegpvivkGEPKEEATARA--RELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 88 IARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGiALLLVTHDVDEALYLSDRVLVMD 152
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMD 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-153 |
9.04e-19 |
|
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: 83.28 E-value: 9.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPRLMPwLTVEQNIGF-SDDVGYDKAWVAqlIDEVGL 67
Cdd:COG4987 374 KSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrRRIAVVPQRPHLFD-TTLRENLRLaRPDATDEELWAA--LERVGL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 68 TGFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHgiALLLVTH 136
Cdd:COG4987 451 GDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITH 528
|
170
....*....|....*..
gi 1864955972 137 DvDEALYLSDRVLVMDN 153
Cdd:COG4987 529 R-LAGLERMDRILVLED 544
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-151 |
1.34e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 81.55 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF---------------VFQEP--RLMPWLTVEQ------NIGFSDDVGYDKAW 57
Cdd:PRK11308 54 KSTLARLLTMIETPTGGELYYQGQDLLKadpeaqkllrqkiqiVFQNPygSLNPRKKVGQileeplLINTSLSAAERREK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:PRK11308 134 ALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISH 213
|
170
....*....|....*
gi 1864955972 137 DVDEALYLSDRVLVM 151
Cdd:PRK11308 214 DLSVVEHIADEVMVM 228
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-164 |
1.37e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG----------------EVAFVFQEPRLMPWLTVEQNIGFSDDVGYDKAWVAQ---- 60
Cdd:PRK11629 48 KSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaelrnqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINsral 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 -LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:PRK11629 128 eMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ 207
|
170 180
....*....|....*....|....*
gi 1864955972 140 EALYLSdRVLVMdnRPSSIRQELAV 164
Cdd:PRK11629 208 LAKRMS-RQLEM--RDGRLTAELSL 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-151 |
1.51e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 80.07 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------------AFVFQEPRLMPWLTVEQNI-------GFSDDVGYDKawVAQ 60
Cdd:COG1137 42 KTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkrarlgiGYLPQEASIFRKLTVEDNIlavlelrKLSKKEREER--LEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDE 140
Cdd:COG1137 120 LLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKE-RGIGVLITDHNVRE 198
|
170
....*....|.
gi 1864955972 141 ALYLSDRVLVM 151
Cdd:COG1137 199 TLGICDRAYII 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1-153 |
2.21e-18 |
|
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: 79.17 E-value: 2.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPRLMpWLTVEQNIGFSDDVGYDKAwVAQLIDEVGLT 68
Cdd:cd03245 43 KSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrRNIGYVPQDVTLF-YGTLRDNITLGAPLADDER-ILRAAELAGVT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHhgIALLLVTHD 137
Cdd:cd03245 121 DFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD--KTLIIITHR 198
|
170
....*....|....*.
gi 1864955972 138 VdEALYLSDRVLVMDN 153
Cdd:cd03245 199 P-SLLDLVDRIIVMDS 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-151 |
2.52e-18 |
|
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: 78.95 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA-----------FVFQEPRLMPWLTVEQNIG-FSDDVGYDKAWVAQLIDEV-GL 67
Cdd:cd03266 44 KTTTLRMLAGLLEPDAGFATVDGFDVVkepaearrrlgFVSDSTGLYDRLTARENLEyFAGLYGLKGDELTARLEELaDR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 68 TGFGQALPK---ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYL 144
Cdd:cd03266 124 LGMEELLDRrvgGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERL 202
|
....*..
gi 1864955972 145 SDRVLVM 151
Cdd:cd03266 203 CDRVVVL 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-152 |
4.09e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.41 E-value: 4.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELL--------QGGGE----VAFVFQEP-RLMPWLTVEQNIGF---SDDVGYDK--AWVAQLI 62
Cdd:PRK13648 48 KSTIAKLMIGIEKVKSGEIFynnqaitdDNFEKlrkhIGIVFQNPdNQFVGSIVKYDVAFgleNHAVPYDEmhRRVSEAL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEAL 142
Cdd:PRK13648 128 KQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM 207
|
170
....*....|
gi 1864955972 143 YlSDRVLVMD 152
Cdd:PRK13648 208 E-ADHVIVMN 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
26-153 |
4.37e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.46 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 26 VAFVFQEPRlmpwltvEQNIG--FSDDVGYD-----------KAWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGL 92
Cdd:PRK13640 86 VGIVFQNPD-------NQFVGatVGDDVAFGlenravprpemIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864955972 93 YSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALyLSDRVLVMDN 153
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDD 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-153 |
4.63e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEP-RLMPWLTVE-------QNIGFSDDVGYDKawVAQ 60
Cdd:PRK13635 46 KSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrqVGMVFQNPdNQFVGATVQddvafglENIGVPREEMVER--VDQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDE 140
Cdd:PRK13635 124 ALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDE 203
|
170
....*....|...
gi 1864955972 141 ALYlSDRVLVMDN 153
Cdd:PRK13635 204 AAQ-ADRVIVMNK 215
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-153 |
4.65e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 80.98 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPRLMPwLTVEQNIGFSDDvGYDKAWVAQLIDEVGLT 68
Cdd:COG1132 379 KSTLVNLLLRFYDPTSGRILIDGvdirdltleslrRQIGVVPQDTFLFS-GTIRENIRYGRP-DATDEEVEEAAKAAQAH 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTHD 137
Cdd:COG1132 457 EFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHR 534
|
170 180
....*....|....*....|.
gi 1864955972 138 vdealyLS-----DRVLVMDN 153
Cdd:COG1132 535 ------LStirnaDRILVLDD 549
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-153 |
4.86e-18 |
|
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: 78.34 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQEPRLMPWLTVEQNIGFSDDV-GYDKAWVAQLIDEV-GLTGFGQA--LP- 75
Cdd:cd03220 61 KSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPELTGRENIYLNGRLlGLSRKEIDEKIDEIiEFSELGDFidLPv 140
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864955972 76 KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIaLLLVTHDVDEALYLSDRVLVMDN 153
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKT-VILVSHDPSSIKRLCDRALVLEK 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-137 |
5.35e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 5.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL-LQGGGEVAFVFQEPRLMPWLTV---------------------EQNIGFSDDVGYDKAWV 58
Cdd:COG0488 37 KSTLLKILAGELEPDSGEVsIPKGLRIGYLPQEPPLDDDLTVldtvldgdaelraleaeleelEAKLAEPDEDLERLAEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVG-----------LTGFG------QALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLL 121
Cdd:COG0488 117 QEEFEALGgweaearaeeiLSGLGfpeedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLK 196
|
170
....*....|....*.
gi 1864955972 122 QlaehHGIALLLVTHD 137
Cdd:COG0488 197 N----YPGTVLVVSHD 208
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1-136 |
5.37e-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: 77.78 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQEPR-----------LMPWLTVEQNIGF-SDDVGYDKAWVAQLIDEVGLT 68
Cdd:TIGR01189 39 KTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHenilylghlpgLKPELSALENLHFwAAIHGGAQRTIEDALAAVGLT 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864955972 69 GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAftrmKLQDLLLQLAEHH---GIALLLVTH 136
Cdd:TIGR01189 119 GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK----AGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1-137 |
6.40e-18 |
|
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: 77.53 E-value: 6.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQE-PRLMPW----------LTVEQNIGFSDDVGYDKAwVAQLIDEVGLTG 69
Cdd:cd03231 39 KTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYlghapgikttLSVLENLRFWHADHSDEQ-VEEALARVGLNG 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864955972 70 FGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:cd03231 118 FEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-153 |
1.20e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPR---LMPwlTVEQNIGFSD-DVGYDKAWVAQLIDE 64
Cdd:PRK13652 43 KSTLFRHFNGILKPTSGSVLIRGEPitkenirevrkfVGLVFQNPDdqiFSP--TVEQDIAFGPiNLGLDEETVAHRVSS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 ----VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDE 140
Cdd:PRK13652 121 alhmLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDL 200
|
170
....*....|...
gi 1864955972 141 ALYLSDRVLVMDN 153
Cdd:PRK13652 201 VPEMADYIYVMDK 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-151 |
1.31e-17 |
|
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: 76.82 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGL--EKDYQGELLQGG---------GEVAFVFQEPRLMPWLTVEQNIGFSddvgydkawvAQLidevgltg 69
Cdd:cd03213 48 KSTLLNALAGRrtGLGVSGEVLINGrpldkrsfrKIIGYVPQDDILHPTLTVRETLMFA----------AKL-------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 70 fgqalpKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAeHHGIALLLVTHDV-DEALYLSDRV 148
Cdd:cd03213 110 ------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA-DTGRTIICSIHQPsSEIFELFDKL 182
|
...
gi 1864955972 149 LVM 151
Cdd:cd03213 183 LLL 185
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-153 |
1.71e-17 |
|
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: 77.02 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 23 GGEVAFVFQEPR--LMPWLTVEQNI--------GFSDDVgydKAWVAQLIDEVGLTGFGQAL---PKALSGGMAQRVAIA 89
Cdd:TIGR02770 61 GRHIATIMQNPRtaFNPLFTMGNHAietlrslgKLSKQA---RALILEALEAVGLPDPEEVLkkyPFQLSGGMLQRVMIA 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 90 RGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:TIGR02770 138 LALLLEPPFLIADEPTTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDD 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-153 |
2.37e-17 |
|
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: 77.05 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGlekdyqgELLQGGGEVAFVFQEPR----------------------LMPWLTVEQNI--GFSDDVGY--- 53
Cdd:COG1119 42 KSTLLSLITG-------DLPPTYGNDVRLFGERRggedvwelrkriglvspalqlrFPRDETVLDVVlsGFFDSIGLyre 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 54 ----DKAWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGI 129
Cdd:COG1119 115 ptdeQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAP 194
|
170 180
....*....|....*....|....
gi 1864955972 130 ALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:COG1119 195 TLVLVTHHVEEIPPGITHVLLLKD 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-151 |
3.31e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.52 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------------AFVfQEPR----LMPWLTVEQNIGFSD----------DVGY 53
Cdd:COG1129 291 RTELARALFGADPADSGEIRLDGKPVrirsprdairagiAYV-PEDRkgegLVLDLSIRENITLASldrlsrggllDRRR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 54 DKAWVAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALL 132
Cdd:COG1129 370 ERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA-EGKAVI 448
|
170
....*....|....*....
gi 1864955972 133 LVTHDVDEALYLSDRVLVM 151
Cdd:COG1129 449 VISSELPELLGLSDRILVM 467
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1-153 |
5.29e-17 |
|
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: 75.77 E-value: 5.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAG-LEKDY--QGELLQGGGE---------VAFVFQEPRLMPWLTVEQNIGF---------SDDVGYDKAWVA 59
Cdd:cd03234 46 KTTLLDAISGrVEGGGttSGQILFNGQPrkpdqfqkcVAYVRQDDILLPGLTVRETLTYtailrlprkSSDAIRKKRVED 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:cd03234 126 VLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRS 205
|
170
....*....|....
gi 1864955972 140 EALYLSDRVLVMDN 153
Cdd:cd03234 206 DLFRLFDRILLLSS 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-151 |
6.12e-17 |
|
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: 77.80 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 23 GGEVAFVFQEP--RLMPWLTVEQNI--------GFSDDVGydKAWVAQLIDEVGLTGFGQ---ALPKALSGGMAQRVAIA 89
Cdd:COG4172 91 GNRIAMIFQEPmtSLNPLHTIGKQIaevlrlhrGLSGAAA--RARALELLERVGIPDPERrldAYPHQLSGGQRQRVMIA 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 90 RGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD---VDEalyLSDRVLVM 151
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvVRR---FADRVAVM 230
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-153 |
9.10e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 75.88 E-value: 9.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE--------------VAFVFQEPR---LMPwlTVEQNIGFSD-DVGYDKAWVAQLI 62
Cdd:PRK13639 41 KSTLFLHFNGILKPTSGEVLIKGEPikydkksllevrktVGIVFQNPDdqlFAP--TVEEDVAFGPlNLGLSKEEVEKRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DE----VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDV 138
Cdd:PRK13639 119 KEalkaVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDV 197
|
170
....*....|....*
gi 1864955972 139 DEALYLSDRVLVMDN 153
Cdd:PRK13639 198 DLVPVYADKVYVMSD 212
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-137 |
1.00e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 77.28 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGE-LLQGGGEVAFVFQEPRLMPWLTVEQNI-------------------GFSD-DVGYDK---- 55
Cdd:TIGR03719 44 KSTLLRIMAGVDKDFNGEaRPQPGIKVGYLPQEPQLDPTKTVRENVeegvaeikdaldrfneisaKYAEpDADFDKlaae 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 56 -AWVAQLIDEVGLTGFGQALPKA---------------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDl 119
Cdd:TIGR03719 124 qAELQEIIDAADAWDLDSQLEIAmdalrcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER- 202
|
170
....*....|....*...
gi 1864955972 120 llQLAEHHGiALLLVTHD 137
Cdd:TIGR03719 203 --HLQEYPG-TVVAVTHD 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
74-151 |
1.37e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 75.35 E-value: 1.37e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864955972 74 LPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK11701 148 LPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVM 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1-156 |
1.39e-16 |
|
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: 75.14 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQEPRLMPWLTVEQNI-GFSDDVGYDKAWVAQLIDEVGLTGFGQALPKALS 79
Cdd:cd03237 38 KTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLsSITKDFYTHPYFKTEIAKPLQIEQILDREVPELS 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864955972 80 GGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVMDNRPS 156
Cdd:cd03237 118 GGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
25-147 |
1.82e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.81 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 25 EVAFVFQEPRLMPwLTVEQNI-------GFSDDVGYDKAWVAQLI-----DEVGLTGFGQALpkALSGGMAQRVAIARGL 92
Cdd:PRK14239 87 EIGMVFQQPNPFP-MSIYENVvyglrlkGIKDKQVLDEAVEKSLKgasiwDEVKDRLHDSAL--GLSGGQQQRVCIARVL 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 93 YSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHgiALLLVTHDVDEALYLSDR 147
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDR 216
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-151 |
2.02e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.51 E-value: 2.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL------LQGGG---------EVAFVFQEP--RLMPWLTVEQNIG----------FSDDVgy 53
Cdd:PRK15079 60 KSTFARAIIGLVKATDGEVawlgkdLLGMKddewravrsDIQMIFQDPlaSLNPRMTIGEIIAeplrtyhpklSRQEV-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 54 dKAWVAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALL 132
Cdd:PRK15079 138 -KDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLI 216
|
170
....*....|....*....
gi 1864955972 133 LVTHDVDEALYLSDRVLVM 151
Cdd:PRK15079 217 FIAHDLAVVKHISDRVLVM 235
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-151 |
2.44e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 75.55 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 23 GGEVAFVFQEP--RLMPWLTVEQNIGFSDDV--GYDKAWVAQ----LIDEVGLTGFGQAL---PKALSGGMAQRVAIARG 91
Cdd:PRK11022 88 GAEVAMIFQDPmtSLNPCYTVGFQIMEAIKVhqGGNKKTRRQraidLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMA 167
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 92 LYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK11022 168 IACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVM 227
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
74-151 |
2.47e-16 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 74.48 E-value: 2.47e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864955972 74 LPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:TIGR02323 145 LPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
77-151 |
2.79e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 74.30 E-value: 2.79e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 77 ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIalLLVTHDVDEALYLSDRVLVM 151
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI--VIVTHNMQQAARVSDYTAFF 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
78-151 |
4.37e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 4.37e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA-EGLSIILVSSEMPEVLGMSDRILVM 468
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-153 |
5.22e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.90 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQG------ELLQGG----------GEVAFVFQ--EPRLMPwLTVE-------QNIGFSDDVGYDK 55
Cdd:PRK13634 46 KSTLLQHLNGLLQPTSGtvtigeRVITAGkknkklkplrKKVGIVFQfpEHQLFE-ETVEkdicfgpMNFGVSEEDAKQK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 56 AwvAQLIDEVGLTgfgQAL----PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIAL 131
Cdd:PRK13634 125 A--REMIELVGLP---EELlarsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTT 199
|
170 180
....*....|....*....|..
gi 1864955972 132 LLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK13634 200 VLVTHSMEDAARYADQIVVMHK 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-163 |
8.99e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.20 E-value: 8.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGeLLQGGGE-------------VAFVFQEP-RLMPWLTVEQNIGFS-DDVGYDKAWVAQLIDE- 64
Cdd:PRK13642 46 KSTTARLIDGLFEEFEG-KVKIDGElltaenvwnlrrkIGMVFQNPdNQFVGATVEDDVAFGmENQGIPREEMIKRVDEa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 ---VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEA 141
Cdd:PRK13642 125 llaVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA 204
|
170 180
....*....|....*....|..
gi 1864955972 142 LYlSDRVLVMdnRPSSIRQELA 163
Cdd:PRK13642 205 AS-SDRILVM--KAGEIIKEAA 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-160 |
2.82e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.61 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 25 EVAFVFQEPRLMPwLTVEQNIGFS------------DDVGYDKAWVAQLIDEVGLTGFGQALpkALSGGMAQRVAIARGL 92
Cdd:PRK14258 89 QVSMVHPKPNLFP-MSVYDNVAYGvkivgwrpkleiDDIVESALKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIARAL 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864955972 93 YSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVMDNRPSSIRQ 160
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQ 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-151 |
3.18e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.54 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------------------------AFVFQEPRLMPWLTVEQNI--------GF 47
Cdd:PRK10619 44 KSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadknqlrllrtrlTMVFQHFNLWSHMTVLENVmeapiqvlGL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 48 SDDVGYDKAwvAQLIDEVGLTGFGQA-LPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEh 126
Cdd:PRK10619 124 SKQEARERA--VKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAE- 200
|
170 180
....*....|....*....|....*
gi 1864955972 127 HGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK10619 201 EGKTMVVVTHEMGFARHVSSHVIFL 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-153 |
3.47e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 71.27 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG-----EVAFVFQeprlmPWLTVEQNIGFSDDV-GYDKAWVAQLIDE-VGLTGFGQA 73
Cdd:COG1134 65 KSTLLKLIAGILEPTSGRVEVNGRvsallELGAGFH-----PELTGRENIYLNGRLlGLSRKEIDEKFDEiVEFAELGDF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 74 L--P-KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIaLLLVTHDVDEALYLSDRVLV 150
Cdd:COG1134 140 IdqPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRT-VIFVSHSMGAVRRLCDRAIW 218
|
...
gi 1864955972 151 MDN 153
Cdd:COG1134 219 LEK 221
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-153 |
3.88e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKdYQGELLQGGGE------------VAFVFQEPRLmPWLTVEQNIGFSDdVGYDKAWVAQLIDEVGLT 68
Cdd:PRK11174 389 KTSLLNALLGFLP-YQGSLKINGIElreldpeswrkhLSWVGQNPQL-PHGTLRDNVLLGN-PDASDEQLQQALENAWVS 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHgiALLLVTHD 137
Cdd:PRK11174 466 EFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQ 543
|
170
....*....|....*.
gi 1864955972 138 VDEaLYLSDRVLVMDN 153
Cdd:PRK11174 544 LED-LAQWDQIWVMQD 558
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
54-153 |
4.25e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.27 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 54 DKAWVAQLIDEVGLTGFGQAL---PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIA 130
Cdd:PRK10418 114 DDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALG 193
|
90 100
....*....|....*....|...
gi 1864955972 131 LLLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK10418 194 MLLVTHDMGVVARLADDVAVMSH 216
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1-153 |
4.50e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 70.39 E-value: 4.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQ-------EPR-LMPWLTV-EQNIGFSDDVGYDK----AWVAQLIDEVGL 67
Cdd:cd03269 39 KTTTIRMILGIILPDSGEVLFDGKPLDIAARnrigylpEERgLYPKMKViDQLVYLAQLKGLKKeearRRIDEWLERLEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 68 TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDR 147
Cdd:cd03269 119 SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEELCDR 197
|
....*.
gi 1864955972 148 VLVMDN 153
Cdd:cd03269 198 VLLLNK 203
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
57-164 |
4.55e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.17 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 WVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:PRK11300 133 RAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEH 212
|
90 100 110
....*....|....*....|....*....|....*
gi 1864955972 137 DVDEALYLSDRVLVM-------DNRPSSIRQELAV 164
Cdd:PRK11300 213 DMKLVMGISDRIYVVnqgtplaNGTPEEIRNNPDV 247
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-151 |
4.59e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF-------------VFQEPRLMPWLTVEQNI------GFSDDVGYDKAW--VA 59
Cdd:COG3845 44 KSTLMKILYGLYQPDSGEILIDGKPVRIrsprdaialgigmVHQHFMLVPNLTVAENIvlglepTKGGRLDRKAARarIR 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLtgfgQALPKA----LSGGMAQRVAIARGLYSRPQVLLLDEPFS-----AVDaftrmKLQDLLLQLAEhHGIA 130
Cdd:COG3845 124 ELSERYGL----DVDPDAkvedLSVGEQQRVEILKALYRGARILILDEPTAvltpqEAD-----ELFEILRRLAA-EGKS 193
|
170 180
....*....|....*....|.
gi 1864955972 131 LLLVTHDVDEALYLSDRVLVM 151
Cdd:COG3845 194 IIFITHKLREVMAIADRVTVL 214
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-173 |
4.66e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 4.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV---------------AFVFQEPRLMPWLTVEQNIGFSDDVGYD------KAWVA 59
Cdd:PRK11831 46 KTTLLRLIGGQIAPDHGEILFDGENIpamsrsrlytvrkrmSMLFQSGALFTDMNVFDNVAYPLREHTQlpapllHSTVM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:PRK11831 126 MKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVP 205
|
170 180 190
....*....|....*....|....*....|....
gi 1864955972 140 EALYLSDRVLVMDNRpSSIRQELAVELVHPRDRR 173
Cdd:PRK11831 206 EVLSIADHAYIVADK-KIVAHGSAQALQANPDPR 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1-137 |
5.88e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGE-LLQGGGEVAFVFQEPRLMPWLTVEQNIgfSDDVGYDKAWVAQL------------------ 61
Cdd:PRK11819 46 KSTLLRIMAGVDKEFEGEaRPAPGIKVGYLPQEPQLDPEKTVRENV--EEGVAEVKAALDRFneiyaayaepdadfdala 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 ---------IDEVGLTGFGQALPKA---------------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQ 117
Cdd:PRK11819 124 aeqgelqeiIDAADAWDLDSQLEIAmdalrcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE 203
|
170 180
....*....|....*....|
gi 1864955972 118 DlllQLAEHHGiALLLVTHD 137
Cdd:PRK11819 204 Q---FLHDYPG-TVVAVTHD 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-152 |
6.49e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 70.89 E-value: 6.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 29 VFQEPRLMPWLT-VEQNIGFS-DDVGYDKAWVAQLIDE----VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLD 102
Cdd:PRK13633 90 VFQNPDNQIVATiVEEDVAFGpENLGIPPEEIRERVDEslkkVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFD 169
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1864955972 103 EPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYlSDRVLVMD 152
Cdd:PRK13633 170 EPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMD 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-153 |
9.84e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.46 E-value: 9.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG--------------GEVAFVFQEPRLMPWL-TVE-------QNIGFSDDVGYDKawV 58
Cdd:PRK13637 46 KSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirKKVGLVFQYPEYQLFEeTIEkdiafgpINLGLSEEEIENR--V 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLT--GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:PRK13637 124 KRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSH 203
|
170
....*....|....*..
gi 1864955972 137 DVDEALYLSDRVLVMDN 153
Cdd:PRK13637 204 SMEDVAKLADRIIVMNK 220
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-153 |
1.25e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.82 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF------------VFQEP--RLMPWLTVEQNIGFSDDVGYD------KAWVAQ 60
Cdd:PRK15112 52 KSTLAKMLAGMIEPTSGELLIDDHPLHFgdysyrsqrirmIFQDPstSLNPRQRISQILDFPLRLNTDlepeqrEKQIIE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVD 139
Cdd:PRK15112 132 TLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLG 211
|
170
....*....|....
gi 1864955972 140 EALYLSDRVLVMDN 153
Cdd:PRK15112 212 MMKHISDQVLVMHQ 225
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-136 |
1.46e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG-----------GEVAFVFQEPRLMPWLTVEQNIGF----SDDVGYDKAWVAqlIDEV 65
Cdd:PRK13538 40 KTSLLRILAGLARPDAGEVLWQGepirrqrdeyhQDLLYLGHQPGIKTELTALENLRFyqrlHGPGDDEALWEA--LAQV 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIAlLLVTH 136
Cdd:PRK13538 118 GLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMV-ILTTH 187
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-153 |
1.60e-14 |
|
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: 69.24 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE-------------VAFVFQEPRLMPWLTVEQNIGFSDDVGYDKAWVAQLIDEVgL 67
Cdd:COG0410 42 KTTLLKAISGLLPPRSGSIRFDGEDitglpphriarlgIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERV-Y 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 68 TGFgqalPK----------ALSGGMAQRVAIARGLYSRPQVLLLDEPF-----SAVDaftrmKLQDLLLQLAEhHGIALL 132
Cdd:COG0410 121 ELF----PRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPSlglapLIVE-----EIFEIIRRLNR-EGVTIL 190
|
170 180
....*....|....*....|.
gi 1864955972 133 LVTHDVDEALYLSDRVLVMDN 153
Cdd:COG0410 191 LVEQNARFALEIADRAYVLER 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-152 |
1.63e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 69.88 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG--------------EVAFVFQEP-RLMPWLTVEQNIGF--------SDDVgydKAW 57
Cdd:PRK13636 45 KSTLFQNLNGILKPSSGRILFDGKpidysrkglmklreSVGMVFQDPdNQLFSASVYQDVSFgavnlklpEDEV---RKR 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:PRK13636 122 VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHD 201
|
170
....*....|....*
gi 1864955972 138 VDEALYLSDRVLVMD 152
Cdd:PRK13636 202 IDIVPLYCDNVFVMK 216
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1-153 |
2.43e-14 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 68.71 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV-------------AFVFQEPRLMPWLTVEQNIgfsdDVGYD--KAWVAQLIDEV 65
Cdd:TIGR03410 39 KTTLLKTLMGLLPVKSGSIRLDGEDItklppheraragiAYVPQGREIFPRLTVEENL----LTGLAalPRRSRKIPDEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 -----GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDE 140
Cdd:TIGR03410 115 yelfpVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDF 194
|
170
....*....|...
gi 1864955972 141 ALYLSDRVLVMDN 153
Cdd:TIGR03410 195 ARELADRYYVMER 207
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-138 |
2.94e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 68.36 E-value: 2.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG--------GEVAF-------VFQEPRLMPWLTVEQNIGF--------SDDVgydKAW 57
Cdd:PRK10908 41 KSTLLKLICGIERPSAGKIWFSGhditrlknREVPFlrrqigmIFQDHHLLMDRTVYDNVAIpliiagasGDDI---RRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAftrmKLQDLLLQLAEHH---GIALLLV 134
Cdd:PRK10908 118 VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD----ALSEGILRLFEEFnrvGVTVLMA 193
|
....
gi 1864955972 135 THDV 138
Cdd:PRK10908 194 THDI 197
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-153 |
3.26e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 68.64 E-value: 3.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAfvfqepRLMPW------------------LTVEQNIG-----FSDDVGYDKAW 57
Cdd:PRK13548 41 KSTLLRALSGELSPDSGEVRLNGRPLA------DWSPAelarrravlpqhsslsfpFTVEEVVAmgrapHGLSRAEDDAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGL------YSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIAL 131
Cdd:PRK13548 115 VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqlwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAV 194
|
170 180
....*....|....*....|..
gi 1864955972 132 LLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK13548 195 IVVLHDLNLAARYADRIVLLHQ 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-151 |
3.41e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 68.89 E-value: 3.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGL---------EKDYQGELLQGGGEVA-----------FVFQEPRLMPWLTVEQNIgFSDDVGYDKAW--- 57
Cdd:PRK09984 43 KSTLLRHLSGLitgdksagsHIELLGRTVQREGRLArdirksrantgYIFQQFNLVNRLSVLENV-LIGALGSTPFWrtc 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 -----------VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEH 126
Cdd:PRK09984 122 fswftreqkqrALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQN 201
|
170 180
....*....|....*....|....*
gi 1864955972 127 HGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK09984 202 DGITVVVTLHQVDYALRYCERIVAL 226
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1-136 |
3.49e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.79 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL-LQGGGEVAFVFQEPrLMPWLTVEQnigfsddvgydkawvaQLIdevgltgfgqaLP--KA 77
Cdd:cd03223 40 KSSLFRALAGLWPWGSGRIgMPEGEDLLFLPQRP-YLPLGTLRE----------------QLI-----------YPwdDV 91
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDaftrMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRLYQLLKELGITVISVGH 146
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-151 |
6.54e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.11 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 23 GGEVAFVFQEP--RLMPWLTVEQNIGFS----DDVGYDKAWVA--QLIDEVGLTGFGQAL---PKALSGGMAQRVAIARG 91
Cdd:PRK10261 103 GADMAMIFQEPmtSLNPVFTVGEQIAESirlhQGASREEAMVEakRMLDQVRIPEAQTILsryPHQLSGGMRQRVMIAMA 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 92 LYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-152 |
6.79e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.32 E-value: 6.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG----------------GEVAFVFQ--EPRLMPWLTVE------QNIGFSDDVGYDKA 56
Cdd:PRK13641 46 KSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrKKVSLVFQfpEAQLFENTVLKdvefgpKNFGFSEDEAKEKA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 wvAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLL--QLAEHhgiALLL 133
Cdd:PRK13641 126 --LKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKdyQKAGH---TVIL 200
|
170
....*....|....*....
gi 1864955972 134 VTHDVDEALYLSDRVLVMD 152
Cdd:PRK13641 201 VTHNMDDVAEYADDVLVLE 219
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
75-151 |
7.69e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 7.69e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864955972 75 PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK09473 159 PHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVM 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-151 |
7.98e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.72 E-value: 7.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG--------------EVAFVFQEPRLMPWLT-VEQNIGFS-DDVGYDKAWVAQLIDE 64
Cdd:PRK13638 40 KSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllalrqQVATVFQDPEQQIFYTdIDSDIAFSlRNLGVPEAEITRRVDE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 ----VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDE 140
Cdd:PRK13638 120 altlVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDL 198
|
170
....*....|.
gi 1864955972 141 ALYLSDRVLVM 151
Cdd:PRK13638 199 IYEISDAVYVL 209
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-156 |
8.00e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.68 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGEL-LQGGGEVAFVFQEPRlMPWLTVEQNIGFSDDVG-YDKAWVAQLIDEVGLTGFGQAL---- 74
Cdd:COG4178 402 KSTLLRAIAGLWPYGSGRIaRPAGARVLFLPQRPY-LPLGTLREALLYPATAEaFSDAELREALEAVGLGHLAERLdeea 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 75 --PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAftrmKLQDLLLQL--AEHHGIALLLVTHDVDEALYlSDRVLV 150
Cdd:COG4178 481 dwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE----ENEAALYQLlrEELPGTTVISVGHRSTLAAF-HDRVLE 555
|
....*.
gi 1864955972 151 MDNRPS 156
Cdd:COG4178 556 LTGDGS 561
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-151 |
8.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 68.11 E-value: 8.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 6 RIVAGLEKDYQGELLQGggEVAFVFQEPRLMPWL-TVEQNIGFSD-DVGYDKAW----VAQLIDEVGL-TGFGQALPKAL 78
Cdd:PRK13645 74 AIPANLKKIKEVKRLRK--EIGLVFQFPEYQLFQeTIEKDIAFGPvNLGENKQEaykkVPELLKLVQLpEDYVKRSPFEL 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 79 SGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-152 |
9.10e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 67.45 E-value: 9.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG-EVAFVFQEPRLMPW--LTVEQNIGFSDdvGYDKAWVAQLIDEVGLTGFGQALPKA 77
Cdd:PRK09544 43 KSTLVRVVLGLVAPDEGVIKRNGKlRIGYVPQKLYLDTTlpLTVNRFLRLRP--GTKKEDILPALKRVQAGHLIDAPMQK 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVMD 152
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-163 |
1.42e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 68.21 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA----------------FVFQEPRLMPWLTVEQNI-------GFSDDVGYDKAw 57
Cdd:PRK10535 47 KSTLMNILGCLDKPTSGTYRVAGQDVAtldadalaqlrrehfgFIFQRYHLLSHLTAAQNVevpavyaGLERKQRLLRA- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 vAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHD 137
Cdd:PRK10535 126 -QELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHD 203
|
170 180 190
....*....|....*....|....*....|..
gi 1864955972 138 VDEALYlSDRVL------VMDNRPSSIRQELA 163
Cdd:PRK10535 204 PQVAAQ-AERVIeirdgeIVRNPPAQEKVNVA 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-146 |
1.44e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 67.11 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 26 VAFVFQEPRLMPwLTVEQNIGFSDDV-GY--------DKAW-VAQLIDEVG--LTGFGQALpkalSGGMAQRVAIARGLY 93
Cdd:PRK14243 93 IGMVFQKPNPFP-KSIYDNIAYGARInGYkgdmdelvERSLrQAALWDEVKdkLKQSGLSL----SGGQQQRLCIARAIA 167
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 94 SRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIalLLVTHDVDEALYLSD 146
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQAARVSD 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
23-153 |
1.83e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.81 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 23 GGEVAFVFQEP--RLMPWLTVEQNI--------GFSDDVGydKAWVAQLIDEVGLTGFGQAL---PKALSGGMAQRVAIA 89
Cdd:PRK15134 91 GNKIAMIFQEPmvSLNPLHTLEKQLyevlslhrGMRREAA--RGEILNCLDRVGIRQAAKRLtdyPHQLSGGERQRVMIA 168
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 90 RGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQN 232
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-148 |
2.07e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 66.40 E-value: 2.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 25 EVAFVFQEPRLMPWLTVEQNIGF----------SDDVGYDKAWV---AQLIDEVG--LTGFgqalPKALSGGMAQRVAIA 89
Cdd:PRK14267 86 EVGMVFQYPNPFPHLTIYDNVAIgvklnglvksKKELDERVEWAlkkAALWDEVKdrLNDY----PSNLSGGQRQRLVIA 161
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 90 RGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIalLLVTHDVDEALYLSDRV 148
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSPAQAARVSDYV 218
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
76-151 |
2.09e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 2.09e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864955972 76 KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK15439 402 RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-153 |
2.57e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 66.67 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQ--------EPRLMPWLTVEQNI-------GFSDDVGydKAWVAQLIDEV 65
Cdd:COG4152 40 KTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigylpeERGLYPKMKVGEQLvylarlkGLSKAEA--KRRADEWLERL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLS 145
Cdd:COG4152 118 GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEELC 196
|
....*...
gi 1864955972 146 DRVLVMDN 153
Cdd:COG4152 197 DRIVIINK 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-153 |
5.31e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 65.45 E-value: 5.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQ------GELLQGGG------------EVAFVFQEPRLMPWLTVEQNIGF---SDDVGyDKAWVA 59
Cdd:PRK14246 49 KSTLLKVLNRLIEIYDskikvdGKVLYFGKdifqidaiklrkEVGMVFQQPNPFPHLSIYDNIAYplkSHGIK-EKREIK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDE----VGL----TGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHhgIAL 131
Cdd:PRK14246 128 KIVEEclrkVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAI 205
|
170 180
....*....|....*....|..
gi 1864955972 132 LLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK14246 206 VIVSHNPQQVARVADYVAFLYN 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-151 |
6.33e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.27 E-value: 6.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 29 VFQEPR--LMPWLTVEQNIGFSDDVGYD-------KAWVAQLIDEVGLTGFG-QALPKALSGGMAQRVAIARGLYSRPQV 98
Cdd:PRK15134 367 VFQDPNssLNPRLNVLQIIEEGLRVHQPtlsaaqrEQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSL 446
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 99 LLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-151 |
8.07e-13 |
|
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: 66.19 E-value: 8.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQEPR-----------LMPWLTVEQNIGFSDDVGyDKAW-VAQL-----ID 63
Cdd:TIGR01257 969 KTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRqslgmcpqhniLFHHLTVAEHILFYAQLK-GRSWeEAQLemeamLE 1047
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 64 EVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLaeHHGIALLLVTHDVDEALY 143
Cdd:TIGR01257 1048 DTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADL 1125
|
....*...
gi 1864955972 144 LSDRVLVM 151
Cdd:TIGR01257 1126 LGDRIAII 1133
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1-153 |
8.14e-13 |
|
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: 63.39 E-value: 8.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAfvfqeprlmPWLTVEqnigFSDDVGYdkawVAQlidEVGLTGfGQALPKALSG 80
Cdd:cd03246 41 KSTLARLILGLLRPTSGRVRLDGADIS---------QWDPNE----LGDHVGY----LPQ---DDELFS-GSIAENILSG 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 81 GMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVdEALYLSDRVLVMDN 153
Cdd:cd03246 100 GQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRP-ETLASADRILVLED 170
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
78-151 |
1.09e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 65.34 E-value: 1.09e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQ-QGVAIIVISSELPEVLGLSDRVLVM 478
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
78-151 |
1.56e-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: 65.23 E-value: 1.56e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQ-EGVAIIVVSSELAEVLGLSDRVLVI 476
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-148 |
1.70e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.78 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDY-----QGELLQGGGE------------VAFVFQEPRLMPWLTVEQNIGFS---DDVGYDKA---- 56
Cdd:PRK14247 42 KSTLLRVFNRLIELYpearvSGEVYLDGQDifkmdvielrrrVQMVFQIPNPIPNLSIFENVALGlklNRLVKSKKelqe 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 ---WV---AQLIDEVglTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHhgIA 130
Cdd:PRK14247 122 rvrWAlekAQLWDEV--KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MT 197
|
170
....*....|....*...
gi 1864955972 131 LLLVTHDVDEALYLSDRV 148
Cdd:PRK14247 198 IVLVTHFPQQAARISDYV 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
25-151 |
1.98e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.88 E-value: 1.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 25 EVAFVFQEP--RLMPWLTVEQNI-------GFSDDVGYDKAwVAQLIDEVGLT-GFGQALPKALSGGMAQRVAIARGLYS 94
Cdd:PRK10261 402 DIQFIFQDPyaSLDPRQTVGDSImeplrvhGLLPGKAAAAR-VAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALAL 480
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1864955972 95 RPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVM 537
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1-154 |
3.23e-12 |
|
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: 61.31 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEvafvfqeprlmpwltveqnigfsdDVGYdkawVAQLidevgltgfgqalpkalSG 80
Cdd:cd03221 39 KSTLLKLIAGELEPDEGIVTWGSTV------------------------KIGY----FEQL-----------------SG 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864955972 81 GMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDlllQLAEHHGiALLLVTHD---VDEalyLSDRVLVMDNR 154
Cdd:cd03221 74 GEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEE---ALKEYPG-TVILVSHDryfLDQ---VATKIIELEDG 143
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-153 |
4.08e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.18 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 26 VAFVFQEPRLMPwLTVEQNIGFSD-DVGYDKA----WVAQLIDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQVL 99
Cdd:PRK13651 109 VVFQFAEYQLFE-QTIEKDIIFGPvSMGVSKEeakkRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFL 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 100 LLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK13651 188 VFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-152 |
4.71e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.08 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE-------------VAFVFQEPRL-MPWLTVEQNIGFS-DDVGYDKAWVAQLID-- 63
Cdd:PRK13644 41 KSTLALHLNGLLRPQKGKVLVSGIDtgdfsklqgirklVGIVFQNPETqFVGRTVEEDLAFGpENLCLPPIEIRKRVDra 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 64 --EVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEa 141
Cdd:PRK13644 121 laEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEE- 198
|
170
....*....|.
gi 1864955972 142 LYLSDRVLVMD 152
Cdd:PRK13644 199 LHDADRIIVMD 209
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1-163 |
5.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 62.84 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE----------------VAFVFQEPRLMPWL-TVEQNIGFS-DDVGYDKAWVAQLI 62
Cdd:PRK13649 46 KSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikqirkkVGLVFQFPESQLFEeTVLKDVAFGpQNFGVSQEEAEALA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DE-VGLTGFGQAL----PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLaEHHGIALLLVTHD 137
Cdd:PRK13649 126 REkLALVGISESLfeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHL 204
|
170 180 190
....*....|....*....|....*....|...
gi 1864955972 138 VDEALYLSDRVLVMD-------NRPSSIRQELA 163
Cdd:PRK13649 205 MDDVANYADFVYVLEkgklvlsGKPKDIFQDVD 237
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-136 |
5.92e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 5.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQEPR---------LMPWLTVEQNIGFSDDV-GYDKAWVAQLIDEVGLTGF 70
Cdd:PRK13539 41 KTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghrnaMKPALTVAENLEFWAAFlGGEELDIAAALEAVGLAPL 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 71 GQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTrmklQDLLLQLAEHH----GIAlLLVTH 136
Cdd:PRK13539 121 AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA----VALFAELIRAHlaqgGIV-IAATH 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
40-153 |
6.85e-12 |
|
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: 61.86 E-value: 6.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 40 TVEQNIGF-----SDDVGYDKAWVAQLIDEVgltgfgQALPKA-----------LSGGMAQRVAIARGLYSRPQVLLLDE 103
Cdd:cd03253 90 TIGYNIRYgrpdaTDEEVIEAAKAAQIHDKI------MRFPDGydtivgerglkLSGGEKQRVAIARAILKNPPILLLDE 163
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1864955972 104 PFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTHDVDEaLYLSDRVLVMDN 153
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKD 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-153 |
7.46e-12 |
|
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: 61.86 E-value: 7.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPWlTVEQNIGFSDDVGYDKAWVAqLIDEVGLT 68
Cdd:cd03254 42 KTTLINLLMRFYDPQKGQILIDGIDirdisrkslrsmIGVVLQDTFLFSG-TIMENIRLGRPNATDEEVIE-AAKEAGAH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPKA-----------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTHD 137
Cdd:cd03254 120 DFIMKLPNGydtvlgenggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHR 197
|
170
....*....|....*.
gi 1864955972 138 VDEALYlSDRVLVMDN 153
Cdd:cd03254 198 LSTIKN-ADKILVLDD 212
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
23-151 |
1.02e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 62.23 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 23 GGEVAFVFQEPR--LMPWLTV----EQNIGFSDDVGY-------DKAWVAQLIDEVGLTGFG---QALPKALSGGMAQRV 86
Cdd:COG4170 88 GREIAMIFQEPSscLDPSAKIgdqlIEAIPSWTFKGKwwqrfkwRKKRAIELLHRVGIKDHKdimNSYPHELTEGECQKV 167
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 87 AIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:COG4170 168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVL 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-162 |
1.22e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.51 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE-------------------VAFVFQEPRLMPWLTVEQN----IG--FSDDVGYDK 55
Cdd:TIGR03269 323 KTTLSKIIAGVLEPTSGEVNVRVGDewvdmtkpgpdgrgrakryIGILHQEYDLYPHRTVLDNlteaIGleLPDELARMK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 56 AwvaqlIDEVGLTGFGQ--------ALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHH 127
Cdd:TIGR03269 403 A-----VITLKMVGFDEekaeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEM 477
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1864955972 128 GIALLLVTHDVDEALYLSDRVLVMDN-------RPSSIRQEL 162
Cdd:TIGR03269 478 EQTFIIVSHDMDFVLDVCDRAALMRDgkivkigDPEEIVEEL 519
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1-171 |
1.34e-11 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 62.46 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA------------FVFQEPRLMPWlTVEQNIGFSDDVgyDKAWV---AQLideV 65
Cdd:COG4618 371 KSTLARLLVGVWPPTAGSVRLDGADLSqwdreelgrhigYLPQDVELFDG-TIAENIARFGDA--DPEKVvaaAKL---A 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLV 134
Cdd:COG4618 445 GVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKA-RGATVVVI 523
|
170 180 190
....*....|....*....|....*....|....*..
gi 1864955972 135 THDVdEALYLSDRVLVMDNRpssirqelAVELVHPRD 171
Cdd:COG4618 524 THRP-SLLAAVDKLLVLRDG--------RVQAFGPRD 551
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
76-151 |
1.59e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 76 KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVD----AFTRmklqDLLLQLAEHhGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:COG3845 401 RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIH----QRLLELRDA-GAAVLLISEDLDEILALSDRIAVM 475
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-153 |
1.74e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.26 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF------------VFQEPrLM---PWLTVEQNI----------GFSddVGYDK 55
Cdd:COG1101 45 KSTLLNAIAGSLPPDSGSILIDGKDVTKlpeykrakyigrVFQDP-MMgtaPSMTIEENLalayrrgkrrGLR--RGLTK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 56 AWVAQLIDEVGLTGFG-----QALPKALSGGmaQRVAIArgL----YSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEH 126
Cdd:COG1101 122 KRRELFRELLATLGLGlenrlDTKVGLLSGG--QRQALS--LlmatLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEE 197
|
170 180
....*....|....*....|....*..
gi 1864955972 127 HGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:COG1101 198 NNLTTLMVTHNMEQALDYGNRLIMMHE 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
26-152 |
1.95e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 61.40 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 26 VAFVFQEPRLMPWL-TVEQNIGFSD-DVGYDKAWVAQL----IDEVGL-TGFGQALPKALSGGMAQRVAIARGLYSRPQV 98
Cdd:PRK13631 118 VSMVFQFPEYQLFKdTIEKDIMFGPvALGVKKSEAKKLakfyLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 99 LLLDEPFSAVDAFTRMKLQDLLLQlAEHHGIALLLVTHDVDEALYLSDRVLVMD 152
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-151 |
2.03e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA-------------FVFQEPRLMPWLTVEQNIGF----SDDvgyDKAWVAQLID 63
Cdd:PRK15439 50 KSTLMKIIAGIVPPDSGTLEIGGNPCArltpakahqlgiyLVPQEPLLFPNLSVKENILFglpkRQA---SMQKMKQLLA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 64 EVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDA------FTRMK-LQDLllqlaehhGIALLLVTH 136
Cdd:PRK15439 127 ALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPaeterlFSRIReLLAQ--------GVGIVFISH 198
|
170
....*....|....*
gi 1864955972 137 DVDEALYLSDRVLVM 151
Cdd:PRK15439 199 KLPEIRQLADRISVM 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-153 |
2.34e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 60.90 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAfvfqepRLMPW------------------LTVEQNIGF-----SDDVGYDKAW 57
Cdd:COG4559 40 KSTLLKLLTGELTPSSGEVRLNGRPLA------AWSPWelarrravlpqhsslafpFTVEEVVALgraphGSSAAQDRQI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGL-------YSRPQVLLLDEPFSAVDaftrMKLQDLLLQLAE---HH 127
Cdd:COG4559 114 VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwepvDGGPRWLFLDEPTSALD----LAHQHAVLRLARqlaRR 189
|
170 180
....*....|....*....|....*.
gi 1864955972 128 GIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:COG4559 190 GGGVVAVLHDLNLAAQYADRILLLHQ 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-153 |
2.36e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.66 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE-------------VAFVFQEPRLMPWLTVEQNIG----FSDDVGYDK--AWVAQL 61
Cdd:PRK11614 44 KTTLLGTLCGDPRATSGRIVFDGKDitdwqtakimreaVAIVPEGRRVFSRMTVEENLAmggfFAERDQFQEriKWVYEL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEVgltgFGQALPKA--LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVD 139
Cdd:PRK11614 124 FPRL----HERRIQRAgtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLRE-QGMTIFLVEQNAN 198
|
170
....*....|....
gi 1864955972 140 EALYLSDRVLVMDN 153
Cdd:PRK11614 199 QALKLADRGYVLEN 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
75-154 |
2.51e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 75 PKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHhgIALLLVTHDVDEALYLSDR-VLVMDN 153
Cdd:PRK14271 161 PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRaALFFDG 238
|
.
gi 1864955972 154 R 154
Cdd:PRK14271 239 R 239
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-171 |
2.54e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.95 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG----------------GEVAFVFQEPRLMPWL-TVEQNI-----GFSDDVGYDKAWV 58
Cdd:PRK13646 46 KSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrKRIGMVFQFPESQLFEdTVEREIifgpkNFKMNLDEVKNYA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLT-GFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:PRK13646 126 HRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHD 205
|
170 180 190
....*....|....*....|....*....|....
gi 1864955972 138 VDEALYLSDRVLVMdnrpssiRQELAVELVHPRD 171
Cdd:PRK13646 206 MNEVARYADEVIVM-------KEGSIVSQTSPKE 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
79-152 |
2.54e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 60.14 E-value: 2.54e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 79 SGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQlAEHHGIALLLVTHDVDEALYLSDRVLVMD 152
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-153 |
3.35e-11 |
|
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: 60.04 E-value: 3.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 24 GEVAFVFQEPrlmpWL---TVEQNIGFSDDvgYDKAWVAQLIDEVGLTGFGQALPKA-----------LSGGMAQRVAIA 89
Cdd:cd03290 79 YSVAYAAQKP----WLlnaTVEENITFGSP--FNKQRYKAVTDACSLQPDIDLLPFGdqteigerginLSGGQRQRICVA 152
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 90 RGLYSRPQVLLLDEPFSAVDA-FTRMKLQDLLLQLAEHHGIALLLVTHDVdEALYLSDRVLVMDN 153
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIhLSDHLMQEGILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKD 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1-152 |
3.39e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.22 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEK---DYQGELLQGGGEV---------AFVFQEPRLMPWLTVEQNIGFS------DDVGYD--KAWVAQ 60
Cdd:TIGR00955 64 KTTLMNALAFRSPkgvKGSGSVLLNGMPIdakemraisAYVQQDDLFIPTLTVREHLMFQahlrmpRRVTKKekRERVDE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGL-----TGFGQA-LPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLV 134
Cdd:TIGR00955 144 VLQALGLrkcanTRIGVPgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTI 223
|
170
....*....|....*...
gi 1864955972 135 THDVDEALYLSDRVLVMD 152
Cdd:TIGR00955 224 HQPSSELFELFDKIILMA 241
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1-152 |
3.40e-11 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 60.04 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG-----------GEVAFVFQEPRLMPW-LTVEQNIGFSDDVgYD------KAWVAQLI 62
Cdd:cd03267 60 KTTTLKILSGLLQPTSGEVRVAGlvpwkrrkkflRRIGVVFGQKTQLWWdLPVIDSFYLLAAI-YDlpparfKKRLDELS 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEAL 142
Cdd:cd03267 139 ELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIE 218
|
170
....*....|
gi 1864955972 143 YLSDRVLVMD 152
Cdd:cd03267 219 ALARRVLVID 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-162 |
5.04e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.13 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG----------------GEVAFVFQEP--RLMPWLTVE------QNIGFSDDVGYDKA 56
Cdd:PRK13643 45 KSTLLQHLNGLLQPTEGKVTVGDivvsstskqkeikpvrKKVGVVFQFPesQLFEETVLKdvafgpQNFGIPKEKAEKIA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 wvAQLIDEVGLTG-FGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLaEHHGIALLLVT 135
Cdd:PRK13643 125 --AEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESI-HQSGQTVVLVT 201
|
170 180 190
....*....|....*....|....*....|....
gi 1864955972 136 HDVDEALYLSDRVLVMDN-------RPSSIRQEL 162
Cdd:PRK13643 202 HLMDDVADYADYVYLLEKghiiscgTPSDVFQEV 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-151 |
5.65e-11 |
|
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: 60.61 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGL--EKDYQGELLQGGGE-------------VAFVFQEPRLMPWLTVEQNIGFSDDVGYDKAWVA------ 59
Cdd:TIGR02633 40 KSTLMKILSGVypHGTWDGEIYWSGSPlkasnirdteragIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAynamyl 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 ---QLIDEVGLTGFGQALPKA-LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLaEHHGIALLLVT 135
Cdd:TIGR02633 120 rakNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYIS 198
|
170
....*....|....*.
gi 1864955972 136 HDVDEALYLSDRVLVM 151
Cdd:TIGR02633 199 HKLNEVKAVCDTICVI 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
60-151 |
6.51e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 59.52 E-value: 6.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVD 139
Cdd:PRK10895 120 ELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVR 198
|
90
....*....|..
gi 1864955972 140 EALYLSDRVLVM 151
Cdd:PRK10895 199 ETLAVCERAYIV 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
26-153 |
7.20e-11 |
|
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: 59.09 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 26 VAFVFQEPRLMPwLTVEQNIGFSDDVGYDKAwVAQLIDEVGLTGFGQALPKA-----------LSGGMAQRVAIARGLYS 94
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIRYGKPDATDEE-VEEAAKKANIHDFIMSLPDGydtlvgergsqLSGGQKQRIAIARALLR 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 95 RPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTHDvdealyLS-----DRVLVMDN 153
Cdd:cd03249 157 NPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHR------LStirnaDLIAVLQN 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-150 |
7.36e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.31 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF-------------VFQEPRLMPWLTVEQNI---------GFSdDVGYDKAWV 58
Cdd:PRK11288 43 KSTLLKILSGNYQPDAGSILIDGQEMRFasttaalaagvaiIYQELHLVPEMTVAENLylgqlphkgGIV-NRRLLNYEA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 59 AQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQL-AEhhGIALLLVTHD 137
Cdd:PRK11288 122 REQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELrAE--GRVILYVSHR 199
|
170
....*....|...
gi 1864955972 138 VDEALYLSDRVLV 150
Cdd:PRK11288 200 MEEIFALCDAITV 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
77-153 |
1.00e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 1.00e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864955972 77 ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSN 466
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
78-156 |
1.04e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 57.97 E-value: 1.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVMDNRPS 156
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPG 150
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1-152 |
1.11e-10 |
|
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: 58.64 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPRLMPwLTVEQNIGFS-DDVGYDKawVAQLIDEVGL 67
Cdd:cd03248 53 KSTVVALLENFYQPQGGQVLLDGkpisqyehkylhSKVSLVGQEPVLFA-RSLQDNIAYGlQSCSFEC--VKEAAQKAHA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 68 TGFGQALPKA-----------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHgiALLLVTH 136
Cdd:cd03248 130 HSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERR--TVLVIAH 207
|
170
....*....|....*.
gi 1864955972 137 DVdEALYLSDRVLVMD 152
Cdd:cd03248 208 RL-STVERADQILVLD 222
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1-153 |
1.19e-10 |
|
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: 57.71 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAFVFQeprlmpwlTVEQNIGFSDDVGYdkawvaqLIDevglTGFGQALPKALSG 80
Cdd:cd03247 41 KSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--------ALSSLISVLNQRPY-------LFD----TTLRNNLGRRFSG 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 81 GMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTHDVdEALYLSDRVLVMDN 153
Cdd:cd03247 102 GERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHL-TGIEHMDKILFLEN 171
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-155 |
1.21e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELlQGGGEVAFVFQEPRLMPWLTVEQNIGFSDDVGYDKAWV-AQLIDEVGLTGFGQALPKALS 79
Cdd:COG1245 379 KTTFAKILAGVLKPDEGEV-DEDLKISYKPQYISPDYDGTVEEFLRSANTDDFGSSYYkTEIIKPLGLEKLLDKNVKDLS 457
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 80 GGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDV---DealYLSDRVLVMDNRP 155
Cdd:COG1245 458 GGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIyliD---YISDRLMVFEGEP 533
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1-151 |
1.43e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGL--EKDYQGELLQGGGEVA--------FVFQEPRLMPWLTVEQNIGFSDDVGYDKAWVAQ--------LI 62
Cdd:PLN03211 107 KSTLLNALAGRiqGNNFTGTILANNRKPTkqilkrtgFVTQDDILYPHLTVRETLVFCSLLRLPKSLTKQekilvaesVI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTG-----FGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAeHHGIALLLVTHD 137
Cdd:PLN03211 187 SELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA-QKGKTIVTSMHQ 265
|
170
....*....|....*
gi 1864955972 138 VDEALY-LSDRVLVM 151
Cdd:PLN03211 266 PSSRVYqMFDSVLVL 280
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
78-163 |
1.85e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVMdnRPSS 157
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGVADRIVVM--REGR 473
|
....*.
gi 1864955972 158 IRQELA 163
Cdd:PRK11288 474 IAGELA 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
27-153 |
1.92e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 27 AFVFQEPRLMPwLTVEQNIGFS------DDVGYDKAWVAqlIDEvgltgFGQALP-----------KALSGGMAQRVAIA 89
Cdd:PTZ00265 1299 SIVSQEPMLFN-MSIYENIKFGkedatrEDVKRACKFAA--IDE-----FIESLPnkydtnvgpygKSLSGGQKQRIAIA 1370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 90 RGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVdEALYLSDRVLVMDN 153
Cdd:PTZ00265 1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1433
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-150 |
2.65e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.40 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGL--EKDYQGELLQGGGE-------------VAFVFQEPRLMPWLTVEQNI---------GFSDdvgYDKA 56
Cdd:PRK13549 44 KSTLMKVLSGVypHGTYEGEIIFEGEElqasnirdteragIAIIHQELALVKELSVLENIflgneitpgGIMD---YDAM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 WV--AQLIDEVGLtGFGQALP-KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLaEHHGIALLL 133
Cdd:PRK13549 121 YLraQKLLAQLKL-DINPATPvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIY 198
|
170
....*....|....*..
gi 1864955972 134 VTHDVDEALYLSDRVLV 150
Cdd:PRK13549 199 ISHKLNEVKAISDTICV 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
45-158 |
3.42e-10 |
|
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: 58.28 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 45 IGFSDDVGYDKAwvAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLA 124
Cdd:TIGR03269 138 IGYEGKEAVGRA--VDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAV 215
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1864955972 125 EHHGIALLLVTH-------DVDEALYLSDRVLVMDNRPSSI 158
Cdd:TIGR03269 216 KASGISMVLTSHwpeviedLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
54-151 |
3.44e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.49 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 54 DKAWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLL 133
Cdd:PRK10575 124 DREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA 203
|
90
....*....|....*...
gi 1864955972 134 VTHDVDEALYLSDRVLVM 151
Cdd:PRK10575 204 VLHDINMAARYCDYLVAL 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-153 |
4.51e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 57.44 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPW-LTVEQNIGFSD-DVGYDKAWVAQLIDE-- 64
Cdd:PRK13647 44 KSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrskVGLVFQDPDDQVFsSTVWDDVAFGPvNMGLDKDEVERRVEEal 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 --VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLaEHHGIALLLVTHDVDEAL 142
Cdd:PRK13647 124 kaVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAA 202
|
170
....*....|.
gi 1864955972 143 YLSDRVLVMDN 153
Cdd:PRK13647 203 EWADQVIVLKE 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-137 |
4.88e-10 |
|
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: 57.76 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPwLTVEQNIGFS-DDVGYDKAWVAqlIDEVGL 67
Cdd:TIGR02868 374 KSTLLATLAGLLDPLQGEVTLDGVPvssldqdevrrrVSVCAQDAHLFD-TTVRENLRLArPDATDEELWAA--LERVGL 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 68 TGFGQALP-----------KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTH 136
Cdd:TIGR02868 451 ADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITH 528
|
.
gi 1864955972 137 D 137
Cdd:TIGR02868 529 H 529
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-136 |
5.62e-10 |
|
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: 57.84 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQ-GGGEVAFVFQEPrLMPWLTVEQNIGFSDDV------GYDKAWVAQLIDEVGLT----- 68
Cdd:TIGR00954 491 KSSLFRILGELWPVYGGRLTKpAKGKLFYVPQRP-YMTLGTLRDQIIYPDSSedmkrrGLSDKDLEQILDNVQLThiler 569
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864955972 69 --GFG--QALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDaftrMKLQDLLLQLAEHHGIALLLVTH 136
Cdd:TIGR00954 570 egGWSavQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS----VDVEGYMYRLCREFGITLFSVSH 637
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-153 |
5.66e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.54 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG------------EVAFVFQEPRLMPWLTVEQNIG---------FSDDVGYDKAWVA 59
Cdd:PRK09536 42 KTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrRVASVPQDTSLSFEFDVRQVVEmgrtphrsrFDTWTETDRAAVE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVD 139
Cdd:PRK09536 122 RAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLD 200
|
170
....*....|....
gi 1864955972 140 EALYLSDRVLVMDN 153
Cdd:PRK09536 201 LAARYCDELVLLAD 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-153 |
6.02e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 56.63 E-value: 6.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV------------AFVFQEPRLMPWLTVEQNIGFsddvG---Y--------DKAW 57
Cdd:COG4604 40 KSTLLSMISRLLPPDSGEVLVDGLDVattpsrelakrlAILRQENHINSRLTVRELVAF----GrfpYskgrltaeDREI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDaftrMK----LQDLLLQLAEHHGIALLL 133
Cdd:COG4604 116 IDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLD----MKhsvqMMKLLRRLADELGKTVVI 191
|
170 180
....*....|....*....|
gi 1864955972 134 VTHDVDEALYLSDRVLVMDN 153
Cdd:COG4604 192 VLHDINFASCYADHIVAMKD 211
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
40-152 |
6.70e-10 |
|
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: 57.42 E-value: 6.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 40 TVEQNIGFSDDVGYDKAWVAQLIDEVGLTGFGQALPKA-----------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAV 108
Cdd:TIGR02203 421 TIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1864955972 109 DAFTRMKLQDLLLQLAEhhGIALLLVTHDVdEALYLSDRVLVMD 152
Cdd:TIGR02203 501 DNESERLVQAALERLMQ--GRTTLVIAHRL-STIEKADRIVVMD 541
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
78-152 |
7.37e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 57.15 E-value: 7.37e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRM----KLQDLLLQlaehhGIALLLVTHDVDEALYLSDRVLVMD 152
Cdd:PRK13536 173 LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHliweRLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLE 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-136 |
9.78e-10 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.04 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTllrIVAGLEKDYQ---GELLQGG------------GEVAFVFQEPRLMPWlTVEQNIGFSDDvGYDKAWVAQLIDEV 65
Cdd:TIGR00958 520 KST---VAALLQNLYQptgGQVLLDGvplvqydhhylhRQVALVGQEPVLFSG-SVRENIAYGLT-DTPDEEIMAAAKAA 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 66 GLTGFGQALPKA-----------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAftrmKLQDLLLQLAEHHGIALLLV 134
Cdd:TIGR00958 595 NAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLI 670
|
..
gi 1864955972 135 TH 136
Cdd:TIGR00958 671 AH 672
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
78-153 |
1.15e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 56.75 E-value: 1.15e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHG---IALLLVThdVDEAlylsDRVLVMDN 153
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTtlvIAHRLST--IVDA----DEILVLEA 567
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-153 |
1.46e-09 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG-----------GEVAFVFQEPRLMPWLTVEQNIG-----FSDDVGYDKAWVAQLIDE 64
Cdd:PRK13537 46 KTTTLRMLLGLTHPDAGSISLCGepvpsrarharQRVGVVPQFDNLDPDFTVRENLLvfgryFGLSAAAARALVPPLLEF 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 65 VGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYL 144
Cdd:PRK13537 126 AKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERL 204
|
....*....
gi 1864955972 145 SDRVLVMDN 153
Cdd:PRK13537 205 CDRLCVIEE 213
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-152 |
1.78e-09 |
|
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: 56.29 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG------------GEVAFVFQEPRLMPWlTVEQN--IGFSDDVGYDKAWVAQLIDEVG 66
Cdd:TIGR01193 513 KSTLAKLLVGFFQARSGEILLNGfslkdidrhtlrQFINYLPQEPYIFSG-SILENllLGAKENVSQDEIWAACEIAEIK 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 67 L------TGFGQALPK---ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHhgiALLLVTHD 137
Cdd:TIGR01193 592 DdienmpLGYQTELSEegsSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHR 668
|
170
....*....|....*
gi 1864955972 138 VDEAlYLSDRVLVMD 152
Cdd:TIGR01193 669 LSVA-KQSDKIIVLD 682
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
78-153 |
2.02e-09 |
|
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: 54.93 E-value: 2.02e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHG---IALLLVThdVDEAlylsDRVLVMDN 153
Cdd:cd03251 139 LSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNRTtfvIAHRLST--IENA----DRIVVLED 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-150 |
2.93e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGL--EKDYQGELLQGGGEVAF-------------VFQEPRLMPWLTVEQNI---------GFSD-DVGYDK 55
Cdd:NF040905 40 KSTLMKVLSGVypHGSYEGEILFDGEVCRFkdirdsealgiviIHQELALIPYLSIAENIflgnerakrGVIDwNETNRR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 56 AwvAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVT 135
Cdd:NF040905 120 A--RELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIIS 196
|
170
....*....|....*
gi 1864955972 136 HDVDEALYLSDRVLV 150
Cdd:NF040905 197 HKLNEIRRVADSITV 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-151 |
3.47e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGellQGGGEVafvfqeprlmPWLTVEQNIGFSDDVG--YDKAWVAQLIDEVGLTG--FGQALPK 76
Cdd:COG2401 69 KSTLLRLLAGALKGTPV---AGCVDV----------PDNQFGREASLIDAIGrkGDFKDAVELLNAVGLSDavLWLRRFK 135
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 77 ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:COG2401 136 ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-169 |
3.97e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.81 E-value: 3.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 23 GGEVAFVFQEPR--LMPWLTVE----QNI-GFS------DDVGYDKAWVAQLIDEVGLTGFGQAL---PKALSGGMAQRV 86
Cdd:PRK15093 88 GHNVSMIFQEPQscLDPSERVGrqlmQNIpGWTykgrwwQRFGWRKRRAIELLHRVGIKDHKDAMrsfPYELTEGECQKV 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 87 AIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVM---DNRPSSIRQELA 163
Cdd:PRK15093 168 MIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLycgQTVETAPSKELV 247
|
....*.
gi 1864955972 164 VELVHP 169
Cdd:PRK15093 248 TTPHHP 253
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-153 |
5.96e-09 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.58 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 26 VAFVFQEPRLMPwLTVEQNI-----GFSDDVGYDKAWVAQLID--EVGLTGFGQALP---KALSGGMAQRVAIARGLYSR 95
Cdd:PRK13657 411 IAVVFQDAGLFN-RSIEDNIrvgrpDATDEEMRAAAERAQAHDfiERKPDGYDTVVGergRQLSGGERQRLAIARALLKD 489
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 96 PQVLLLDEPFSAVDAFTRMKLQDLLLQLAehHG-----IALLLVThdVDEAlylsDRVLVMDN 153
Cdd:PRK13657 490 PPILILDEATSALDVETEAKVKAALDELM--KGrttfiIAHRLST--VRNA----DRILVFDN 544
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-156 |
1.06e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGgEVAFVFQEPRLMPWLTVEQNIGFSDDvGYDKAWV-AQLIDEVGLTGFGQALPKALS 79
Cdd:PRK13409 378 KTTFAKLLAGVLKPDEGEVDPEL-KISYKPQYIKPDYDGTVEDLLRSITD-DLGSSYYkSEIIKPLQLERLLDKNVKDLS 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 80 GGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDV---DealYLSDRVLVMDNRPS 156
Cdd:PRK13409 456 GGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIymiD---YISDRLMVFEGEPG 532
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-151 |
1.54e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 24 GEVAFVFQeprlMPWL---TVEQNIGFSDDVGYDKAWVAqlIDEVGLTGFGQALPKA-----------LSGGMAQRVAIA 89
Cdd:PLN03232 679 GSVAYVPQ----VSWIfnaTVRENILFGSDFESERYWRA--IDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMA 752
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1864955972 90 RGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQlAEHHGIALLLVTHDVdEALYLSDRVLVM 151
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQL-HFLPLMDRIILV 812
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
58-152 |
1.59e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHD 137
Cdd:NF033858 378 VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHF 457
|
90 100
....*....|....*....|...
gi 1864955972 138 VDEALyLSDR--------VLVMD 152
Cdd:NF033858 458 MNEAE-RCDRislmhagrVLASD 479
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
95-153 |
2.21e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.78 E-value: 2.21e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 95 RPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:COG4586 172 RPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDH 230
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
61-156 |
2.39e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDE 140
Cdd:cd03236 123 LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAV 201
|
90
....*....|....*.
gi 1864955972 141 ALYLSDRVLVMDNRPS 156
Cdd:cd03236 202 LDYLSDYIHCLYGEPG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
78-162 |
2.49e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.86 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVMDNrpSS 157
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD-DGKVILMVSSELPEIITVCDRIAVFCE--GR 486
|
....*
gi 1864955972 158 IRQEL 162
Cdd:PRK09700 487 LTQIL 491
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-153 |
3.75e-08 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 52.37 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG-EVAFVFQEPR-LMPWLTVEQNI-GFSDDVgyDKAWVAQLidevgLTGFG------ 71
Cdd:COG0488 354 KSTLLKLLAGELEPDSGTVKLGETvKIGYFDQHQEeLDPDKTVLDELrDGAPGG--TEQEVRGY-----LGRFLfsgdda 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 72 QALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAehhGiALLLVTHD---VDEalyLSDRV 148
Cdd:COG0488 427 FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDryfLDR---VATRI 499
|
....*
gi 1864955972 149 LVMDN 153
Cdd:COG0488 500 LEFED 504
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-151 |
4.23e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 51.55 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPWLTVEQNIGF------------SDDvgyDKA 56
Cdd:PRK11231 41 KSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarrLALLPQHHLTPEGITVRELVAYgrspwlslwgrlSAE---DNA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 WVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTH 136
Cdd:PRK11231 118 RVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLH 196
|
170
....*....|....*
gi 1864955972 137 DVDEALYLSDRVLVM 151
Cdd:PRK11231 197 DLNQASRYCDHLVVL 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
76-153 |
4.26e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 4.26e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1864955972 76 KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAeHHGIALLLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK10938 134 KYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLH-QSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
54-138 |
4.46e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.42 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 54 DKAWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLL 133
Cdd:PRK15056 119 DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRD-EGKTMLV 197
|
....*
gi 1864955972 134 VTHDV 138
Cdd:PRK15056 198 STHNL 202
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
26-153 |
4.48e-08 |
|
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: 50.96 E-value: 4.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 26 VAFVFQEPRLMPWlTVEQNIGFSDDVGYDKAWVAqlIDEVGLTGFGQALPKAL-----------SGGMAQRVAIARGLYS 94
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLDPFGEYSDEELWQA--LERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLR 156
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 95 RPQVLLLDEPFSAVDAFTRMKLQDLLLQlaEHHGIALLLVTHDVDeALYLSDRVLVMDN 153
Cdd:cd03244 157 KSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLD-TIIDSDRILVLDK 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1-152 |
8.81e-08 |
|
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: 50.56 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVA------------FVFQEPRLMPwLTVEQNIGFSDDvGYDKAWVAQLIDEVGLT 68
Cdd:cd03252 41 KSTLTKLIQRFYVPENGRVLVDGHDLAladpawlrrqvgVVLQENVLFN-RSIRDNIALADP-GMSMERVIEAAKLAGAH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTHD 137
Cdd:cd03252 119 DFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHR 196
|
170
....*....|....*
gi 1864955972 138 VdEALYLSDRVLVMD 152
Cdd:cd03252 197 L-STVKNADRIIVME 210
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
55-152 |
1.05e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.89 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 55 KAWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLV 134
Cdd:NF000106 122 RARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLT 200
|
90
....*....|....*...
gi 1864955972 135 THDVDEALYLSDRVLVMD 152
Cdd:NF000106 201 TQYMEEAEQLAHELTVID 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-152 |
1.06e-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: 49.95 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDY---QGELLQGG-----------GEVAFVFQEPRLMPWLTVEQNIGFSddvgydkawvaqlidevg 66
Cdd:cd03233 46 CSTLLKALANRTEGNvsvEGDIHYNGipykefaekypGEIIYVSEEDVHFPTLTVRETLDFA------------------ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 67 LTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLA-EHHGIALLLVTHDVDEALYLS 145
Cdd:cd03233 108 LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASDEIYDLF 187
|
....*..
gi 1864955972 146 DRVLVMD 152
Cdd:cd03233 188 DKVLVLY 194
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-110 |
1.31e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.89 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 24 GEVAFVFQeprlMPWL---TVEQNIGFSDDVGYDKAWVAqlIDEVGLTGFGQALPKA-----------LSGGMAQRVAIA 89
Cdd:PLN03130 679 GTVAYVPQ----VSWIfnaTVRDNILFGSPFDPERYERA--IDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMA 752
|
90 100
....*....|....*....|.
gi 1864955972 90 RGLYSRPQVLLLDEPFSAVDA 110
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDA 773
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
54-158 |
1.68e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.98 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 54 DKAWVAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLL 133
Cdd:PRK10253 120 DEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAA 199
|
90 100 110
....*....|....*....|....*....|..
gi 1864955972 134 VTHDVDEA-------LYLSDRVLVMDNRPSSI 158
Cdd:PRK10253 200 VLHDLNQAcryashlIALREGKIVAQGAPKEI 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-155 |
1.97e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 49.46 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG-----GE----VAFVFQEPRLMPWLTVEQNIGFSDDV-GYD-KAWVAQLIDEVGLTG 69
Cdd:PRK13543 50 KTTLLRVLAGLLHVESGQIQIDGktatrGDrsrfMAYLGHLPGLKADLSTLENLHFLCGLhGRRaKQMPGSALAIVGLAG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 70 FGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDaFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRVL 149
Cdd:PRK13543 130 YEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD-LEGITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRML 208
|
....*.
gi 1864955972 150 VMDNRP 155
Cdd:PRK13543 209 TLEAAA 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
78-169 |
2.34e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYlSDRVLVMDNRPSS 157
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNRERG 658
|
90
....*....|..
gi 1864955972 158 IRQELAVELVHP 169
Cdd:PTZ00265 659 STVDVDIIGEDP 670
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1-153 |
2.64e-07 |
|
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: 48.78 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKD--YQGELLQGGG--------EVAFVFQEPRLMPWLTVEQNIGFSddvgydkawvaqlidevgltgf 70
Cdd:cd03232 46 KTTLLDVLAGRKTAgvITGEILINGRpldknfqrSTGYVEQQDVHSPNLTVREALRFS---------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 71 gqALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLS-DRVL 149
Cdd:cd03232 104 --ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSASIFEKfDRLL 180
|
....
gi 1864955972 150 VMDN 153
Cdd:cd03232 181 LLKR 184
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
60-156 |
2.97e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhGIALLLVTHDVd 139
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL- 271
|
90
....*....|....*....
gi 1864955972 140 eAL--YLSDRVLVMDNRPS 156
Cdd:PRK13409 272 -AVldYLADNVHIAYGEPG 289
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
78-153 |
3.27e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 49.44 E-value: 3.27e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHgiALLLVTHDVdEALYLSDRVLVMDN 153
Cdd:PRK11160 476 LSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRL-TGLEQFDRICVMDN 548
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1-151 |
3.47e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLqGGGEVAFVFQEPRLMPwLTVEQNIGFSDD-----------VGYDKAWVAQL-------I 62
Cdd:PTZ00243 699 KSTLLQSLLSQFEISEGRVW-AERSIAYVPQQAWIMN-ATVRGNILFFDEedaarladavrVSQLEADLAQLgggleteI 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTgfgqalpkaLSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKL-QDLLlqLAEHHGIALLLVTHDVdEA 141
Cdd:PTZ00243 777 GEKGVN---------LSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVvEECF--LGALAGKTRVLATHQV-HV 844
|
170
....*....|
gi 1864955972 142 LYLSDRVLVM 151
Cdd:PTZ00243 845 VPRADYVVAL 854
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-110 |
5.16e-07 |
|
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: 49.17 E-value: 5.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGgEVAFVFQEPrlmpWL---TVEQNIGFSDDVgyDKAWVAQLIDEVGLTGFGQALPKA 77
Cdd:TIGR00957 677 KSSLLSALLAEMDKVEGHVHMKG-SVAYVPQQA----WIqndSLRENILFGKAL--NEKYYQQVLEACALLPDLEILPSG 749
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1864955972 78 -----------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDA 110
Cdd:TIGR00957 750 drteigekgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1-153 |
5.56e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.31 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELlQGGGEVAFVFQEPRLMPWlTVEQNIGFSddVGYDKAWVAQLIDEVGLTGFGQALPK---- 76
Cdd:cd03291 76 KTSLLMLILGELEPSEGKI-KHSGRISFSSQFSWIMPG-TIKENIIFG--VSYDEYRYKSVVKACQLEEDITKFPEkdnt 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 77 -------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKL-QDLLLQLAEHHgiALLLVTHDVdEALYLSDRV 148
Cdd:cd03291 152 vlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANK--TRILVTSKM-EHLKKADKI 228
|
....*
gi 1864955972 149 LVMDN 153
Cdd:cd03291 229 LILHE 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1-137 |
6.72e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGG-EVAFVFQE-PRLMPWLTVEQNIGFSDDV----GYD---KAWVAQLidevgltGFG 71
Cdd:TIGR03719 361 KSTLFRMITGQEQPDSGTIEIGETvKLAYVDQSrDALDPNKTVWEEISGGLDIiklgKREipsRAYVGRF-------NFK 433
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 72 ----QALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAehhGIAlLLVTHD 137
Cdd:TIGR03719 434 gsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA---GCA-VVISHD 499
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
76-156 |
8.33e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 76 KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVdeAL--YLSDRVLVMDN 153
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAE-EGKYVLVVEHDL--AIldYLADYVHILYG 287
|
...
gi 1864955972 154 RPS 156
Cdd:COG1245 288 EPG 290
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-153 |
1.48e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELlQGGGEVAFVFQEPRLMPWlTVEQNIGFSddVGYDKAWVAQLIDEVGLTGFGQALPK---- 76
Cdd:TIGR01271 465 KSSLLMMIMGELEPSEGKI-KHSGRISFSPQTSWIMPG-TIKDNIIFG--LSYDEYRYTSVIKACQLEEDIALFPEkdkt 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 77 -------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKL-QDLLLQLAEHHgiALLLVTHDVdEALYLSDRV 148
Cdd:TIGR01271 541 vlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNK--TRILVTSKL-EHLKKADKI 617
|
....*
gi 1864955972 149 LVMDN 153
Cdd:TIGR01271 618 LLLHE 622
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1-153 |
1.94e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 46.76 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEkDYQGELLQGGGEV------------AFVFQEPRLMPWLTVEQNIGFSDDVGYDKAWVAQLIDEvgLT 68
Cdd:COG4138 35 KSTLLARMAGLL-PGQGEILLNGRPLsdwsaaelarhrAYLSQQQSPPFAMPVFQYLALHQPAGASSEAVEQLLAQ--LA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 69 GFGQALPK------ALSGGMAQRVAIAR-------GLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVT 135
Cdd:COG4138 112 EALGLEDKlsrpltQLSGGEWQRVRLAAvllqvwpTINPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSS 190
|
170
....*....|....*...
gi 1864955972 136 HDVDEALYLSDRVLVMDN 153
Cdd:COG4138 191 HDLNHTLRHADRVWLLKQ 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
62-151 |
2.87e-06 |
|
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: 46.93 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEA 141
Cdd:TIGR01257 2055 IQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEEC 2133
|
90
....*....|
gi 1864955972 142 LYLSDRVLVM 151
Cdd:TIGR01257 2134 EALCTRLAIM 2143
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-136 |
3.81e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 45.33 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGG-----------GEVAFVFQEPRLMPWLTVEQNIGFSDDVGYDKAWVAQLIDEVGLTG 69
Cdd:PRK13540 40 KTTLLKLIAGLLNPEKGEILFERqsikkdlctyqKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEH 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 70 FGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDaftRMKLQDLLLQLAEH--HGIALLLVTH 136
Cdd:PRK13540 120 LIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSLLTIITKIQEHraKGGAVLLTSH 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1-153 |
4.18e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 45.69 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLekdyqgelLQGGGEVAFVFQEPRLMP---------WLTVEQNIGFSDDV----------GYDKAWVAQL 61
Cdd:PRK03695 35 KSTLLARMAGL--------LPGSGSIQFAGQPLEAWSaaelarhraYLSQQQTPPFAMPVfqyltlhqpdKTRTEAVASA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 62 IDEV-GLTGFGQALPK---ALSGGMAQRVAIA-------RGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIA 130
Cdd:PRK03695 107 LNEVaEALGLDDKLGRsvnQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIA 185
|
170 180
....*....|....*....|...
gi 1864955972 131 LLLVTHDVDEALYLSDRVLVMDN 153
Cdd:PRK03695 186 VVMSSHDLNHTLRHADRVWLLKQ 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-136 |
8.58e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 8.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE------------VAFVFQEPRLMPwLTVEQNIGFSDDVGYDKAWvaQLIDEVGLT 68
Cdd:PRK10790 380 KSTLASLLMGYYPLTEGEIRLDGRPlsslshsvlrqgVAMVQQDPVVLA-DTFLANVTLGRDISEEQVW--QALETVQLA 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 69 GFGQALPKA-----------LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHhgIALLLVTH 136
Cdd:PRK10790 457 ELARSLPDGlytplgeqgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAH 533
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1-141 |
8.60e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.50 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAfvfqEPR-------------------LMPWLTVEQNIGFSDDV-GYDKAWVAQ 60
Cdd:NF033858 40 KSSLLSLIAGARKIQQGRVEVLGGDMA----DARhrravcpriaympqglgknLYPTLSVFENLDFFGRLfGQDAAERRR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 61 LIDEV----GLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQL-AEHHGIALLLVT 135
Cdd:NF033858 116 RIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVAT 195
|
....*.
gi 1864955972 136 HDVDEA 141
Cdd:NF033858 196 AYMEEA 201
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
78-151 |
9.40e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 9.40e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVTHDVDEALYLSDRVLVM 151
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAA-EGKGVIVISSELPELLGMCDRIYVM 477
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
78-152 |
1.60e-05 |
|
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: 43.94 E-value: 1.60e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQlaEHHGIALLLVTHDVdEALYLSDRVLVMD 152
Cdd:cd03369 126 LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRL-RTIIDYDKILVMD 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-151 |
3.02e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.84 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF-------------VFQEPRLMPWLTVEQNI----GFSDDVG-------YDKA 56
Cdd:PRK10762 43 KSTMMKVLTGIYTRDAGSILYLGKEVTFngpkssqeagigiIHQELNLIPQLTIAENIflgrEFVNRFGridwkkmYAEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 57 wvAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPfsaVDAFTRMKLQDLL-----LQlAEHHGIal 131
Cdd:PRK10762 123 --DKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP---TDALTDTETESLFrvireLK-SQGRGI-- 194
|
170 180
....*....|....*....|
gi 1864955972 132 LLVTHDVDEALYLSDRVLVM 151
Cdd:PRK10762 195 VYISHRLKEIFEICDDVTVF 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
78-123 |
3.07e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 43.85 E-value: 3.07e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQL 123
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL 526
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
77-137 |
4.10e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 4.10e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864955972 77 ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLqlaEHHGiALLLVTHD 137
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK---TFQG-SIIFISHD 212
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
78-151 |
6.15e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.78 E-value: 6.15e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHgiALLLVTHDVdEALYLSDRVLVM 151
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRL-SALTEASEILVM 522
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
76-136 |
2.51e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 2.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1864955972 76 KALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhgiALLLVTH 136
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1-153 |
3.16e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 40.73 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEVAF------------VFQEPRLMPWLTVEQniGFSDDVGYDKAWVAQL--IDEVG 66
Cdd:PRK10522 362 KSTLAMLLTGLYQPQSGEILLDGKPVTAeqpedyrklfsaVFTDFHLFDQLLGPE--GKPANPALVEKWLERLkmAHKLE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 67 LTGfGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEpfSAVDA---FTRMKLQDLLLQLAEhHGIALLLVTHDvDEALY 143
Cdd:PRK10522 440 LED-GRISNLKLSKGQKKRLALLLALAEERDILLLDE--WAADQdphFRREFYQVLLPLLQE-MGKTIFAISHD-DHYFI 514
|
170
....*....|
gi 1864955972 144 LSDRVLVMDN 153
Cdd:PRK10522 515 HADRLLEMRN 524
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
60-155 |
3.40e-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: 39.61 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLT--GFGQALPkALSGGMAQRVAIARGLYSRPQ--VLLLDEPFSAVDAFTRMKLQDLLLQLAEhHGIALLLVT 135
Cdd:cd03238 69 QFLIDVGLGylTLGQKLS-TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLID-LGNTVILIE 146
|
90 100
....*....|....*....|
gi 1864955972 136 HDVDeALYLSDRVLVMDNRP 155
Cdd:cd03238 147 HNLD-VLSSADWIIDFGPGS 165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
76-137 |
3.83e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.32 E-value: 3.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1864955972 76 KALSGGMAQRVAIARgLYSRPQVLL-LDEPFSAVDAFTRMKLQDLllqLAEHHGiALLLVTHD 137
Cdd:PRK11147 439 KALSGGERNRLLLAR-LFLKPSNLLiLDEPTNDLDVETLELLEEL---LDSYQG-TVLLVSHD 496
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-151 |
4.50e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 40.15 E-value: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGE-------------VAFVFQEPRLMPWLTVEQNIgFSDDVGYDKAW---------- 57
Cdd:PRK09700 44 KSTLMKVLSGIHEPTKGTITINNINynkldhklaaqlgIGIIYQELSVIDELTVLENL-YIGRHLTKKVCgvniidwrem 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 58 ---VAQLIDEVGLTGFGQALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLaEHHGIALLLV 134
Cdd:PRK09700 123 rvrAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL-RKEGTAIVYI 201
|
170
....*....|....*..
gi 1864955972 135 THDVDEALYLSDRVLVM 151
Cdd:PRK09700 202 SHKLAEIRRICDRYTVM 218
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
78-146 |
7.90e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.46 E-value: 7.90e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864955972 78 LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDaftrMKLQDLLLQ-LAEHHGiALLLVTHD-------VDEALYLSD 146
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLD----LDAVEALIQgLVLFQG-GVLMVSHDehlisgsVDELWVVSE 699
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-132 |
8.24e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 1 KSTLLRIVAGLEKDYQGELLQGGGEV--------AFVFQEPRLMPWLTVEQNIGFSDDVGYDKAWVAQLIDEVGLTGFGQ 72
Cdd:PRK13541 39 KSSLLRMIAGIMQPSSGNIYYKNCNInniakpycTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLD 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 73 ALPKALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALL 132
Cdd:PRK13541 119 EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKANSGGIVLL 178
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
63-160 |
1.51e-03 |
|
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: 38.30 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQlaEHHGIAL 131
Cdd:cd03289 113 EEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ--AFADCTV 190
|
90 100
....*....|....*....|....*....
gi 1864955972 132 LLVTHDVdEALYLSDRVLVMDNrpSSIRQ 160
Cdd:cd03289 191 ILSEHRI-EAMLECQRFLVIEE--NKVRQ 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
78-151 |
1.61e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.27 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 78 LSGGMAQRVAIARGL---------YSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEALYLSDRV 148
Cdd:PRK13547 146 LSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRI 225
|
...
gi 1864955972 149 LVM 151
Cdd:PRK13547 226 AML 228
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
60-104 |
2.03e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 2.03e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1864955972 60 QLIDEVGLtGF---GQALPkALSGGMAQRVAIARGLYSRPQ---VLLLDEP 104
Cdd:COG0178 808 QTLQDVGL-GYiklGQPAT-TLSGGEAQRVKLASELSKRSTgktLYILDEP 856
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
63-132 |
2.76e-03 |
|
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: 37.97 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 63 DEVGLTGFGQALPK-----------ALSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQ--------L 123
Cdd:TIGR01271 1328 EEVGLKSVIEQFPDkldfvlvdggyVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQsfsnctviL 1407
|
....*....
gi 1864955972 124 AEHHGIALL 132
Cdd:TIGR01271 1408 SEHRVEALL 1416
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
67-141 |
2.81e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 37.69 E-value: 2.81e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 67 LTGFGQALPKA----LSGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEHHGIALLLVTHDVDEA 141
Cdd:PRK10938 387 ILGIDKRTADApfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
60-139 |
5.62e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 36.91 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1864955972 60 QLIDEVGLT--GFGQALPkALSGGMAQRVAIARGLYSR---PQVLLLDEPFSAVDAFTRMKLQDLLLQLAeHHGIALLLV 134
Cdd:TIGR00630 811 QTLCDVGLGyiRLGQPAT-TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLV-DKGNTVVVI 888
|
....*
gi 1864955972 135 THDVD 139
Cdd:TIGR00630 889 EHNLD 893
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
79-152 |
8.17e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 36.64 E-value: 8.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1864955972 79 SGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTrmklqDLLLQLA---EHHGIALLLVTHDVDeALYLSDRVLVMD 152
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRT-----DALIQKTireEFKSCTMLIIAHRLN-TIIDCDRILVLD 1446
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
79-137 |
8.74e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 36.30 E-value: 8.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1864955972 79 SGGMAQRVAIARGLYSRPQVLLLDEPFSAVDAFTRMKLQDLLLQLAEhhgiALLLVTHD 137
Cdd:PRK10636 432 SGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHD 486
|
|
| |
