|
Name |
Accession |
Description |
Interval |
E-value |
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-255 |
0e+00 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 501.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQNEG 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK11248 81 LLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 161 AFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGPGRVLERLPLEFARRYVAGEPVRSIKSDPLFIEQR 240
Cdd:PRK11248 161 AFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVERLPLNFARRFVAGESSRSIKSDPQFIAMR 240
|
250
....*....|....*
gi 493863201 241 EYVLSRVFEQREAFS 255
Cdd:PRK11248 241 EYVLSRVFEQREAFS 255
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-255 |
5.14e-164 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 454.32 E-value: 5.14e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGG----KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVF 76
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:COG4525 83 QKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 157 GALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGPGRVLERLPLEFARRYVAGEPVRSIKSDPLF 236
Cdd:COG4525 163 GALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLELDFSRRFLAGEDARAIKSDPAF 242
|
250
....*....|....*....
gi 493863201 237 IEQREYVLSRVFEQREAFS 255
Cdd:COG4525 243 IALREELLDIIFAQEEAEA 261
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-253 |
2.90e-121 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 345.92 E-value: 2.90e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY----GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVF 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:COG1116 87 QEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 157 GALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGPGRVLERLPLEFARryvagEPVRSIKSDPLF 236
Cdd:COG1116 167 GALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLPR-----PRDRELRTSPEF 241
|
250
....*....|....*..
gi 493863201 237 IEQREYVLSRVFEQREA 253
Cdd:COG1116 242 AALRAEILDLLREEAER 258
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-217 |
2.50e-114 |
|
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: 326.74 E-value: 2.50e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGK----PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQ 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:cd03293 81 QDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 158 ALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGPGRVLERLPLEF 217
Cdd:cd03293 161 ALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVEVDL 220
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-205 |
1.01e-85 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 258.87 E-value: 1.01e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--VFQ 77
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlPPEKRNVgmVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:COG3842 85 DYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLS 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 158 ALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG3842 165 ALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-205 |
2.28e-81 |
|
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: 243.20 E-value: 2.28e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---GVVFQN 78
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERrniGMVFQD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:cd03259 81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 159 LDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEG 207
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-205 |
5.53e-74 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 228.88 E-value: 5.53e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG--PGAERGV--VFQ 77
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnlPPRERRVgfVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:COG1118 83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 158 ALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-224 |
7.84e-71 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 221.10 E-value: 7.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--VFQ 77
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlPPKDRNIamVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:COG3839 83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863201 158 ALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGpgrVLERL--PLE-FAR---RYVAG 224
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDG---RIQQVgtPEElYDRpanLFVAG 232
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-244 |
1.25e-69 |
|
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: 213.87 E-value: 1.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQNEGLLPWRNVQENVAFGLQ 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 97 --LAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRL 174
Cdd:TIGR01184 81 rvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863201 175 WHETGKQVLLITHDIEEAVFMATELVLLSPGP----GRVLErLPLEFARRYVAgepvrsIKSDPLFIEQREYVL 244
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPaaniGQILE-VPFPRPRDRLE------VVEDPSYYDLRNEAL 227
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-205 |
1.08e-68 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 213.80 E-value: 1.08e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAE-R---GV 74
Cdd:COG1125 1 MIEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDlDPVElRrriGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAE--KRFIWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLDPEEyrDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 153 DEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-205 |
1.50e-68 |
|
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: 211.33 E-value: 1.50e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--VFQN 78
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlPPHKRPVntVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 159 LDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKG 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-188 |
1.93e-67 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 207.97 E-value: 1.93e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGK----PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER--- 72
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELarl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -----GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANP 147
Cdd:COG1136 84 rrrhiGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493863201 148 QLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHD 188
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-205 |
1.59e-66 |
|
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: 205.42 E-value: 1.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGG----KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER----- 72
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 ----GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:cd03255 81 rrhiGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDiEEAVFMATELVLLSPG 205
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHD-PELAEYADRIIELRDG 216
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-193 |
1.87e-64 |
|
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: 202.10 E-value: 1.87e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQNEGLL 82
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrelrrkkiSMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 83 PWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190
....*....|....*....|....*....|.
gi 493863201 163 TREQMQTLLLRLWHETGKQVLLITHDIEEAV 193
Cdd:cd03294 195 IRREMQDELLRLQAELQKTIVFITHDLDEAL 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-205 |
3.97e-64 |
|
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: 200.22 E-value: 3.97e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVV 75
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrkiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAE--KRFIWQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493863201 154 EPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNG 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-205 |
2.53e-61 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 197.09 E-value: 2.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE-RGV--VFQN 78
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEnRHVntVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 159 LDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK09452 175 LDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-205 |
3.37e-61 |
|
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: 192.55 E-value: 3.37e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA-ERGV--VFQNEG 80
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqERNVgfVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRNVQENVAFGLQLAgvAREQRLNTA------RDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVK--PRSERPPEAeirakvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 155 PFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-205 |
7.81e-59 |
|
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: 184.31 E-value: 7.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-------GV 74
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplrrriGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGLqlagvareqrlntardmlkkvglegaekrfiwqlSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:cd03229 81 VFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 155 PFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
2-205 |
1.51e-58 |
|
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: 189.48 E-value: 1.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER--GVVFQN 78
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRlPPQKRdyGIVFQS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 159 LDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:TIGR03265 165 LDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-205 |
1.69e-58 |
|
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: 184.77 E-value: 1.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--VFQN 78
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlPPKDRDIamVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 159 LDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG 207
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-205 |
1.74e-58 |
|
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: 185.23 E-value: 1.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVV 75
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrrkvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNegllPWR-----NVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLL 150
Cdd:COG1122 81 FQN----PDDqlfapTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 151 LLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAELADRVIVLDDG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
7.11e-58 |
|
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: 192.04 E-value: 7.11e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-----GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER--- 72
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlre 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -----GVVFQN--EGLLPWRNVQENVAFGLQLAGVA-REQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARAL 143
Cdd:COG1123 340 lrrrvQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863201 144 AANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLERLPLE 216
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMY--DGRIVEDGPTE 490
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-205 |
7.94e-57 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 181.44 E-value: 7.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQNEG 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LlPWR---NVQENVAFGLQ-----LAGVAREQRlNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:COG1121 86 V-DWDfpiTVRDVVLMGRYgrrglFRRPSRADR-EAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 153 DEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1121 164 DEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-205 |
8.11e-57 |
|
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: 181.33 E-value: 8.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER------- 72
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELyelrrri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVFQNEGLLPWRNVQENVAFGL-QLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-190 |
8.68e-57 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 180.63 E-value: 8.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER------- 72
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:COG2884 81 iGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIE 190
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEI-NRRGTTVLIATHDLE 198
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-205 |
1.69e-56 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 180.64 E-value: 1.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE-R---GVVFQ 77
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvRrriGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 158 ALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1131 161 GLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKG 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-205 |
2.26e-56 |
|
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: 179.20 E-value: 2.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVVF 76
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKElrrkvGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QN-EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 156 FGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03225 162 TAGLDPAGRRELLELLKKL-KAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-205 |
2.89e-56 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 180.00 E-value: 2.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---GVVFQNEG 80
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDrkiGFVFQHYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493863201 161 AFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:TIGR00968 163 AKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNG 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-205 |
2.80e-55 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 177.25 E-value: 2.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPAleAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--VFQ 77
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlPPAERPVsmLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFGLQ----LAGVAREQrlntARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:COG3840 79 ENNLFPHLTVAQNIGLGLRpglkLTAEQRAQ----VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493863201 154 EPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-205 |
4.50e-54 |
|
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: 177.30 E-value: 4.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 32 VLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNT 108
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLrhiNMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 109 ARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHD 188
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170
....*....|....*..
gi 493863201 189 IEEAVFMATELVLLSPG 205
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRKG 177
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-190 |
5.16e-54 |
|
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: 173.92 E-value: 5.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGK----PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER--- 72
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 ----GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:cd03258 81 rrriGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIE 190
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEME 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-205 |
7.19e-53 |
|
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: 171.77 E-value: 7.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER----GVV 75
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELarriAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGlLPWR-NVQENVAFG----LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLL 150
Cdd:COG1120 81 PQEPP-APFGlTVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 151 LLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-216 |
8.99e-53 |
|
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: 178.56 E-value: 8.99e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY--GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGTIHLEGKRVTGP-----GA 70
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELsealrGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 71 ERGVVFQNEG--LLPWRnVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:COG1123 84 RIGMVFQDPMtqLNPVT-VGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLERLPLE 216
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMD--DGRIVEDGPPE 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-216 |
1.45e-52 |
|
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: 170.75 E-value: 1.45e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYG----GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG--PGAERG- 73
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrrRKAFRRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 --VVFQN-EGLL-PWRNVQENVAFGLQLAGVAREQRlnTARDMLKKVGLEGAEK-RFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:COG1124 81 vqMVFQDpYASLhPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPSFLdRYPHQLSGGQRQRVAIARALILEPE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLspGPGRVLERLPLE 216
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM--QNGRIVEELTVA 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-160 |
3.26e-52 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 169.40 E-value: 3.26e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-------G 73
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDInklrrkvG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQNEGLLPWRNVQENVAFGL-QLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
....*...
gi 493863201 153 DEPFGALD 160
Cdd:COG1126 161 DEPTSALD 168
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-206 |
3.74e-52 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 168.43 E-value: 3.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGTIHLEGKRVTGPGAER---GV 74
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQrriGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGLQlAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493863201 155 PFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGP 206
Cdd:COG4136 160 PFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-205 |
6.83e-52 |
|
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: 168.67 E-value: 6.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGgKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---GVVFQN 78
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKrdiSYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:cd03299 80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 159 LDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNG 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-196 |
8.56e-52 |
|
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: 167.71 E-value: 8.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG-------AERGV 74
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKkninelrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGL-QLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 154 EPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEEA-------VFMA 196
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFArevadrvIFMD 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-205 |
9.39e-52 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 168.50 E-value: 9.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER----GVVF 76
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREArrqiGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 157 GALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG4555 161 NGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKG 208
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-190 |
2.07e-51 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 170.64 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGK----PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER--- 72
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 ----GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:COG1135 81 rrkiGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIE 190
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMD 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-202 |
2.55e-51 |
|
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: 166.91 E-value: 2.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGK----PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---- 72
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 ----GVVFQN--EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAE---KRFIWQLSGGQRQRVGIARAL 143
Cdd:cd03257 81 rkeiQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevlNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 144 AANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLL 202
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-190 |
1.24e-50 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 164.63 E-value: 1.24e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQNEgLLP 83
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQRR-SID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WR---NVQENVAFGLQ-----LAGVAREQRlNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:cd03235 81 RDfpiSVRDVVLMGLYghkglFRRLSKADK-AKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190
....*....|....*....|....*....|....*
gi 493863201 156 FGALDAFTREQMQTLLLRLwHETGKQVLLITHDIE 190
Cdd:cd03235 160 FAGVDPKTQEDIYELLREL-RREGMTILVVTHDLG 193
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-205 |
1.26e-50 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 169.63 E-value: 1.26e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--VFQ 77
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvPPYQRPInmMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 158 ALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-205 |
1.47e-50 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 166.01 E-value: 1.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIhLEGkrvTGPGAE-----RgVVF 76
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLAEaredtR-LMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPWRNVQENVafGLQLAGVAREQrlntARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:PRK11247 88 QDARLLPWKKVIDNV--GLGLKGQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 157 GALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK11247 162 GALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-211 |
2.19e-50 |
|
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: 164.98 E-value: 2.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER--------GVV 75
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrrmGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGLQ--LAGVAREQRlNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLRehTRLSEEEIR-EIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 154 EPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLspGPGRVLE 211
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL--YDGKIVA 217
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-224 |
3.32e-49 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 165.59 E-value: 3.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNIT--NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--V 75
Cdd:PRK11000 1 MASVTlrNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDvPPAERGVgmV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGLQLAGVA---REQRLNTARDMLKkvgLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:PRK11000 81 FQSYALYPHLSVAENMSFGLKLAGAKkeeINQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 153 DEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGP----GRvlerlPLEF----ARRYVAG 224
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRvaqvGK-----PLELyhypANRFVAG 232
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-205 |
3.79e-49 |
|
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: 160.92 E-value: 3.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLD-SGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG-------KRVTGPGAER--GVV 75
Cdd:cd03297 1 MLCVDIEKRLPDFTLKIDFDlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLPPQQRkiGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGLQlaGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:cd03297 81 FQQYALFPHLNVRENLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 156 FGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03297 159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDG 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-205 |
1.01e-48 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 164.10 E-value: 1.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA-ER--GVVFQNEG 80
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHArDRkvGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRNVQENVAFGLQLagVAREQRLNTA------RDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTV--LPRRERPNAAaikakvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 155 PFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
20-210 |
1.95e-47 |
|
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: 160.65 E-value: 1.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 20 INLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG-------KRVTGPgAER---GVVFQNEGLLPWRNVQE 89
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsaRGIFLP-PHRrriGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 90 NVAFGLQLAGVA-REQRLNTARDMLkkvGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
Cdd:COG4148 97 NLLYGRKRAPRAeRRISFDEVVELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEIL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 169 TLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVL 210
Cdd:COG4148 174 PYLERLRDELDIPILYVSHSLDEVARLADHVVLLE--QGRVV 213
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-188 |
4.13e-47 |
|
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: 155.95 E-value: 4.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGG----KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER----- 72
Cdd:TIGR02982 2 ISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQlvqlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 ---GVVFQNEGLLPWRNVQENVAFGLQL-AGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:TIGR02982 82 rriGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHD 188
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD 201
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-205 |
6.30e-47 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 156.02 E-value: 6.30e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA-------ERG 73
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVderlirqEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQNEGLLPWRNVQENVAFG-LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 153 DEPFGALDAFTREQ----MQTLLlrlwhETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK09493 161 DEPTSALDPELRHEvlkvMQDLA-----EEGMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-205 |
2.16e-46 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 2.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVVF 76
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrqvAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLlpWRN-VQENVAFGLQLagvaREQRLN--TARDMLKKVGLEGA--EKRFIwQLSGGQRQRVGIARALAANPQLLL 151
Cdd:COG4619 81 QEPAL--WGGtVRDNLPFPFQL----RERKFDreRALELLERLGLPPDilDKPVE-RLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-205 |
4.46e-46 |
|
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: 151.24 E-value: 4.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTgpgaergvvfqnegLLP 83
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA--------------KLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WRNVQENVAFglqlagvareqrlntardmlkkvglegaekrfIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:cd00267 68 LEELRRRIGY--------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 164 REQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd00267 116 RERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-188 |
6.56e-46 |
|
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: 152.25 E-value: 6.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER----GVVF 76
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPWRNVQENVAFGLQLAGVAREQRlnTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|..
gi 493863201 157 GALDAFTREQMQTLLLRlWHETGKQVLLITHD 188
Cdd:COG4133 160 TALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-205 |
6.80e-46 |
|
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: 151.43 E-value: 6.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTgpgaergvvfqnegLLP 83
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA--------------SLS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WRNVQENVAFGLQlagvareqrlntardMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:cd03214 68 PKELARKIAYVPQ---------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 164 REQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03214 133 QIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-190 |
1.56e-45 |
|
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: 151.61 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GV 74
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrreklGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 493863201 155 PFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIE 190
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPE 195
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-156 |
3.72e-45 |
|
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: 148.56 E-value: 3.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-----PGAERGVVFQNEGLLPWRNVQENV 91
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDderksLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 92 AFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIW----QLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-205 |
4.51e-45 |
|
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: 149.08 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER----GVVFQ 77
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVafglqlagvareqrlntardmlkkvglegaekrfiwQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 158 ALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03230 125 GLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-224 |
7.93e-45 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 153.85 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGK-PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG--PgAERGV--V 75
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEleP-ADRDIamV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGLQLAGVAR---EQRLNTARDMLKkvgLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:PRK11650 82 FQNYALYPHMSVRENMAYGLKIRGMPKaeiEERVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 153 DEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGpgrVLERL--PLEF----ARRYVAG 224
Cdd:PRK11650 159 DEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG---VAEQIgtPVEVyekpASTFVAS 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-214 |
8.96e-45 |
|
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: 150.02 E-value: 8.96e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQH-----GTIHLEGKRVTGPGAER---- 72
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 ---GVVFQNEGLLPwRNVQENVAFGLQLAGVAREQRLNT-ARDMLKKVGLEGAEKR--FIWQLSGGQRQRVGIARALAAN 146
Cdd:cd03260 81 rrvGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 147 PQLLLLDEPFGALDAFTREQMQTLLLRLWHETGkqVLLITHDIEEAVFMATELVLLSpgPGRVLERLP 214
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYT--IVIVTHNMQQAARVADRTAFLL--NGRLVEFGP 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
6-205 |
4.09e-44 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 152.18 E-value: 4.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTgpgaERGV-------VFQN 78
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT----HRSIqqrdicmVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 159 LDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-192 |
4.30e-44 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 149.05 E-value: 4.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER------ 72
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlRGRALrrlrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -GVVFQNEGLLPWRNVQENVAFGLQ--------LAGVAREQRLNTARDMLKKVGLEG-AEKRfIWQLSGGQRQRVGIARA 142
Cdd:COG3638 82 iGMIFQQFNLVPRLSVLTNVLAGRLgrtstwrsLLGLFPPEDRERALEALERVGLADkAYQR-ADQLSGGQQQRVAIARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEA 192
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLA 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
22-205 |
1.24e-43 |
|
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: 146.87 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 22 LTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT-GPGAERGV--VFQNEGLLPWRNVQENVAFGLQLA 98
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaAPPADRPVsmLFQENNLFAHLTVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 99 GVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHET 178
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAET 178
|
170 180
....*....|....*....|....*..
gi 493863201 179 GKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03298 179 KMTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-194 |
8.07e-43 |
|
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: 145.95 E-value: 8.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG----AERGVV- 75
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPphriARLGIAr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 -FQNEGLLPWRNVQENVAFGLQ-------------LAGVAREQRLNT--ARDMLKKVGLEGAEKRFIWQLSGGQRQRVGI 139
Cdd:COG0411 84 tFQNPRLFPELTVLENVLVAAHarlgrgllaallrLPRARREEREARerAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIeEAVF 194
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDM-DLVM 217
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-188 |
1.27e-42 |
|
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: 144.88 E-value: 1.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG--------AER-GVVFQNEGLLPWRNV 87
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedararlrARHvGFVFQSFQLLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLAGV--AREQrlntARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
Cdd:COG4181 108 LENVMLPLELAGRrdARAR----ARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGE 183
|
170 180
....*....|....*....|...
gi 493863201 166 QMQTLLLRLWHETGKQVLLITHD 188
Cdd:COG4181 184 QIIDLLFELNRERGTTLVLVTHD 206
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-190 |
1.33e-42 |
|
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: 144.31 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG------PGAER- 72
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlrgrqlPLLRRr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:TIGR02673 81 iGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLL 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIE 190
Cdd:TIGR02673 161 ADEPTGNLDPDLSERILDLLKRL-NKRGTTVIVATHDLS 198
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-205 |
3.91e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 143.57 E-value: 3.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALeaINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--VFQ 77
Cdd:PRK10771 1 MLKLTDITWLYHHLPMR--FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTtPPSRRPVsmLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFG----LQLAGVAREQRlntaRDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:PRK10771 79 ENNLFSHLTVAQNIGLGlnpgLKLNAAQREKL----HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493863201 154 EPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-205 |
9.71e-42 |
|
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: 142.71 E-value: 9.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYG-GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGAER------ 72
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRqlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVFQNEGLLPWRNVQENVAFGL--------QLAGVAREQRLNTARDMLKKVGLEG-AEKRfIWQLSGGQRQRVGIARAL 143
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDkAYQR-ADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493863201 144 AANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-210 |
1.06e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 142.95 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAE----RGVV 75
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWElarrRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGL-LPWRnVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALA-------ANP 147
Cdd:COG4559 81 PQHSSLaFPFT-VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493863201 148 QLLLLDEPFGALDafTREQMQTL-LLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVL 210
Cdd:COG4559 160 RWLFLDEPTSALD--LAHQHAVLrLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGrlvaqgtPEEVL 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-196 |
1.09e-41 |
|
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: 144.81 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGK----PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVP---YQHGTIHLEGKRVTG-PGAE- 71
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKlSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 72 ---RG----VVFQN--EGLLPWRNVQENVAFGLQLAGVA-REQRLNTARDMLKKVGLEGAEKR---FIWQLSGGQRQRVG 138
Cdd:COG0444 81 rkiRGreiqMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLsKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMA 196
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIA 218
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-190 |
2.29e-41 |
|
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: 141.42 E-value: 2.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG----AERGVV-- 75
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGLQ--------LAGVAREQR--LNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAA 145
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQartgsgllLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493863201 146 NPQLLLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIE 190
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMD 204
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-205 |
1.07e-40 |
|
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: 139.56 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV-TGPGAER---GVV 75
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARqslGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 156 FGALDAFTREQMQTLLLRLwhETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03263 161 TSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDG 208
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
12-190 |
6.11e-40 |
|
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: 137.15 E-value: 6.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG------PGAER--GVVFQNEGLLP 83
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraiPYLRRkiGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:cd03292 92 DRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDT 171
|
170 180
....*....|....*....|....*..
gi 493863201 164 REQMQTLLLRLwHETGKQVLLITHDIE 190
Cdd:cd03292 172 TWEIMNLLKKI-NKAGTTVVVATHAKE 197
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-205 |
1.09e-39 |
|
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: 137.43 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYG-GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER------- 72
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrklrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -GVVFQNEGLLPWRNVQENVAFGL--------QLAGVAREQRLNTARDMLKKVGLEG-AEKRfIWQLSGGQRQRVGIARA 142
Cdd:TIGR02315 81 iGMIFQHYNLIERLTVLENVLHGRlgykptwrSLLGRFSEEDKERALSALERVGLADkAYQR-ADQLSGGQQQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863201 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-205 |
1.99e-39 |
|
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: 136.14 E-value: 1.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 21 NLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGV--VFQNEGLLPWRNVQENVAFG--- 94
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGlAPYQRPVsmLFQENNLFAHLTVRQNIGLGlhp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 95 -LQLAGVAREQRLNTARdmlkKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLR 173
Cdd:TIGR01277 98 gLKLNAEQQEKVVDAAQ----QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|..
gi 493863201 174 LWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:TIGR01277 174 LCSERQRTLLMVTHHLSDARAIASQIAVVSQG 205
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-205 |
2.53e-39 |
|
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: 137.18 E-value: 2.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADY--GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG-------------KRVtgp 68
Cdd:TIGR04520 3 VENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGldtldeenlweirKKV--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 69 gaerGVVFQNegllPwRN------VQENVAFGLQLAGVARE---QRLNTArdmLKKVGLEGAEKRFIWQLSGGQRQRVGI 139
Cdd:TIGR04520 80 ----GMVFQN----P-DNqfvgatVEDDVAFGLENLGVPREemrKRVDEA---LKLVGMEDFRDREPHLLSGGQKQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVfMATELVLLSPG 205
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKG 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-205 |
1.16e-38 |
|
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: 133.86 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGeLLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE-RGVVfqneG 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlRRRI----G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRN-------VQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:cd03264 76 YLPQEFgvypnftVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493863201 154 EPFGALDAFTREQMQTLLLRLwhETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIVEDVESLCNQVAVLNKG 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-190 |
3.02e-38 |
|
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: 131.35 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GV 74
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkniAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPwRNVQENVafglqlagvareqrlntardmlkkvglegaekrfiwqLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:cd03228 81 VPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190
....*....|....*....|....*....|....*.
gi 493863201 155 PFGALDAFTREQMQTLLLRLwhETGKQVLLITHDIE 190
Cdd:cd03228 123 ATSALDPETEALILEALRAL--AKGKTVIVIAHRLS 156
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
14-205 |
3.08e-38 |
|
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: 134.50 E-value: 3.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER--------GVVFQN-EGLLPW 84
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKlkdlrkkvGLVFQFpEHQLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVAFGLQLAGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:TIGR04521 98 ETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKG 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 164 REQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:TIGR04521 178 RKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKG 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-205 |
7.18e-37 |
|
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: 129.32 E-value: 7.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-GVVFQNEG 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRiGYLPEERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493863201 161 AFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03269 161 PVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-212 |
7.90e-37 |
|
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: 136.43 E-value: 7.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVVFQ 77
Cdd:COG4988 339 LEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrrqiAWVPQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWrNVQENVAFG------------LQLAGVAR-----EQRLNTardmlkKVGLEGAekrfiwQLSGGQRQRVGIA 140
Cdd:COG4988 419 NPYLFAG-TIRENLRLGrpdasdeeleaaLEAAGLDEfvaalPDGLDT------PLGEGGR------GLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493863201 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHetGKQVLLITHDIEEAVFMATELVLlspGPGRVLER 212
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVL---DDGRIVEQ 552
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-211 |
8.01e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.13 E-value: 8.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTL---LNLIAgfVPyQHGTIHLEG-----KRVTGPGAER--- 72
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNLLE--MP-RSGTLNIAGnhfdfSKTPSDKAIRelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 ---GVVFQNEGLLPWRNVQEN-VAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:PRK11124 82 rnvGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLE 211
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYME--NGHIVE 221
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-192 |
8.55e-37 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 128.51 E-value: 8.55e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 11 YGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPyqhgtiHLEGKRVTGPGAERGVVFQNEGL---LPWRnV 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR------PTSGTVRRAGGARVAYVPQRSEVpdsLPLT-V 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGL--QLAGVAREQRLNTAR--DMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:NF040873 75 RDLVAMGRwaRRGLWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180
....*....|....*....|....*....
gi 493863201 164 REQMqTLLLRLWHETGKQVLLITHDIEEA 192
Cdd:NF040873 155 RERI-IALLAEEHARGATVVVVTHDLELV 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-205 |
4.87e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.35 E-value: 4.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAE----RGVV 75
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAElarrRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGL-LPWRnVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALA------ANPQ 148
Cdd:PRK13548 82 PQHSSLsFPFT-VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 149 LLLLDEPFGALDafTREQMQTL-LLR-LWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13548 161 WLLLDEPTSALD--LAHQHHVLrLARqLAHERGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-205 |
6.79e-36 |
|
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: 127.89 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFV-PYQHGTIHLEGKRVTG------------ 67
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpPTYGNDVRLFGERRGGedvwelrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 68 ---------PGAERG--VV----FQNEGLlpWRNVQEnvafglqlagvarEQRlNTARDMLKKVGLEG-AEKRFIwQLSG 131
Cdd:COG1119 83 vspalqlrfPRDETVldVVlsgfFDSIGL--YREPTD-------------EQR-ERARELLELLGLAHlADRPFG-TLSQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863201 132 GQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1119 146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-232 |
6.87e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.69 E-value: 6.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 21 NLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQNEGLLPWRNVQENV 91
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevrrkkiAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 92 AFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
Cdd:PRK10070 128 AFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDEL 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 172 LRLWHETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVLERLPLEFARRYVAGEPVRSIKS 232
Cdd:PRK10070 208 VKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGevvqvgtPDEILNNPANDYVRTFFRGVDISQVFS 275
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-190 |
1.32e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 129.54 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGK----PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG-----AE 71
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekelrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 72 R---GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:PRK11153 81 RrqiGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIE 190
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMD 202
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-211 |
2.05e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.28 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLL---NLIAgfVPyQHGTIHLEGKRV---TGPGAER------- 72
Cdd:COG4161 7 NINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLrvlNLLE--TP-DSGQLNIAGHQFdfsQKPSEKAirllrqk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -GVVFQNEGLLPWRNVQEN-VAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLL 150
Cdd:COG4161 84 vGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493863201 151 LLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLE 211
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVASQVVYME--KGRIIE 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-212 |
2.72e-35 |
|
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: 132.20 E-value: 2.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADY--GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERgvVFQNE 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD--LRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GLLPWRN------VQENVAFGLQLAGvarEQRLntaRDMLKKVGL----------------EGAEkrfiwQLSGGQRQRV 137
Cdd:COG4987 412 AVVPQRPhlfdttLRENLRLARPDAT---DEEL---WAALERVGLgdwlaalpdgldtwlgEGGR-----RLSGGERRRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHetGKQVLLITHDIEEAVFMATELVLlspGPGRVLER 212
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVL---EDGRIVEQ 550
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-188 |
3.39e-35 |
|
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: 132.65 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGAER---GV 74
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRrqiGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPwRNVQENVAFG------------LQLAGV-----AREQRLNTardmlkKVGLEGAekrfiwQLSGGQRQRV 137
Cdd:COG2274 554 VLQDVFLFS-GTIRENITLGdpdatdeeiieaARLAGLhdfieALPMGYDT------VVGEGGS------NLSGGQRQRL 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHetGKQVLLITHD 188
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHR 669
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
16-188 |
3.68e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 127.93 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE------RGV--VFQN--EGLLPWR 85
Cdd:COG4608 33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrplrRRMqmVFQDpyASLNPRM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 86 NVQENVAFGLQLAGVA-REQRLNTARDMLKKVGL--EGAEkRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
Cdd:COG4608 113 TVGDIIAEPLRIHGLAsKAERRERVAELLELVGLrpEHAD-RYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVS 191
|
170 180
....*....|....*....|....*.
gi 493863201 163 TREQMQTLLLRLWHETGKQVLLITHD 188
Cdd:COG4608 192 IQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-210 |
8.52e-35 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 125.25 E-value: 8.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLL---NLI----AGFVpyQHGTIHLEGKRVTGP--GAE 71
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLLeqpeAGTI--RVGDITIDTARSLSQqkGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 72 R------GVVFQNEGLLPWRNVQENVAFG-LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALA 144
Cdd:PRK11264 81 RqlrqhvGFVFQNFNLFPHRTVLENIIEGpVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863201 145 ANPQLLLLDEPFGALDA-FTREQMQTllLRLWHETGKQVLLITHDI-------EEAVFMaTELVLLSPGPGRVL 210
Cdd:PRK11264 161 MRPEVILFDEPTSALDPeLVGEVLNT--IRQLAQEKRTMVIVTHEMsfardvaDRAIFM-DQGRIVEQGPAKAL 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-216 |
1.06e-34 |
|
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: 127.54 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 20 INLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG-------KRVTGPGAER--GVVFQNEGLLPWRNVQEN 90
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlfdsrKGIFLPPEKRriGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAFGLQLAGVArEQRLNTARdMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
Cdd:TIGR02142 96 LRYGMKRARPS-ERRISFER-VIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493863201 171 LLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLERLPLE 216
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLE--DGRVAAAGPIA 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-160 |
1.26e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.76 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLL---NLIAGFVPYQH--GTIHLEGKRVTGPG----AER 72
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIPGARveGEILLDGEDIYDPDvdvvELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 ---GVVFQNEGLLPWrNVQENVAFGLQLAGVAREQRLN-TARDMLKKVGLegaekrfiWQ------------LSGGQRQR 136
Cdd:COG1117 92 rrvGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDeIVEESLRKAAL--------WDevkdrlkksalgLSGGQQQR 162
|
170 180
....*....|....*....|....
gi 493863201 137 VGIARALAANPQLLLLDEPFGALD 160
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALD 186
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
17-201 |
1.49e-34 |
|
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: 123.62 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQNEGLLPWRNV 87
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNEraklrnkklGFIYQFHHLLPDFTA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
Cdd:TIGR02211 101 LENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKII 180
|
170 180 190
....*....|....*....|....*....|....
gi 493863201 168 QTLLLRLWHETGKQVLLITHDIEEAVFMATELVL 201
Cdd:TIGR02211 181 FDLMLELNRELNTSFLVVTHDLELAKKLDRVLEM 214
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-212 |
3.17e-34 |
|
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: 122.33 E-value: 3.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---GVVFQN 78
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALrriGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQLAGVaREQRLNTARDMlkkVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:cd03268 81 PGFYPNLTARENLRLLARLLGI-RKKRIDEVLDV---VGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493863201 159 LDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLspGPGRVLER 212
Cdd:cd03268 157 LDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGII--NKGKLIEE 207
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-210 |
7.40e-34 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 121.88 E-value: 7.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 22 LTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQNEGLlPWR---NVQENVAFG-LQL 97
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQRHEF-AWDfpiSVAHTVMSGrTGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 98 AGVAREQRLN---TARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRL 174
Cdd:TIGR03771 80 IGWLRRPCVAdfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIEL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 493863201 175 WHEtGKQVLLITHDIEEAVFMATELVLLSpgpGRVL 210
Cdd:TIGR03771 160 AGA-GTAILMTTHDLAQAMATCDRVVLLN---GRVI 191
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-192 |
9.30e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 122.58 E-value: 9.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLL---NLIAGFVP--YQHGTIHLEGKRVTGPGA----- 70
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPevTITGSIVYNGHNIYSPRTdtvdl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 71 --ERGVVFQNEGLLPWrNVQENVAFGLQLAGVAREQRLNTARDMlkkvGLEGAEkrfIWQ------------LSGGQRQR 136
Cdd:PRK14239 85 rkEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEK----SLKGAS---IWDevkdrlhdsalgLSGGQQQR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETgkQVLLITHDIEEA 192
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQA 210
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-205 |
1.15e-33 |
|
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: 121.39 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER-----GVV 75
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHERaragiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENvafgLQLAGVAREQRlnTARDMLKKV-----GLEGAEKRFIWQLSGGQRQRVGIARALAANPQLL 150
Cdd:cd03224 81 PEGRRIFPELTVEEN----LLLGAYARRRA--KRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 151 LLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-155 |
2.61e-33 |
|
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: 120.86 E-value: 2.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE----RGVVF 76
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGllpwRN------VQENvafgLQLAGVAREQRLNTARDM---------LKkvglegaEKRFIW--QLSGGQRQRVGI 139
Cdd:COG0410 83 VPEG----RRifpsltVEEN----LLLGAYARRDRAEVRADLervyelfprLK-------ERRRQRagTLSGGEQQMLAI 147
|
170
....*....|....*.
gi 493863201 140 ARALAANPQLLLLDEP 155
Cdd:COG0410 148 GRALMSRPKLLLLDEP 163
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-174 |
4.79e-33 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.13 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-P---GAERGVvf 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlPmhkRARLGI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 qneGLLP-----WRN--VQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQL 149
Cdd:COG1137 81 ---GYLPqeasiFRKltVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180
....*....|....*....|....*
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRL 174
Cdd:COG1137 158 ILLDEPFAGVDPIAVADIQKIIRHL 182
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-189 |
7.38e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 119.80 E-value: 7.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER----GVV 75
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELakrlAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGlqlagvaR----EQRLnTARD------MLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAA 145
Cdd:COG4604 81 RQENHINSRLTVRELVAFG-------RfpysKGRL-TAEDreiideAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493863201 146 NPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:COG4604 153 DTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDI 196
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-191 |
9.17e-33 |
|
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: 119.18 E-value: 9.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER---GVvfq 77
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKRarlGI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 neGLLP-----WRN--VQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLL 150
Cdd:cd03218 78 --GYLPqeasiFRKltVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493863201 151 LLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEE 191
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRE 195
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-205 |
9.97e-33 |
|
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: 118.51 E-value: 9.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKP-ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVtgPGAER----GVVFQN 78
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI--KAKERrksiGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRN-VQENVAFGLQLAGVAREQrlntARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:cd03226 80 VDYQLFTDsVREELLLGLKELDAGNEQ----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 158 ALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03226 156 GLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-188 |
1.21e-32 |
|
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: 124.41 E-value: 1.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGG----KPALEAINLTLDSGELLVVLGPSGCGKT----TLLNLIAGFVPYQHGTIHLEGKRVTGP---- 68
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLsere 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 69 -----GAERGVVFQnE---GLLPWRNVQENVAFGLQL-AGVAREQRLNTARDMLKKVGLEGAEKRFIW---QLSGGQRQR 136
Cdd:COG4172 86 lrrirGNRIAMIFQ-EpmtSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493863201 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHD 188
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD 216
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-205 |
1.47e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.12 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLeGKRVTGPGAER----------GVVFQ-NEGLLPW 84
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkklkplrkkvGIVFQfPEHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVAFGLQLAGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 164 REQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13634 181 RKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKG 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-188 |
1.48e-32 |
|
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: 124.41 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTL----LNLIAgfvpyQHGTIHLEGKRVTG-PGAER-------GVVFQNE--GL 81
Cdd:COG4172 301 AVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGlSRRALrplrrrmQVVFQDPfgSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 82 LPWRNVQENVAFGLQL--AGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:COG4172 376 SPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190
....*....|....*....|....*....|
gi 493863201 159 LDAFTREQMQTLLLRLWHETGKQVLLITHD 188
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISHD 485
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
4.57e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.55 E-value: 4.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----G 73
Cdd:PRK13632 7 MIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEirkkiG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQNE-----GLlpwrNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:PRK13632 87 IIFQNPdnqfiGA----TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVfMATELVLLSPG 205
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-205 |
6.18e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 118.67 E-value: 6.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA--------ER 72
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRrrigylpeER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GvvfqnegLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:COG4152 81 G-------LYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 153 DEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG4152 154 DEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKG 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-205 |
8.28e-32 |
|
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: 116.32 E-value: 8.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER---GVVFQNEGL 81
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVRePREVRrriGIVFQDLSV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 82 LPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493863201 162 FTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
14-205 |
1.10e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 117.81 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG-----AERGVVFQN-EGLLPWRNV 87
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrRQVGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
Cdd:PRK13635 100 QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 493863201 168 QTLLLRLWHETGKQVLLITHDIEEAVFmATELVLLSPG 205
Cdd:PRK13635 180 LETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-199 |
1.82e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 116.07 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA---------ERGVVFQNEGLLPWRNV 87
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaelrnqKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
Cdd:PRK11629 105 LENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSI 184
|
170 180 190
....*....|....*....|....*....|..
gi 493863201 168 QTLLLRLWHETGKQVLLITHDIEEAVFMATEL 199
Cdd:PRK11629 185 FQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-191 |
4.44e-31 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 119.74 E-value: 4.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG---AER---GV 74
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSprdAQAagiAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGLQL--AGVAREQRLN-TARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPrrGGLIDWRAMRrRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEE 191
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDE 202
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-189 |
9.21e-31 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 113.82 E-value: 9.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG------PGAER- 72
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPFLRRq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:PRK10908 81 iGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493863201 152 LDEPFGALDaftrEQMQTLLLRLWHE---TGKQVLLITHDI 189
Cdd:PRK10908 161 ADEPTGNLD----DALSEGILRLFEEfnrVGVTVLMATHDI 197
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-205 |
1.46e-30 |
|
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: 112.26 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQH--GTIHLEGKRVT--GPGAERGVVFQNEGLLPWRNV 87
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDkrSFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLAGvareqrlntardmlkkvglegaekrfiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
Cdd:cd03213 100 RETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 493863201 168 QTLLLRLWHeTGKQVLLITHDIEEAVF-MATELVLLSPG 205
Cdd:cd03213 151 MSLLRRLAD-TGRTIICSIHQPSSEIFeLFDKLLLLSQG 188
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-189 |
2.09e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 114.01 E-value: 2.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGG---------KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGA 70
Cdd:PRK10419 3 LLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 71 ERG-------VVFQNE--GLLPWRNVQENVAFGLQ-LAGVAREQRLNTARDMLKKVGL--EGAEKRfIWQLSGGQRQRVG 138
Cdd:PRK10419 83 QRKafrrdiqMVFQDSisAVNPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLddSVLDKR-PPQLSGGQLQRVC 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDL 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-192 |
3.08e-30 |
|
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: 110.60 E-value: 3.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVtgpgaergvvfqnegl 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV---------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 82 lpwrnvqenvafglqlagvareqRLNTARDMLKKvGLEgaekrFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
Cdd:cd03216 65 -----------------------SFASPRDARRA-GIA-----MVYQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
|
170 180 190
....*....|....*....|....*....|.
gi 493863201 162 FTREQMQTLLLRLwHETGKQVLLITHDIEEA 192
Cdd:cd03216 116 AEVERLFKVIRRL-RAQGVAVIFISHRLDEV 145
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-187 |
7.89e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 7.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGAER---GVVFQNEGLLPwRN 86
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRdlTLESLRrqiGVVPQDTFLFS-GT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 87 VQENVAFG------------LQLAGVAR-----EQRLNTardmlkKVGLEGAekrfiwQLSGGQRQRVGIARALAANPQL 149
Cdd:COG1132 430 IRENIRYGrpdatdeeveeaAKAAQAHEfiealPDGYDT------VVGERGV------NLSGGQRQRIAIARALLKDPPI 497
|
170 180 190
....*....|....*....|....*....|....*...
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRLWHetGKQVLLITH 187
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMK--GRTTIVIAH 533
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-205 |
8.39e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 112.10 E-value: 8.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYG-G----KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER-- 72
Cdd:COG1101 1 MLELKNLSKTFNpGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKlPEYKRak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 --GVVFQN--EGLLPWRNVQENVA--------FGLQLaGVAREQRlNTARDMLKKVGLeGAEKRF---IWQLSGGQRQRV 137
Cdd:COG1101 81 yiGRVFQDpmMGTAPSMTIEENLAlayrrgkrRGLRR-GLTKKRR-ELFRELLATLGL-GLENRLdtkVGLLSGGQRQAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-205 |
9.37e-30 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.03 E-value: 9.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERgvVFQNEG 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWR-------NVQENVAFG----LQLAG-VAREQRLNTARDMLKKVGLEGAEKRfIWQLSGGQRQRVGIARALAANPQ 148
Cdd:PRK11231 80 LLPQHhltpegiTVRELVAYGrspwLSLWGrLSAEDNARVNQAMEQTRINHLADRR-LTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 149 LLLLDEPFGALDafTREQMQTL-LLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK11231 159 VVLLDEPTTYLD--INHQVELMrLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANG 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-190 |
1.77e-29 |
|
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: 109.87 E-value: 1.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 8 SADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKrvtgpgaeRGVVFQNegllPW-RN 86
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQE----PWiQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 87 --VQENVAFGLQLagvaREQRLNTA-------RDM-------LKKVGLEGAekrfiwQLSGGQRQRVGIARALAANPQLL 150
Cdd:cd03250 80 gtIRENILFGKPF----DEERYEKVikacalePDLeilpdgdLTEIGEKGI------NLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493863201 151 LLDEPFGALDAFTREQ-MQTLLLRLWHEtGKQVLLITHDIE 190
Cdd:cd03250 150 LLDDPLSAVDAHVGRHiFENCILGLLLN-NKTRILVTHQLQ 189
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-205 |
2.03e-29 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 110.15 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKP----ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV-TGPGAER--- 72
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEARrrl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 153 DEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
14-205 |
3.12e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAG-FVPYQ--HGTIHLEGKRVTGPGA----ER-GVVFQN-EGLLPW 84
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlLLPDDnpNSKITVDGITLTAKTVwdirEKvGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
Cdd:PRK13640 100 ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493863201 165 EQMQTLLLRLWHETGKQVLLITHDIEEAVfMATELVLLSPG 205
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDG 219
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-214 |
3.69e-29 |
|
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: 110.67 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY---------GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT---GP 68
Cdd:TIGR02769 2 LLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqldRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 69 GAER-----GVVFQN--EGLLPWRNVQENVAFGLQ-LAGVAREQRLNTARDMLKKVGLEGAE-KRFIWQLSGGQRQRVGI 139
Cdd:TIGR02769 82 QRRAfrrdvQLVFQDspSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDaDKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLERLP 214
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMD--KGQIVEECD 234
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-187 |
3.97e-29 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 108.74 E-value: 3.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVtgpGAERGVVFQN-- 78
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI---RRQRDEYHQDll 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 ---------EGLLPWrnvqENVAFGLQLAGVAREQRLNTArdmLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQL 149
Cdd:PRK13538 78 ylghqpgikTELTAL----ENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRlwH-ETGKQVLLITH 187
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQ--HaEQGGMVILTTH 187
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-250 |
5.14e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.60 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTgPGAER------GVVF 76
Cdd:PRK13647 7 VEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN-AENEKwvrskvGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QN-EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:PRK13647 86 QDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 156 FGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLerlplefarryVAGEPvrSIKSDPL 235
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRL-HNQGKTVIVATHDVDLAAEWADQVIVLK--EGRVL-----------AEGDK--SLLTDED 229
|
250
....*....|....*...
gi 493863201 236 FIEQ---REYVLSRVFEQ 250
Cdd:PRK13647 230 IVEQaglRLPLVAQIFED 247
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-160 |
6.00e-29 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 109.89 E-value: 6.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLL---NLIAgfVPYQhGTIHLEGKRV----TGPGA--- 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLrciNLLE--TPDS-GEIRVGGEEIrlkpDRDGElvp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 71 ------ER-----GVVFQNEGLLPWRNVQENVAFG-LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVG 138
Cdd:COG4598 85 adrrqlQRirtrlGMVFQSFNLWSHMTVLENVIEApVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180
....*....|....*....|..
gi 493863201 139 IARALAANPQLLLLDEPFGALD 160
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALD 186
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-196 |
8.97e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.85 E-value: 8.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVtgPGAERG------- 73
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI--PAMSRSrlytvrk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 ---VVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDM-LKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQL 149
Cdd:PRK11831 85 rmsMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMA 196
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIA 211
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1-211 |
1.91e-28 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 108.38 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKR------VTGPGAERGV 74
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaelelYQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEgllpWRNVQENVAFGLQL---AGVAREQRL------------NTARDMLKKVGLEGA----EKRfiwQLSGGQRQ 135
Cdd:TIGR02323 83 LMRTE----WGFVHQNPRDGLRMrvsAGANIGERLmaigarhygnirATAQDWLEEVEIDPTriddLPR---AFSGGMQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLE 211
Cdd:TIGR02323 156 RLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQ--QGRVVE 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-199 |
2.15e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 107.27 E-value: 2.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVF---Q 77
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYlghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NeGLLPWRNVQENVAFGLQLAGvareQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:PRK13539 82 N-AMKPALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493863201 158 ALDAFTREQMQTLLLRlwH-ETGKQVLLITHdIEEAVFMATEL 199
Cdd:PRK13539 157 ALDAAAVALFAELIRA--HlAQGGIVIAATH-IPLGLPGAREL 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
2.69e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 108.63 E-value: 2.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV----TGPGAER--- 72
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkKSLLEVRktv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVFQN-EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:PRK13639 81 GIVFQNpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-190 |
2.78e-28 |
|
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: 112.38 E-value: 2.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGK-PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGkrVTGPGAER-------G 73
Cdd:TIGR02857 322 LEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNG--VPLADADAdswrdqiA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQNEGLLPwRNVQENVAFG------------LQLAGVAreQRLNTARDML-KKVGLEGAEkrfiwqLSGGQRQRVGIA 140
Cdd:TIGR02857 400 WVPQHPFLFA-GTIAENIRLArpdasdaeireaLERAGLD--EFVAALPQGLdTPIGEGGAG------LSGGQAQRLALA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLRLwhETGKQVLLITHDIE 190
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLA 518
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-192 |
4.49e-28 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 106.79 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQNEGLLPWRNV 87
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklrakhvGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
|
170 180
....*....|....*....|....*
gi 493863201 168 QTLLLRLWHETGKQVLLITHDIEEA 192
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLA 210
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-188 |
4.93e-28 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 107.38 E-value: 4.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PG---AERGVV- 75
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGlPGhqiARMGVVr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 -FQNEGLLPWRNVQEN--VAFGLQ-----LAGV--------AREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGI 139
Cdd:PRK11300 85 tFQHVRLFREMTVIENllVAQHQQlktglFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHD 188
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-228 |
6.39e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.90 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT----GPGAERGVVF- 76
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRGIGYl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 -QNEGLLPWRNVQENVAFGLQL-AGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:PRK10895 84 pQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 155 PFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPGP----GRVLERLPLEFARRYVAGEPVR 228
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHliahGTPTEILQDEHVKRVYLGEDFR 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
16-189 |
1.18e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 108.13 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE------RGV--VFQNE--GLLPWR 85
Cdd:PRK11308 30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkllrQKIqiVFQNPygSLNPRK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 86 NV----QENVAFGLQLAGVAREQRlntARDMLKKVGLEgAE--KRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
Cdd:PRK11308 110 KVgqilEEPLLINTSLSAAERREK---ALAMMAKVGLR-PEhyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190
....*....|....*....|....*....|
gi 493863201 160 DAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK11308 186 DVSVQAQVLNLMMDLQQELGLSYVFISHDL 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-188 |
1.18e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 110.97 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQNEGLLPWRNV 87
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrehfGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180
....*....|....*....|.
gi 493863201 168 QTLLLRLwHETGKQVLLITHD 188
Cdd:PRK10535 184 MAILHQL-RDRGHTVIIVTHD 203
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-211 |
1.43e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGAERGVV---FQNEGLLPwRN 86
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIStlKPEIYRQQVsycAQTPTLFG-DT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 87 VQENVAFGLQLAGVAREQrlNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDP--AIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493863201 166 QMQTLLLRLWHETGKQVLLITHDIEEaVFMATELVLLSPGPGRVLE 211
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDE-INHADKVITLQPHAGEMQE 219
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-188 |
1.79e-27 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 110.14 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT----GPGAERGVVF 76
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSsldqDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPWRNVQENVAFGlqlAGVAREQRLntaRDMLKKVGLE--------------GAEKRFiwqLSGGQRQRVGIARA 142
Cdd:TIGR02868 415 AQDAHLFDTTVRENLRLA---RPDATDEEL---WAALERVGLAdwlralpdgldtvlGEGGAR---LSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493863201 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLRLwhETGKQVLLITHD 188
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-192 |
4.44e-27 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 104.66 E-value: 4.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER---GVVF- 76
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlPMHERarlGIGYl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 -QNEGLLPWRNVQENVAFGLQLAG-VAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:TIGR04406 82 pQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 493863201 155 PFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEA 192
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHL-KERGIGVLITDHNVRET 198
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-227 |
7.54e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.23 E-value: 7.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE---RGV--V 75
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARaasRRVasV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFG----LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:PRK09536 83 PQDTSLSFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 152 LDEPFGALDafTREQMQTL-LLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVL--ERLPLEF-ARR 220
Cdd:PRK09536 163 LDEPTASLD--INHQVRTLeLVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGrvraagpPADVLtaDTLRAAFdART 240
|
....*..
gi 493863201 221 YVAGEPV 227
Cdd:PRK09536 241 AVGTDPA 247
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-187 |
8.03e-27 |
|
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: 101.91 E-value: 8.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGAER---GV 74
Cdd:cd03246 1 LEVENVSFRYPGaePPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGdhvGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPwRNVQENVafglqlagvareqrlntardmlkkvglegaekrfiwqLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:cd03246 81 LPQDDELFS-GSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190
....*....|....*....|....*....|...
gi 493863201 155 PFGALDAfTREQMQTLLLRLWHETGKQVLLITH 187
Cdd:cd03246 123 PNSHLDV-EGERALNQAIAALKAAGATRIVIAH 154
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-193 |
9.43e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 104.78 E-value: 9.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGG------KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG------KRVTGP 68
Cdd:PRK13633 4 MIKCKNVSYKYESneesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 69 GAERGVVFQN-EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANP 147
Cdd:PRK13633 84 RNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 493863201 148 QLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAV 193
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAV 209
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
16-189 |
2.17e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 104.79 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER--------GVVFQN--EGLLPWR 85
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEwravrsdiQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 86 NVQENVAFGLQL--AGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
Cdd:PRK15079 116 TIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS 195
|
170 180
....*....|....*....|....*..
gi 493863201 163 TREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK15079 196 IQAQVVNLLQQLQREMGLSLIFIAHDL 222
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-189 |
2.30e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 103.38 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKP---------ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT-GPGAE 71
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEyGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 72 RG----VVFQ--NEGLLPWRNVQENVAFGLQLA----GVAREQRLNtarDMLKKVGL--EGAEkRFIWQLSGGQRQRVGI 139
Cdd:COG4167 85 RCkhirMIFQdpNTSLNPRLNIGQILEEPLRLNtdltAEEREERIF---ATLRLVGLlpEHAN-FYPHMLSSGQKQRVAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHL 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-205 |
2.45e-26 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.12 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERG-------- 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 ----------VVFQNEGLLPWRNVQENVAFG-LQLAGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIAR 141
Cdd:PRK10619 86 qlrllrtrltMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863201 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQG 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-205 |
3.57e-26 |
|
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: 101.78 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPA---LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE----RGVVFQN 78
Cdd:cd03248 16 NVTFAYPTRPDtlvLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylhsKVSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNVQENVAFGLQ---LAGVAREQRLNTARDMLKK--------VGLEGAekrfiwQLSGGQRQRVGIARALAANP 147
Cdd:cd03248 96 EPVLFARSLQDNIAYGLQscsFECVKEAAQKAHAHSFISElasgydteVGEKGS------QLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 148 QLLLLDEPFGALDAFTREQMQTlLLRLWHETgKQVLLITHDIeEAVFMATELVLLSPG 205
Cdd:cd03248 170 QVLILDEATSALDAESEQQVQQ-ALYDWPER-RTVLVIAHRL-STVERADQILVLDGG 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-187 |
3.98e-26 |
|
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: 100.90 E-value: 3.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVF----Q 77
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIlylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFGLQLAGVAReqrlNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGAQ----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 493863201 158 ALDAFTREQMQTlLLRLWHETGKQVLLITH 187
Cdd:TIGR01189 157 ALDKAGVALLAG-LLRAHLARGGIVLLTTH 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
13-187 |
1.27e-25 |
|
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: 100.38 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG-----AERGVVFQNEGLLPwRNV 87
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTlaslrRQIGLVSQDVFLFN-DTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQlaGVAREQ-----RLNTARDMLKK--------VGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:cd03251 93 AENIAYGRP--GATREEveeaaRAANAHEFIMElpegydtvIGERGV------KLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190
....*....|....*....|....*....|...
gi 493863201 155 PFGALDAFTREQMQTLLLRLwhETGKQVLLITH 187
Cdd:cd03251 165 ATSALDTESERLVQAALERL--MKNRTTFVIAH 195
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-155 |
1.29e-25 |
|
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: 100.29 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAER-----GVV 75
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKlPPHERaragiAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTA-------RDMLKKVGleGaekrfiwQLSGGQRQRVGIARALAANPQ 148
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIyelfpvlKEMLGRRG--G-------DLSGGQQQQLAIARALVTRPK 151
|
....*..
gi 493863201 149 LLLLDEP 155
Cdd:TIGR03410 152 LLLLDEP 158
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-205 |
1.83e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.22 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVtgPGAER------GVV 75
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV--PARARlarariGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQEN-VAFGLQLAGVAREQRlNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:PRK13536 120 PQFDNLDLEFTVRENlLVFGRYFGMSTREIE-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 155 PFGALDAFTR----EQMQTLLLRlwhetGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13536 199 PTTGLDPHARhliwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
19-205 |
2.45e-25 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 102.26 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 19 AINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG-------KRVTGPGAER--GVVFQNEGLLPWRNVQE 89
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEKRriGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 90 NVAFGLqlAGVAREQrlntardMLKKVGLEGAE---KRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
Cdd:PRK11144 96 NLRYGM--AKSMVAQ-------FDKIVALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 493863201 167 MQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-234 |
2.74e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG------KRVTGPGAERG 73
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQN-EGLLPWRNVQENVAFG---LQLAGVAREQRLNTArdmLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQL 149
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGpenLCLPPIEIRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEaVFMATELVLLSPGpgrvleRLPLEfarryvaGEPvRS 229
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLEE-LHDADRIIVMDRG------KIVLE-------GEP-EN 221
|
....*
gi 493863201 230 IKSDP 234
Cdd:PRK13644 222 VLSDV 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-192 |
3.32e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.24 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLL-------NLIAGFvpYQHGTIHLEGKRVTGPGAER-- 72
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF--RVEGKVTFHGKNLYAPDVDPve 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -----GVVFQNEGLLPwRNVQENVAFGLQLAG--------VAREQR----LNTARDMLKKVGLegaekrfiwQLSGGQRQ 135
Cdd:PRK14243 89 vrrriGMVFQKPNPFP-KSIYDNIAYGARINGykgdmdelVERSLRqaalWDEVKDKLKQSGL---------SLSGGQQQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlrlwHETGKQ--VLLITHDIEEA 192
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELM----HELKEQytIIIVTHNMQQA 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-205 |
3.95e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLegkrvtGPGAERGVVFQ-NE 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL------GETVKIGYFDQhQE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GLLPWRNVQENVAfglQLAGVAREQrlnTARDMLKKVGLEGAE-KRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:COG0488 389 ELDPDKTVLDELR---DGAPGGTEQ---EVRGYLGRFLFSGDDaFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNH 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 159 LDAFTREQMQTLLLRlWHETgkqVLLITHDIEeavFM---ATELVLLSPG 205
Cdd:COG0488 463 LDIETLEALEEALDD-FPGT---VLLVSHDRY---FLdrvATRILEFEDG 505
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
16-205 |
4.99e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.19 E-value: 4.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQ-NEGLLPWR 85
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrkkvGVVFQfPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 86 NVQENVAFGLQLAGVAREQRLNTARDMLKKVGL--EGAEKRfIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLadEFWEKS-PFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 164 REQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13643 180 RIEMMQLFESI-HQSGQTVVLVTHLMDDVADYADYVYLLEKG 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
7-201 |
7.07e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 103.00 E-value: 7.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 7 LSADygGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQhGTIHLEGK--RVTGPGAER---GVVFQNEgL 81
Cdd:PRK11174 358 LSPD--GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIelRELDPESWRkhlSWVGQNP-Q 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 82 LPWRNVQENVAFGLQLAGvarEQRLNTArdmlkkvgLEGAE-KRFIWQ---------------LSGGQRQRVGIARALAA 145
Cdd:PRK11174 434 LPHGTLRDNVLLGNPDAS---DEQLQQA--------LENAWvSEFLPLlpqgldtpigdqaagLSVGQAQRLALARALLQ 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 146 NPQLLLLDEPFGALDAFTREQMQTLLLRLWHetGKQVLLITHDIEEAVFMATELVL 201
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVM 556
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-224 |
7.33e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 99.15 E-value: 7.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ-----HGTIHLEGKRVTGPGA-------ERG 73
Cdd:PRK14267 9 NLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVdpievrrEVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQNEGLLPWRNVQENVAFGLQLAGVAREQRL--NTARDMLKKVGL-EGAEKR---FIWQLSGGQRQRVGIARALAANP 147
Cdd:PRK14267 89 MVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 148 QLLLLDEPFGALDAFTREQMQTLLLRLWHETgkQVLLITHDIEEAVFMATELV------LLSPGPGR-VLERLPLEFARR 220
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAflylgkLIEVGPTRkVFENPEHELTEK 246
|
....
gi 493863201 221 YVAG 224
Cdd:PRK14267 247 YVTG 250
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
4-205 |
8.99e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.35 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYG-GKP----ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA-------E 71
Cdd:PRK13637 5 IENLTHIYMeGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsdirkK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 72 RGVVFQ-NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGL--EGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:PRK13637 85 VGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13637 165 ILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKG 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-192 |
1.37e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.64 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 11 YGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGAER----GVVFQNEGLLPW 84
Cdd:COG3845 15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRirSPRDAIalgiGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVAFGLQLAGVAReQRLNTARDMLKKV----GLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEP----- 155
Cdd:COG3845 95 LTVAENIVLGLEPTKGGR-LDRKAARARIRELseryGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPtavlt 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493863201 156 -------FGALDAFTREqmqtlllrlwhetGKQVLLITHDIEEA 192
Cdd:COG3845 174 pqeadelFEILRRLAAE-------------GKSIIFITHKLREV 204
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
6-187 |
1.72e-24 |
|
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: 97.30 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVVFQNE 79
Cdd:cd03254 7 NVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSlrsmiGVVLQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GLLPwRNVQENVAFGLQLAGVAREQRLNT---ARDMLKKV--GL-----EGAEKrfiwqLSGGQRQRVGIARALAANPQL 149
Cdd:cd03254 87 FLFS-GTIMENIRLGRPNATDEEVIEAAKeagAHDFIMKLpnGYdtvlgENGGN-----LSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRLWHetGKQVLLITH 187
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAH 196
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
16-205 |
2.54e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.31 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQ-NEGLLPWR 85
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpvrkriGMVFQfPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 86 NVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEgaekRFI-----WQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK13646 102 TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS----RDVmsqspFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493863201 161 AFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-227 |
2.82e-24 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 101.63 E-value: 2.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTgpgAERGVVFQNEGLLPWRN------ 86
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE---TNLDAVRQSLGMCPQHNilfhhl 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 87 -VQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
Cdd:TIGR01257 1019 tVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493863201 166 QMQTLLLRlwHETGKQVLLITHDIEEAVFMATELVLLSPGpgrvlerlplefaRRYVAGEPV 227
Cdd:TIGR01257 1099 SIWDLLLK--YRSGRTIIMSTHHMDEADLLGDRIAIISQG-------------RLYCSGTPL 1145
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-205 |
3.24e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.16 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKP-----ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHL----------EGKRVTGP 68
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanlkKIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 69 GAERGVVFQ-NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARALAAN 146
Cdd:PRK13645 89 RKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 147 PQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEG 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-205 |
3.77e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.55 E-value: 3.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTT----LLNLIA--GFVPYQHGTIHLEGKRVTGPGAER-GVVFQ--NEGLL 82
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINsqGEIWFDGQPLHNLNRRQLLPVRHRiQVVFQdpNSSLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 83 PWRNVQENVAFGLQ-----LAGVAREQRLNTArdmLKKVGLEGAEK-RFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:PRK15134 377 PRLNVLQIIEEGLRvhqptLSAAQREQQVIAV---MEEVGLDPETRhRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 157 GALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-196 |
5.17e-24 |
|
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: 94.81 E-value: 5.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSadygGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA----ERGVVF 76
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrdaiRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 -----QNEGLLPWRNVQENVAFGlqlagvareqrlntardmlkkvglegaekrfiWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:cd03215 80 vpedrKREGLVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMA 196
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLC 171
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-212 |
5.86e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.00 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGpgAERGV------ 74
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY--SKRGLlalrqq 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 ---VFQN-EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLL 150
Cdd:PRK13638 79 vatVFQDpEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 151 LLDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIE------EAVFMATELVLLSPG-PGRVLER 212
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDliyeisDAVYVLRQGQILTHGaPGEVFAC 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-187 |
6.30e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.90 E-value: 6.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADY--GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG--PGAERgvvfQ 77
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADysEAALR----Q 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWR------NVQENvafgLQLAG-VAREQRLntaRDMLKKVGL----EGAEKRFIW------QLSGGQRQRVGIA 140
Cdd:PRK11160 415 AISVVSQRvhlfsaTLRDN----LLLAApNASDEAL---IEVLQQVGLekllEDDKGLNAWlgeggrQLSGGEQRRLGIA 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLRlwHETGKQVLLITH 187
Cdd:PRK11160 488 RALLHDAPLLLLDEPTEGLDAETERQILELLAE--HAQNKTVLMITH 532
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
14-205 |
6.51e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 97.21 E-value: 6.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQ-NEGLLP 83
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrkkvSLVFQfPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493863201 163 TREQMQTLLLRlWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13641 180 GRKEMMQLFKD-YQKAGHTVILVTHNMDDVAEYADDVLVLEHG 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-191 |
1.10e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.34 E-value: 1.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNIT---NLSADYGG---KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA---- 70
Cdd:PRK13650 1 MSNIIevkNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 71 -ERGVVFQN-EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:PRK13650 81 hKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEE 191
Cdd:PRK13650 161 IIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDE 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-188 |
1.15e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.98 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEgkrvtgPGAERGVVFQNEGLLP 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------KGLRIGYLPQEPPLDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WRNVQENVAFGLQ--LAGVAREQRLNT------------------------------ARDMLKKVGLEGAE-KRFIWQLS 130
Cdd:COG0488 75 DLTVLDTVLDGDAelRALEAELEELEAklaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDlDRPVSELS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 131 GGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRlWHETgkqVLLITHD 188
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN-YPGT---VLVVSHD 208
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-211 |
1.23e-23 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 95.76 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKR------VTGPGAERGV 74
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEgllpWRNVQENVAFGLQL---AGVAREQRL------------NTARDMLKKVGLEGAE-----KRFiwqlSGGQR 134
Cdd:PRK11701 86 LLRTE----WGFVHQHPRDGLRMqvsAGGNIGERLmavgarhygdirATAGDWLERVEIDAARiddlpTTF----SGGMQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 135 QRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLE 211
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK--QGRVVE 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-205 |
1.31e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.35 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER---------GVVFQ-NEGLLPW 84
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirkkvGLVFQfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVAFGLQLAGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 164 REQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13649 181 RKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-202 |
1.69e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 94.65 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPyQHGTIhleGKRVTGPGAER---------GVVFQNEGLLPWRNV 87
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTT---SGQILFNGQPRkpdqfqkcvAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLA------GVAREQRLNTARdmLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
Cdd:cd03234 99 RETLTYTAILRlprkssDAIRKKRVEDVL--LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493863201 162 FTREQMQTLLLRLWHEtGKQVLLITHDIEEAVFMATELVLL 202
Cdd:cd03234 177 FTALNLVSTLSQLARR-NRIVILTIHQPRSDLFRLFDRILL 216
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
20-216 |
1.71e-23 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 94.74 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 20 INLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ----HGTIHLEGKRVTGP---GAERGVVFQN--EGLLPWRNVQEN 90
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGltqtSGEILLDGRPLLPLsirGRHIATIMQNprTAFNPLFTMGNH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAFGLQLAGVAREQRLNTARDMLKKVGLEGAE---KRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
Cdd:TIGR02770 85 AIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQARV 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 168 QTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLERLPLE 216
Cdd:TIGR02770 165 LKLLRELRQLFGTGILLITHDLGVVARIADEVAVMD--DGRIVERGTVK 211
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-192 |
3.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.16 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKP---ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA-----ER 72
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnlrrKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVFQN-EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:PRK13642 84 GMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEA 192
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA 204
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-192 |
4.05e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLL-NLIAGFVPYQhGTI-----HLEGKRVTGPGAER----------------- 72
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIeHLNALLLPDT-GTIewifkDEKNKKKTKEKEKVleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 -------GVVFQ-NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGGQRQRVGIARAL 143
Cdd:PRK13651 101 keirrrvGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 144 AANPQLLLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEA 192
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNL-NKQGKTIILVTHDLDNV 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
13-187 |
5.84e-23 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 97.24 E-value: 5.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGAER---GVVFQNEGLLpWRNV 87
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPADLRrniGYVPQDPRLF-YGTL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFG------------LQLAGVAR-EQRLNTARDMLkkVGlEGAEkrfiwQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:TIGR03375 556 RDNIALGapyaddeeilraAELAGVTEfVRRHPDGLDMQ--IG-ERGR-----SLSGGQRQAVALARALLRDPPILLLDE 627
|
170 180 190
....*....|....*....|....*....|...
gi 493863201 155 PFGALDAFTREQMQTLLLRLWHetGKQVLLITH 187
Cdd:TIGR03375 628 PTSAMDNRSEERFKDRLKRWLA--GKTLVLVTH 658
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-187 |
8.46e-23 |
|
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: 92.17 E-value: 8.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGkrvTGPGAERGVVFQN--- 78
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARGlly 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 ----EGLLPWRNVQENVAFGLQLAGVAreqrlnTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:cd03231 78 lghaPGIKTTLSVLENLRFWHADHSDE------QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|...
gi 493863201 155 PFGALDAFTREQMQTlLLRLWHETGKQVLLITH 187
Cdd:cd03231 152 PTTALDKAGVARFAE-AMAGHCARGGMVVLTTH 183
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-187 |
8.74e-23 |
|
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: 92.65 E-value: 8.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGK--RVTGPGAER---GVVFQNEGLLpWRNVQ 88
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTdiRQLDPADLRrniGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 89 ENVAFGLQLAG---VAREQRLNTARDMLKK----VGLEGAEKRFiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDa 161
Cdd:cd03245 96 DNITLGAPLADderILRAAELAGVTDFVNKhpngLDLQIGERGR--GLSGGQRQAVALARALLNDPPILLLDEPTSAMD- 172
|
170 180
....*....|....*....|....*.
gi 493863201 162 FTREQMQTLLLRLWHEtGKQVLLITH 187
Cdd:cd03245 173 MNSEERLKERLRQLLG-DKTLIIITH 197
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-188 |
8.97e-23 |
|
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: 90.59 E-value: 8.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAG-FVPYqhgtihlEGKRVTGPGAergvvfqneg 80
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPD-------EGIVTWGSTV---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 llpwrnvqenvafglqlagvareqrlntardmlkKVGlegaekrFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:cd03221 64 ----------------------------------KIG-------YFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180
....*....|....*....|....*...
gi 493863201 161 AFTREQMQTLLLRlWHETgkqVLLITHD 188
Cdd:cd03221 103 LESIEALEEALKE-YPGT---VILVSHD 126
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-205 |
9.15e-23 |
|
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: 92.88 E-value: 9.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-----GGK--PALEAINLTLDSGELLVVLGPSGCGKTTLLNLI-------AGFVPYQHGtihleGKRVT 66
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKrlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVRHD-----GGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 67 GPGAE-------R----GVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLegaeKRFIWQL-----S 130
Cdd:COG4778 79 LAQASpreilalRrrtiGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNL----PERLWDLppatfS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 131 GGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIE--EAVfmATELVLLSPG 205
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEvrEAV--ADRVVDVTPF 228
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-247 |
1.24e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.18 E-value: 1.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQhGTIHLEGK-----------RVTGPGA 70
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELE-SEVRVEGRveffnqniyerRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 71 ERGV--VFQNEGLLPwRNVQENVAFGLQLAGVAREQRLntarDMLKKVGLEGAEkrfIW------------QLSGGQRQR 136
Cdd:PRK14258 87 RRQVsmVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEI----DDIVESALKDAD---LWdeikhkihksalDLSGGQQQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGPGRVLERlpLE 216
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRIGQL--VE 236
|
250 260 270
....*....|....*....|....*....|.
gi 493863201 217 FARryvagepVRSIKSDPLFIEQREYVLSRV 247
Cdd:PRK14258 237 FGL-------TKKIFNSPHDSRTREYVLSRL 260
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
27-205 |
1.28e-22 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 96.49 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 27 GELLVVLGPSGCGKTTLLNLIAGFVPYQH--GTIHLEGKRVTGPGAER-GVVFQNEGLLPWRNVQENVAFGLQL---AGV 100
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRtGFVTQDDILYPHLTVRETLVFCSLLrlpKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 101 AREQRLNTARDMLKKVGLEGAEK-----RFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLW 175
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLA 253
|
170 180 190
....*....|....*....|....*....|.
gi 493863201 176 HEtGKQVLLITHDIEEAVF-MATELVLLSPG 205
Cdd:PLN03211 254 QK-GKTIVTSMHQPSSRVYqMFDSVLVLSEG 283
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-188 |
1.39e-22 |
|
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: 95.97 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG-PGAERGvvfQN 78
Cdd:COG4618 331 LSVENLTVVPPGskRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELG---RH 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPwRNVQ-------ENVA-FG----------LQLAGVareqrlntaRDMLKK--------VGLEGAekrfiwQLSGG 132
Cdd:COG4618 408 IGYLP-QDVElfdgtiaENIArFGdadpekvvaaAKLAGV---------HEMILRlpdgydtrIGEGGA------RLSGG 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 133 QRQRVGIARALAANPQLLLLDEPFGALDAfTREQMQTLLLRLWHETGKQVLLITHD 188
Cdd:COG4618 472 QRQRIGLARALYGDPRLVVLDEPNSNLDD-EGEAALAAAIRALKARGATVVVITHR 526
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-205 |
1.56e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 93.15 E-value: 1.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFV-----PYQHgtIHLEGKRVTGPG------ 69
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksAGSH--IELLGRTVQREGrlardi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 70 ----AERGVVFQNEGLLPWRNVQENVAFGLQ---------LAGVAREQRlNTARDMLKKVGLEGAEKRFIWQLSGGQRQR 136
Cdd:PRK09984 82 rksrANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQK-QRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
13-211 |
3.48e-22 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 94.87 E-value: 3.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLegkrvtgPGAERgVVFqneglLPWR------N 86
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR-------PAGAR-VLF-----LPQRpylplgT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 87 VQENVAFGLQLAGVAREQrlntARDMLKKVGLEGAEKRF----IWQ--LSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:COG4178 442 LREALLYPATAEAFSDAE----LREALEAVGLGHLAERLdeeaDWDqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 161 AFTREQMQTLLLRLWHETGkqVLLITHDIEEAVFMATELVLLSPGPGRVLE 211
Cdd:COG4178 518 EENEAALYQLLREELPGTT--VISVGHRSTLAAFHDRVLELTGDGSWQLLP 566
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-187 |
4.66e-22 |
|
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: 89.68 E-value: 4.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTgpgaergvvfqne 79
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 gllpwrNVQENVAfglQLAGVAREQRLNTARDMLKKVGLegaekrfiwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
Cdd:cd03247 68 ------DLEKALS---SLISVLNQRPYLFDTTLRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180
....*....|....*....|....*...
gi 493863201 160 DAFTREQMQTLLLRlwHETGKQVLLITH 187
Cdd:cd03247 130 DPITERQLLSLIFE--VLKDKTLIWITH 155
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-205 |
5.44e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 91.65 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGK---------RVTGPG-- 69
Cdd:PRK14246 10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkdifQIDAIKlr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 70 AERGVVFQNEGLLPWRNVQENVAFGLQLAGVAREQRLNT-ARDMLKKVGL-EGAEKRF---IWQLSGGQRQRVGIARALA 144
Cdd:PRK14246 90 KEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493863201 145 ANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGkqVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIA--IVIVSHNPQQVARVADYVAFLYNG 228
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-211 |
7.17e-22 |
|
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: 90.62 E-value: 7.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV-----TGPGAERGVVFQnEGLLPWRNV 87
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladpAWLRRQVGVVLQ-ENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAF---GLQLAGVAREQRLNTARDMLKK--------VGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:cd03252 93 RDNIALadpGMSMERVIEAAKLAGAHDFISElpegydtiVGEQGA------GLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 157 GALDAFTREQMQTLLLRLWheTGKQVLLITHDIeEAVFMATELVLLSpgPGRVLE 211
Cdd:cd03252 167 SALDYESEHAIMRNMHDIC--AGRTVIIIAHRL-STVKNADRIIVME--KGRIVE 216
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-205 |
8.12e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 91.20 E-value: 8.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVVFQNEG 80
Cdd:PRK10253 12 QLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEvarriGLLAQNAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRNVQENVAFG----LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:PRK10253 92 TPGDITVQELVARGryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 157 GALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREG 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
6-193 |
8.33e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 91.35 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPA--LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVVFQN 78
Cdd:PRK13648 12 NVSFQYQSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrkhiGIVFQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 -EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:PRK13648 92 pDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATS 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 493863201 158 ALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAV 193
Cdd:PRK13648 172 MLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM 207
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-225 |
9.27e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 90.74 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFV-----PYQHGTIHLEGKRV-TGPGAE--RG 73
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIElrRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 V--VFQNEGLLPWRNVQENVAFGLQLagvareQRLNTARDMLKKVGLEGAEKRFIWQ------------LSGGQRQRVGI 139
Cdd:PRK14247 84 VqmVFQIPNPIPNLSIFENVALGLKL------NRLVKSKKELQERVRWALEKAQLWDevkdrldapagkLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 140 ARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETgkQVLLITHDIEEAVFMATELVLL------SPGPGR-VLER 212
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLykgqivEWGPTReVFTN 235
|
250
....*....|...
gi 493863201 213 LPLEFARRYVAGE 225
Cdd:PRK14247 236 PRHELTEKYVTGR 248
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-205 |
2.10e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.63 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVtgPGAER------GVV 75
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV--PSRARharqrvGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVA-----FGLQlAGVAREQrlntARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLL 150
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLvfgryFGLS-AAAARAL----VPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 151 LLDEPFGALDAFTR----EQMQTLLLRlwhetGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13537 161 VLDEPTTGLDPQARhlmwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
13-212 |
4.09e-21 |
|
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: 88.44 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG---KRVTGPGAER--GVVFQNEGLLPwRNV 87
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRRaiGVVPQDTVLFN-DTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFG------------LQLAGVARE-QRLNTARDmlKKVGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:cd03253 92 GYNIRYGrpdatdeevieaAKAAQIHDKiMRFPDGYD--TIVGERGL------KLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 155 PFGALDAFTREQMQTLLLRLwhETGKQVLLITHDIEEAVfMATELVLLSpgPGRVLER 212
Cdd:cd03253 164 ATSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIV-NADKIIVLK--DGRIVER 216
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-205 |
4.31e-21 |
|
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: 88.54 E-value: 4.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 10 DYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIhlegkRVTG--PGAER-------GVVF-QNE 79
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGlvPWKRRkkflrriGVVFgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GL---LPWRNVQENVAFGLQLAGVAREQRLNTARDMLKkvgLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:cd03267 105 QLwwdLPVIDSFYLLAAIYDLPPARFKKRLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 157 GALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-190 |
6.04e-21 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 91.40 E-value: 6.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 8 SADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHL----EGKRVTGPG------AER--GVV 75
Cdd:TIGR03269 291 SVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGpdgrgrAKRyiGIL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENV--AFGLQLAG-VAREQRLNTardmLKKVGLEGAEKRFIW-----QLSGGQRQRVGIARALAANP 147
Cdd:TIGR03269 371 HQEYDLYPHRTVLDNLteAIGLELPDeLARMKAVIT----LKMVGFDEEKAEEILdkypdELSEGERHRVALAQVLIKEP 446
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493863201 148 QLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIE 190
Cdd:TIGR03269 447 RIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMD 489
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-196 |
6.33e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 91.23 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSadygGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGA--ERGVVF 76
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirSPRDaiRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 -----QNEGLLPWRNVQENVAFG----LQLAGVAREQRLN-TARDMLKKVGL--EGAEKRfIWQLSGGQRQRVGIARALA 144
Cdd:COG1129 332 vpedrKGEGLVLDLSIRENITLAsldrLSRGGLLDRRRERaLAEEYIKRLRIktPSPEQP-VGNLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493863201 145 ANPQLLLLDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEEAVFMA 196
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLS 461
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-187 |
8.76e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 87.60 E-value: 8.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVtgpgaeR-----------GVVFQnEGLLP 83
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI------RdlnlrwlrsqiGLVSQ-EPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WRNVQENVAFGL---QLAGVAREQRLNTARDMLKK--------VGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:cd03249 90 DGTIAENIRYGKpdaTDEEVEEAAKKANIHDFIMSlpdgydtlVGERGS------QLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190
....*....|....*....|....*....|....*
gi 493863201 153 DEPFGALDAFTREQMQTLLLRLwhETGKQVLLITH 187
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRA--MKGRTTIVIAH 196
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
13-190 |
1.02e-20 |
|
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: 87.39 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVfQNEGLL------PW-- 84
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRS-RNRYSVayaaqkPWll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 -RNVQENVAFG-----LQLAGVAREQRLNTARDML-----KKVGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:cd03290 92 nATVEENITFGspfnkQRYKAVTDACSLQPDIDLLpfgdqTEIGERGI------NLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 493863201 154 EPFGALDAFTREQ-MQTLLLRLWHETGKQVLLITHDIE 190
Cdd:cd03290 166 DPFSALDIHLSDHlMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
4-160 |
1.13e-20 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 90.79 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYG--GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG--PGAER---GVVF 76
Cdd:TIGR03797 454 VDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGldVQAVRrqlGVVL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPwRNVQENVAFG-----------LQLAGVAREqrlntARDM---LKKVGLEGAEkrfiwQLSGGQRQRVGIARA 142
Cdd:TIGR03797 534 QNGRLMS-GSIFENIAGGapltldeaweaARMAGLAED-----IRAMpmgMHTVISEGGG-----TLSGGQRQRLLIARA 602
|
170
....*....|....*...
gi 493863201 143 LAANPQLLLLDEPFGALD 160
Cdd:TIGR03797 603 LVRKPRILLFDEATSALD 620
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
1.99e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.55 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GV 74
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrkfvGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQN-EGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:PRK13652 83 VFQNpDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 493863201 154 EPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-192 |
2.07e-20 |
|
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: 89.78 E-value: 2.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGK-----RVTGPGAERGVVFQN 78
Cdd:TIGR02203 335 NVTFRYPGrdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHdladyTLASLRRQVALVSQD 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPwRNVQENVAFGlQLAGVAREQRLNTARDMLKK-------------VGLEGAekrfiwQLSGGQRQRVGIARALAA 145
Cdd:TIGR02203 415 VVLFN-DTIANNIAYG-RTEQADRAEIERALAAAYAQdfvdklplgldtpIGENGV------LLSGGQRQRLAIARALLK 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493863201 146 NPQLLLLDEPFGALDAFTREQMQTLLLRLwhETGKQVLLITH---DIEEA 192
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERL--MQGRTTLVIAHrlsTIEKA 534
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-192 |
2.08e-20 |
|
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: 90.18 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYG-GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGpgAERGVVFQNEG 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKD--IDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPwrnvQENVAF-GLQLAGVAREQRLNTARDMLKKVgLEGAE-KRFIWQ---------------LSGGQRQRVGIARAL 143
Cdd:TIGR01193 552 YLP----QEPYIFsGSILENLLLGAKENVSQDEIWAA-CEIAEiKDDIENmplgyqtelseegssISGGQKQRIALARAL 626
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 144 AANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETgkqVLLITHDIEEA 192
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKT---IIFVAHRLSVA 672
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-210 |
2.10e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.60 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV--TGPGAER-----GVVFQN-EGLLPW 84
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKlresvGMVFQDpDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
Cdd:PRK13636 98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 165 EQMQTLLLRLWHETGKQVLLITHDIE------EAVFMATE-LVLLSPGPGRVL 210
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDivplycDNVFVMKEgRVILQGNPKEVF 230
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-187 |
3.03e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 89.25 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGK-PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG---KRVTGPGAER--GVVFQNE 79
Cdd:PRK13657 339 DVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdiRTVTRASLRRniAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GLLPwRNVQENVAFG--------LQLAGVA---------REQRLNTArdmlkkVGLEGAekrfiwQLSGGQRQRVGIARA 142
Cdd:PRK13657 419 GLFN-RSIEDNIRVGrpdatdeeMRAAAERaqahdfierKPDGYDTV------VGERGR------QLSGGERQRLAIARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 493863201 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHetGKQVLLITH 187
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAH 528
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-243 |
3.30e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.07 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLL-------NLIAGFvpYQHGTIHLEGKRVTGPG------AER 72
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmnDKVSGY--RYSGDVLLGGRSIFNYRdvlefrRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVFQNEGLLPwRNVQENVAFGLQLAG-VAREQRLNTARDMLKKVGLEGAEKRFI----WQLSGGQRQRVGIARALAANP 147
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRLsdspFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 148 QLLLLDEPFGALDAFTREQMQTLLLRLWHETgkQVLLITHDIEEAvfmatelvllspgpGRVLERLPLEFARRYVAGEPV 227
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQA--------------ARISDRAALFFDGRLVEEGPT 246
|
250
....*....|....*.
gi 493863201 228 RSIKSDPLFIEQREYV 243
Cdd:PRK14271 247 EQLFSSPKHAETARYV 262
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
3.52e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.60 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKP-----ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTI---------HLEGKRVT 66
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 67 GPGAER------------GVVFQ-NEGLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGL-EGAEKRFIWQLSGG 132
Cdd:PRK13631 101 TNPYSKkiknfkelrrrvSMVFQfPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGG 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863201 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13631 181 QKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDKG 252
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
26-205 |
4.32e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 26 SGELLVVLGPSGCGKTTLLNLIAGFVP----YQhGTIHLEGKRVTGPGAER--GVVFQNEGLLPWRNVQENVAFGLQL-- 97
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPkgvkGS-GSVLLNGMPIDAKEMRAisAYVQQDDLFIPTLTVREHLMFQAHLrm 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 98 -AGVAREQRLNTARDMLKKVGLEGAEKRFIWQ------LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
Cdd:TIGR00955 129 pRRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQV 208
|
170 180 190
....*....|....*....|....*....|....*.
gi 493863201 171 LLRLwHETGKQVLLITHDIEEAVF-MATELVLLSPG 205
Cdd:TIGR00955 209 LKGL-AQKGKTIICTIHQPSSELFeLFDKIILMAEG 243
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-187 |
5.00e-20 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 88.56 E-value: 5.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG-------KRVTGPGAerGVVFQNEGLLPw 84
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGadlkqwdRETFGKHI--GYLPQDVELFP- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVA-FG--LQLAGVAREQRLNTARDMLKK--------VGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:TIGR01842 406 GTVAENIArFGenADPEKIIEAAKLAGVHELILRlpdgydtvIGPGGA------TLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190
....*....|....*....|....*....|....
gi 493863201 154 EPFGALDAFTREQMQTLLLRLwHETGKQVLLITH 187
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKAL-KARGITVVVITH 512
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-189 |
5.18e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.47 E-value: 5.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY----GGKPALEAINLTLDSGELLVVLGPSGCGKT----TLLNLIA--GFVpyqHGTIHLEGKRVTG-PG 69
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRI---GGSATFNGREILNlPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 70 -------AER-GVVFQN--EGLLPWRNVQENVAFGLQL-AGVAREQRLNTARDMLKKVGLEGAEKR---FIWQLSGGQRQ 135
Cdd:PRK09473 89 kelnklrAEQiSMIFQDpmTSLNPYMRVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493863201 136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-187 |
1.81e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.35 E-value: 1.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGTIHLEGKRVTG-PGAER-----G 73
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDILElSPDERaragiF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQN----EGLlpwrnvqeNVAFGLQLAGVAREQR-------LNTARDMLKKVGL----------EGaekrfiwqLSGG 132
Cdd:COG0396 81 LAFQYpveiPGV--------SVSNFLRTALNARRGEelsarefLKLLKEKMKELGLdedfldryvnEG--------FSGG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 493863201 133 QRQRVGIARALAANPQLLLLDEPFGALD--AFT--REQMQTLllrlwHETGKQVLLITH 187
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDidALRivAEGVNKL-----RSPDRGILIITH 198
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-187 |
2.29e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.96 E-value: 2.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGTIHLEGKRVTG-PGAERGvvfqN 78
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDlPPEERA----R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGL-LPWrnvQENVAFglqlAGVareqrlnTARDMLKKVGlEGaekrfiwqLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:cd03217 77 LGIfLAF---QYPPEI----PGV-------KNADFLRYVN-EG--------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190
....*....|....*....|....*....|..
gi 493863201 158 ALDAftrEQMQTL--LLRLWHETGKQVLLITH 187
Cdd:cd03217 134 GLDI---DALRLVaeVINKLREEGKSVLIITH 162
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-226 |
2.50e-19 |
|
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: 86.78 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ--------HGTIHLEGKRVTGPG---- 69
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsgriiyHVALCEKCGYVERPSkvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 70 ---------------------AER-------GVVFQNE-GLLPWRNVQENVAFGLQLAGVAREQRLNTARDMLKKVGLEG 120
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdKLRrrirkriAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 121 AEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELV 200
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|....*.
gi 493863201 201 LLSPGPgRVLERLPLEFARRYVAGEP 226
Cdd:TIGR03269 241 WLENGE-IKEEGTPDEVVAVFMEGVS 265
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-205 |
2.57e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQhGTIHLEGKRVTG-PGAE----RGVVFQNEGLLPWRNVQENV 91
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPLSDwSAAElarhRAYLSQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 92 AFGLQlAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARAL-----AANP--QLLLLDEPFGALDAftr 164
Cdd:COG4138 91 ALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLDV--- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493863201 165 eQMQTLLLRL---WHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG4138 167 -AQQAALDRLlreLCQQGITVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
15-187 |
3.22e-19 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 86.72 E-value: 3.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV--TGPGAER---GVVFQnEGLLPWRNVQE 89
Cdd:TIGR01846 471 EVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiADPAWLRrqmGVVLQ-ENVLFSRSIRD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 90 NVAF---GLQLAGVAREQRLNTARDML--------KKVGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:TIGR01846 550 NIALcnpGAPFEHVIHAAKLAGAHDFIselpqgynTEVGEKGA------NLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180
....*....|....*....|....*....
gi 493863201 159 LDAFTREQMQTLLLRLwhETGKQVLLITH 187
Cdd:TIGR01846 624 LDYESEALIMRNMREI--CRGRTVIIIAH 650
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-187 |
5.06e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 82.31 E-value: 5.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA--ERGVVF-- 76
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCtyQKQLCFvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPWRNVQENVAFGLQLAGVAREqrlntARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190
....*....|....*....|....*....|.
gi 493863201 157 GALDAFTREQMQTlLLRLWHETGKQVLLITH 187
Cdd:PRK13540 156 VALDELSLLTIIT-KIQEHRAKGGAVLLTSH 185
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-227 |
5.13e-19 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.06 E-value: 5.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV-TGPGAE-----RGV--VFQN--EGLLPWR 85
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdTLSPGKlqalrRDIqfIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 86 NVQENVAFGLQ----LAGVAREQRLNTardMLKKVGLEGAEK-RFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK10261 419 TVGDSIMEPLRvhglLPGKAAAARVAW---LLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 161 AFTREQMQTLLLRLWHETGKQVLLITHDI--------EEAVFMATELVLLspGPGR-VLERLPLEFARRYVAGEPV 227
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDFGIAYLFISHDMavverishRVAVMYLGQIVEI--GPRRaVFENPQHPYTRKLMAAVPV 569
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-190 |
6.90e-19 |
|
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: 82.20 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGkRVTGPgAERGVVFQNEg 80
Cdd:cd03220 22 KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSL-LGLGGGFNPE- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 lLPWRnvqENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:cd03220 99 -LTGR---ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190
....*....|....*....|....*....|
gi 493863201 161 AFTREQMQTLLLRLWhETGKQVLLITHDIE 190
Cdd:cd03220 175 AAFQEKCQRRLRELL-KQGKTVILVSHDPS 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-187 |
9.85e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.16 E-value: 9.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA---ERGVVF-QNEGLLPWRNVQE 89
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhylHRQVALvGQEPVLFSGSVRE 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 90 NVAFGLQLAgvAREQRLNTAR---------DMLKKVGLEGAEKRFiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:TIGR00958 574 NIAYGLTDT--PDEEIMAAAKaanahdfimEFPNGYDTEVGEKGS--QLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|....*..
gi 493863201 161 AftreQMQTLLLRLWHETGKQVLLITH 187
Cdd:TIGR00958 650 A----ECEQLLQESRSRASRTVLLIAH 672
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-189 |
1.05e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 83.64 E-value: 1.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKP----ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQhGTIHLEGKRVTGP-------- 68
Cdd:PRK11022 3 LLNVDKLSVHFGDESapfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYP-GRVMAEKLEFNGQdlqrisek 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 69 ------GAERGVVFQNegllPWRNVQENVAFGLQL-------AGVAREQRLNTARDMLKKVGLEGAEKR---FIWQLSGG 132
Cdd:PRK11022 82 errnlvGAEVAMIFQD----PMTSLNPCYTVGFQImeaikvhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-216 |
1.75e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSAdYGGKPALEAINLTLDSGELLVVLGPSGCGKT----TLLNLIAGFVPYQHGTIHLEGKRVTgPGAERG---- 73
Cdd:PRK10418 5 IELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA-PCALRGrkia 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQN--EGLLPWRNVQENVAFGLQLAGvaREQRLNTARDMLKKVGLEGAE---KRFIWQLSGGQRQRVGIARALAANPQ 148
Cdd:PRK10418 83 TIMQNprSAFNPLHTMHTHARETCLALG--KPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 149 LLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSpgPGRVLERLPLE 216
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMS--HGRIVEQGDVE 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-189 |
2.07e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.99 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY--GG--KPALEAINLTLDSGELLVVLGPSGCGKT----TLLNLI-AGFVPYQHGTIHLEGKRVTGPGAE 71
Cdd:PRK15134 5 LLAIENLSVAFrqQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 72 --RGV-------VFQNE--GLLPWRNVQENVAFGLQL-AGVAREQRLNTARDMLKKVGLEGAEKR---FIWQLSGGQRQR 136
Cdd:PRK15134 85 tlRGVrgnkiamIFQEPmvSLNPLHTLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK15134 165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNL 217
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-235 |
2.52e-18 |
|
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: 84.29 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGG--KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAErgvVFQN 78
Cdd:TIGR01257 1937 ILRLNELTKVYSGtsSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQN 2013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLPWRNV-------QENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:TIGR01257 2014 MGYCPQFDAiddlltgREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEEAVFMATELVLLSPGPGRVL---ERLPLEFARRYVAGEPVR 228
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLgtiQHLKSKFGDGYIVTMKIK 2172
|
....*..
gi 493863201 229 SIKSDPL 235
Cdd:TIGR01257 2173 SPKDDLL 2179
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-205 |
3.97e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER------GV 74
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKimreavAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGLQLAGVAR-EQRLNTARDMLKKVglegAEKRF--IWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFAERDQfQERIKWVYELFPRL----HERRIqrAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENG 213
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-206 |
4.34e-18 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 79.89 E-value: 4.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQNE--GLLPWRNVQENVA 92
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHlpGLKADLSTLENLH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 93 FGLQLAGVAREQRLNTArdmLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAftreQMQTLLL 172
Cdd:PRK13543 105 FLCGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL----EGITLVN 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 493863201 173 RLWH---ETGKQVLLITHDIEEAVFMATELVLLSPGP 206
Cdd:PRK13543 178 RMISahlRGGGAALVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-205 |
4.57e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 4.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE---RGVVF------ 76
Cdd:PRK10575 16 NVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKafaRKVAYlpqqlp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLlpwrNVQENVAFG-------LQLAGVAREQRLNTARDMlkkVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQL 149
Cdd:PRK10575 96 AAEGM----TVRELVAIGrypwhgaLGRFGAADREKVEEAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-191 |
6.91e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.38 E-value: 6.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSA-DYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA----ERGVVF 76
Cdd:COG3845 258 LEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPrerrRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 -----QNEGLLPWRNVQENVAFGLQ-LAGVAREQRLNT------ARDMLKK--VGLEGAEKRfIWQLSGGQRQRVGIARA 142
Cdd:COG3845 338 ipedrLGRGLVPDMSVAENLILGRYrRPPFSRGGFLDRkairafAEELIEEfdVRTPGPDTP-ARSLSGGNQQKVILARE 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 143 LAANPQLLLLDEPFGALD----AFTREQMqtLLLRlwhETGKQVLLITHDIEE 191
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDvgaiEFIHQRL--LELR---DAGAAVLLISEDLDE 464
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-212 |
8.35e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 82.37 E-value: 8.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGK--PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGK-----RVTGPGAERGVVFQN 78
Cdd:PRK11176 346 NVTFTYPGKevPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQVALVSQN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 EGLLpwrN--VQENVAFGLQlAGVAREQ-----RLNTARDMLKK--------VGLEGAekrfiwQLSGGQRQRVGIARAL 143
Cdd:PRK11176 426 VHLF---NdtIANNIAYART-EQYSREQieeaaRMAYAMDFINKmdngldtvIGENGV------LLSGGQRQRIAIARAL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493863201 144 AANPQLLLLDEPFGALDAFTREQMQTLLLRLwhETGKQVLLITH---DIEEavfmATELVLLSpgPGRVLER 212
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDEL--QKNRTSLVIAHrlsTIEK----ADEILVVE--DGEIVER 559
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-191 |
3.17e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 80.64 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPyqHGT----IHLEGKRVTGPG----AER 72
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYP--HGTwdgeIYWSGSPLKASNirdtERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVF--QNEGLLPWRNVQENVAFG--LQLAG--VAREQRLNTARDMLKKVGLEGA-EKRFIWQLSGGQRQRVGIARALAA 145
Cdd:TIGR02633 79 GIVIihQELTLVPELSVAENIFLGneITLPGgrMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 146 NPQLLLLDEPFGALdafTREQMQTLL--LRLWHETGKQVLLITHDIEE 191
Cdd:TIGR02633 159 QARLLILDEPSSSL---TEKETEILLdiIRDLKAHGVACVYISHKLNE 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-191 |
3.63e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.48 E-value: 3.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG--PGAERG----V 74
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltPAKAHQlgiyL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGLQLAGVARE------QRLNTARDMLKKVG-LEGAEkrfiwqlsggqRQRVGIARALAANP 147
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQkmkqllAALGCQLDLDSSAGsLEVAD-----------RQIVEILRGLMRDS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 148 QLLLLDEPFGALDAFTRE----QMQTLLlrlwhETGKQVLLITHDIEE 191
Cdd:PRK15439 160 RILILDEPTASLTPAETErlfsRIRELL-----AQGVGIVFISHKLPE 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-189 |
6.22e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.90 E-value: 6.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKT----TLLNLI---AGFVPYQHGTIHLEGKRVTG------------PGAERGVV 75
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvRGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQN--EGLLPWRNVQENVAFGLQL-AGVAREQRLNTARDMLKKVGLEGAE---KRFIWQLSGGQRQRVGIARALAANPQL 149
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDM 229
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
13-190 |
6.31e-17 |
|
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: 77.97 E-value: 6.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPgaergvvfQNEGLLPwRNVQENVA 92
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS--------QFSWIMP-GTIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 93 FGLQ---------LAGVAREQRLNTARDMLKKVGLEGAekrfiWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:cd03291 120 FGVSydeyryksvVKACQLEEDITKFPEKDNTVLGEGG-----ITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180
....*....|....*....|....*...
gi 493863201 164 REQM-QTLLLRLWheTGKQVLLITHDIE 190
Cdd:cd03291 195 EKEIfESCVCKLM--ANKTRILVTSKME 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-191 |
6.48e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGK---RVTGPGAER---GVVFQNE 79
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynKLDHKLAAQlgiGIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GLLPWRNVQENVAFGLQLA----GVA----REQRLNTArDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:PRK09700 90 SVIDELTVLENLYIGRHLTkkvcGVNiidwREMRVRAA-MMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEE 191
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAE 207
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-189 |
7.62e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEgkrvtgPGAERGVVFQNEG 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN------GKLRIGYVPQKLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPwrNVQENVAFGLQLAGVAREQRLNTArdmLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK09544 78 LDT--TLPLTVNRFLRLRPGTKKEDILPA---LKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180
....*....|....*....|....*....
gi 493863201 161 AFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK09544 153 VNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-191 |
1.02e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV----TGPGAERGV--V 75
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAAGVaiI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLLPWRNVQENVAFGlQL---AGVAREQRLN-TARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLG-QLphkGGIVNRRLLNyEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEE 191
Cdd:PRK11288 164 FDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEE 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-205 |
1.16e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 11 YGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGkRVTGPgAERGVVFQNE--GLlpwrnvq 88
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAL-LELGAGFHPEltGR------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 89 ENVAFGLQLAGVAREQrlntARDMLKKVgLEGAE-KRFIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:COG1134 107 ENIYLNGRLLGLSRKE----IDEKFDEI-VEFAElGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 493863201 164 REQMQTLLLRLWhETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:COG1134 182 QKKCLARIRELR-ESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
15-189 |
1.35e-16 |
|
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: 79.22 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPgaeRGVVFQNEGLlpwrnvQENVAFG 94
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVP---QQAWIQNDSL------RENILFG 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 95 LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM-QT 169
Cdd:TIGR00957 723 KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEkgvnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIfEH 802
|
170 180
....*....|....*....|
gi 493863201 170 LLLRLWHETGKQVLLITHDI 189
Cdd:TIGR00957 803 VIGPEGVLKNKTRILVTHGI 822
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-190 |
2.08e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 77.25 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY----GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVP---------YQHGTIHL------E 61
Cdd:COG4170 3 LLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhvtadrFRWNGIDLlklsprE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 62 GKRVTGpgAERGVVFQNegllPWRNVQENVAFGLQLAGVA------------REQRLNTARDMLKKVGLEGAE---KRFI 126
Cdd:COG4170 83 RRKIIG--REIAMIFQE----PSSCLDPSAKIGDQLIEAIpswtfkgkwwqrFKWRKKRAIELLHRVGIKDHKdimNSYP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863201 127 WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIE 190
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLE 220
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-192 |
2.87e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAgfvpyqhgtihlegkrvtgpGAERGVVFQNEGLLPWRNVQENVAF 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA--------------------GALKGTPVAGCVDVPDNQFGREASL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 94 glqLAGVAREQRLNTARDMLKKVGLEGAekrFIW-----QLSGGQRQRVGIARALAANPQLLLLDEpFGA-LDAFTREQM 167
Cdd:COG2401 103 ---IDAIGRKGDFKDAVELLNAVGLSDA---VLWlrrfkELSTGQKFRFRLALLLAERPKLLVIDE-FCShLDRQTAKRV 175
|
170 180
....*....|....*....|....*..
gi 493863201 168 QTLLLRLWHETGKQVLLITH--DIEEA 192
Cdd:COG2401 176 ARNLQKLARRAGITLVVATHhyDVIDD 202
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
17-205 |
3.49e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 75.35 E-value: 3.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQhGTIHLEGKRVTG-PGAE----RGVVFQnegllpwrnvQENV 91
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPLEAwSAAElarhRAYLSQ----------QQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 92 AFG------LQL---AGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARAL-----AANP--QLLLLDEP 155
Cdd:PRK03695 81 PFAmpvfqyLTLhqpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 156 FGALDAftreQMQTLLLRLWHE---TGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK03695 161 MNSLDV----AQQAALDRLLSElcqQGIAVVMSSHDLNHTLRHADRVWLLKQG 209
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-191 |
3.55e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNlsaDYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPY--QHGTIHLEGKRVTGPG----AERGV 74
Cdd:PRK13549 8 MKNITK---TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQASNirdtERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 V--FQNEGLLPWRNVQENVAFGLQL--AGVAREQRLNT-ARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQL 149
Cdd:PRK13549 85 AiiHQELALVKELSVLENIFLGNEItpGGIMDYDAMYLrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493863201 150 LLLDEPFGALdafTREQMQTLL--LRLWHETGKQVLLITHDIEE 191
Cdd:PRK13549 165 LILDEPTASL---TESETAVLLdiIRDLKAHGIACIYISHKLNE 205
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
13-187 |
4.58e-16 |
|
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: 73.34 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHL-EGKRVT--------GPGAERGVVfqnegLLP 83
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLflpqrpylPLGTLREQL-----IYP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WRNVqenvafglqlagvareqrlntardmlkkvglegaekrfiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALDaft 163
Cdd:cd03223 88 WDDV-----------------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALD--- 123
|
170 180
....*....|....*....|....
gi 493863201 164 rEQMQTLLLRLWHETGKQVLLITH 187
Cdd:cd03223 124 -EESEDRLYQLLKELGITVISVGH 146
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-192 |
5.42e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.09 E-value: 5.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGkrvtGPGAERG--------VV 75
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG----GDMADARhrravcprIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 76 FQNEGLlpWRN------VQENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQL 149
Cdd:NF033858 80 YMPQGL--GKNlyptlsVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493863201 150 LLLDEPFGALDAFTREQMQTLLLRLWHET-GKQVLLITHDIEEA 192
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVATAYMEEA 201
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-205 |
6.57e-16 |
|
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: 76.87 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADygGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPgaergvvfQNEGL 81
Cdd:TIGR01271 429 LFFSNFSLY--VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSP--------QTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 82 LPwRNVQENVAFGLQ---------LAGVAREQRLNTARDMLKKVGLEGAekrfiWQLSGGQRQRVGIARALAANPQLLLL 152
Cdd:TIGR01271 499 MP-GTIKDNIIFGLSydeyrytsvIKACQLEEDIALFPEKDKTVLGEGG-----ITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 493863201 153 DEPFGALDAFT-REQMQTLLLRLWheTGKQVLLITHDIEEaVFMATELVLLSPG 205
Cdd:TIGR01271 573 DSPFTHLDVVTeKEIFESCLCKLM--SNKTRILVTSKLEH-LKKADKILLLHEG 623
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
14-205 |
9.40e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE--RG---VVFQNEGLLPwRNVQ 88
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDswRSrlaVVSQTPFLFS-DTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 89 ENVAFG------LQLAGVAR-----EQRLNTARDMLKKVGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:PRK10789 407 NNIALGrpdatqQEIEHVARlasvhDDILRLPQGYDTEVGERGV------MLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 493863201 158 ALDAFTREQ-MQTllLRLWHEtGKQVLLITHDIeEAVFMATELVLLSPG 205
Cdd:PRK10789 481 AVDGRTEHQiLHN--LRQWGE-GRTVIISAHRL-SALTEASEILVMQHG 525
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-191 |
1.29e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.60 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNlsaDYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFvpYQHGT----IHLEGKRVTGPG----AER 72
Cdd:NF040905 4 MRGITK---TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV--YPHGSyegeILFDGEVCRFKDirdsEAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVF--QNEGLLPWRNVQENVAFGLQLA--GVA-REQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANP 147
Cdd:NF040905 79 GIVIihQELALIPYLSIAENIFLGNERAkrGVIdWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 493863201 148 QLLLLDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEE 191
Cdd:NF040905 159 KLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNE 201
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
16-189 |
2.11e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 73.67 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT-GPGAERG----VVFQN--EGLLPWRNVQ 88
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSYRSqrirMIFQDpsTSLNPRQRIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 89 ENVAFGLQL----AGVAREQRLNTArdmLKKVGLEGAEKRFI-WQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:PRK15112 108 QILDFPLRLntdlEPEQREKQIIET---LRQVGLLPDHASYYpHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184
|
170 180
....*....|....*....|....*.
gi 493863201 164 REQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK15112 185 RSQLINLMLELQEKQGISYIYVTQHL 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-188 |
2.65e-15 |
|
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: 74.97 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLegkrvtGPGAERGVVFQN-EGLLPW 84
Cdd:TIGR03719 327 NLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI------GETVKLAYVDQSrDALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVAFG---LQLAGVAREQRLNTAR------DMLKKVGlegaekrfiwQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:TIGR03719 401 KTVWEEISGGldiIKLGKREIPSRAYVGRfnfkgsDQQKKVG----------QLSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
170 180 190
....*....|....*....|....*....|...
gi 493863201 156 FGALDAFTREQMQTLLLrlwhETGKQVLLITHD 188
Cdd:TIGR03719 471 TNDLDVETLRALEEALL----NFAGCAVVISHD 499
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
13-189 |
5.29e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVF--QNEGLlPWRN---V 87
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYvpQSEEV-DWSFpvlV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFG----LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:PRK15056 98 EDVVMMGryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180
....*....|....*....|....*.
gi 493863201 164 REQMQTLLLRLWHEtGKQVLLITHDI 189
Cdd:PRK15056 178 EARIISLLRELRDE-GKTMLVSTHNL 202
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-191 |
5.88e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.81 E-value: 5.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNL-------------IAGFVPYQHGTIHLegKRVtgpgaerGVVF-QNE 79
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMltgilvptsgevrVLGYVPFKRRKEFA--RRI-------GVVFgQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GL---LPwrnVQENvaFGL-----QLAGVAREQRLNTARDMLkkvGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:COG4586 106 QLwwdLP---AIDS--FRLlkaiyRIPDAEYKKRLDELVELL---DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITH---DIEE 191
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHdmdDIEA 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
13-163 |
8.16e-15 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 73.44 E-value: 8.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFvpYQH--GTIHLEGKrvtgPGAE--RGVVF------QNEGLL 82
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGL--YQPwsGEILFDGI----PREEipREVLAnsvamvDQDIFL 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 83 PWRNVQENVAfgLQLAGVAREQRLNTARD------MLKKVG------LEGAEkrfiwQLSGGQRQRVGIARALAANPQLL 150
Cdd:TIGR03796 565 FEGTVRDNLT--LWDPTIPDADLVRACKDaaihdvITSRPGgydaelAEGGA-----NLSGGQRQRLEIARALVRNPSIL 637
|
170
....*....|...
gi 493863201 151 LLDEPFGALDAFT 163
Cdd:TIGR03796 638 ILDEATSALDPET 650
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-232 |
2.73e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.63 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPyqhGTIHLEGKRVTG-------PGAE-- 71
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGdvtlngePLAAid 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 72 -------RGVVFQ-NEGLLPWrNVQENVAFG----LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGI 139
Cdd:PRK13547 78 aprlarlRAVLPQaAQPAFAF-SAREIVLLGryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 140 ARALA---------ANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG----- 205
Cdd:PRK13547 157 ARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGaivah 236
|
250 260
....*....|....*....|....*....
gi 493863201 206 --PGRVLErlPLEFARRYvaGEPVRSIKS 232
Cdd:PRK13547 237 gaPADVLT--PAHIARCY--GFAVRLVDA 261
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-220 |
2.79e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSAdyggkPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GP--GAERGVVFQ 77
Cdd:PRK10762 258 LKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrSPqdGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NE-----GLLPWRNVQENVAFGL-----QLAGVAREQRLNTARD---MLKKVGLEGAEKRfIWQLSGGQRQRVGIARALA 144
Cdd:PRK10762 333 SEdrkrdGLVLGMSVKENMSLTAlryfsRAGGSLKHADEQQAVSdfiRLFNIKTPSMEQA-IGLLSGGNQQKVAIARGLM 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 145 ANPQLLLLDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEEAVFMATELVLLSPGpgrvleRLPLEFARR 220
Cdd:PRK10762 412 TRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEG------RISGEFTRE 480
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
11-207 |
3.02e-14 |
|
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: 70.13 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 11 YGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTgpgaergvvFQNEGLLPWRNVQEN 90
Cdd:cd03237 9 TLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---------YKPQYIKADYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAFGLQLAGVAREQRLNTarDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTL 170
Cdd:cd03237 80 DLLSSITKDFYTHPYFKT--EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKV 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 493863201 171 LLRLWHETGKQVLLITHDIEEAVFMATELVLLSPGPG 207
Cdd:cd03237 158 IRRFAENNEKTAFVVEHDIIMIDYLADRLIVFEGEPS 194
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-205 |
7.91e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 7.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG------PGAERGV 74
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVArlqqdpPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VF---------QNEGLLPWRNVQENVAFGLQLAGVAREQRL-------------NTARDMLKKVGLEGAEKrfIWQLSGG 132
Cdd:PRK11147 83 VYdfvaegieeQAEYLKRYHDISHLVETDPSEKNLNELAKLqeqldhhnlwqleNRINEVLAQLGLDPDAA--LSSLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863201 133 QRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLrlwhETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK11147 161 WLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRSFIRNMATRIVDLDRG 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
14-205 |
9.98e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPyqhgtiHLEGKRVTGPGAergVVFQNEglLPW---RNVQEN 90
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS------HAETSSVVIRGS---VAYVPQ--VSWifnATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAFG-----------LQLAGVAREQRLNTARDmLKKVGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
Cdd:PLN03232 699 ILFGsdfeserywraIDVTALQHDLDLLPGRD-LTEIGERGV------NISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 160 DAFTREQMQTLLLRlwHE-TGKQVLLITHDIEEAVFMaTELVLLSPG 205
Cdd:PLN03232 772 DAHVAHQVFDSCMK--DElKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-212 |
9.98e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.13 E-value: 9.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADY-GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE---RGV-VF 76
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSvlrQGVaMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 QNEGLLPWRNVQENVAFGLQLAGVAREQRLNT------ARDMlkkvgLEGAEKRFIWQ---LSGGQRQRVGIARALAANP 147
Cdd:PRK10790 421 QQDPVVLADTFLANVTLGRDISEEQVWQALETvqlaelARSL-----PDGLYTPLGEQgnnLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 148 QLLLLDEPFGALDAFTREQMQTLLLRLWHETgkQVLLITHDIEEAVFMATELVLLSpgpGRVLER 212
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLSTIVEADTILVLHR---GQAVEQ 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
12-188 |
1.39e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.96 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGF-VPYqhgtihlEGKRVTGPGAERGVVFQNEGLLPWRNVQEN 90
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKDF-------NGEARPQPGIKVGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAFGLQ--LAGVAREQRLNTA----RDMLKKVGLEGAEKRFI------WQ-----------------------LSGGQRQ 135
Cdd:TIGR03719 89 VEEGVAeiKDALDRFNEISAKyaepDADFDKLAAEQAELQEIidaadaWDldsqleiamdalrcppwdadvtkLSGGERR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlrlwHETGKQVLLITHD 188
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-190 |
2.09e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 68.68 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADY----GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGfvpyqhgtIHLEGKRVTG--------- 67
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG--------VTKDNWRVTAdrmrfddid 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 68 -----PGAERGVVFQNEGLL---PWRNVQENVAFGLQLA---------GVAREQ---RLNTARDMLKKVGLE---GAEKR 124
Cdd:PRK15093 75 llrlsPRERRKLVGHNVSMIfqePQSCLDPSERVGRQLMqnipgwtykGRWWQRfgwRKRRAIELLHRVGIKdhkDAMRS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 125 FIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIE 190
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQ 220
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-187 |
3.54e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.97 E-value: 3.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGTIHLEGKRVTGPGAE----RGV 74
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESILDLEPEerahLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 --VFQNEGLLPWRNvqeNVAFgLQLAGVAREQRLNTA-----------RDMLKKVGLegaEKRFIWQ-----LSGGQRQR 136
Cdd:CHL00131 87 flAFQYPIEIPGVS---NADF-LRLAYNSKRKFQGLPeldplefleiiNEKLKLVGM---DPSFLSRnvnegFSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 137 VGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITH 187
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITH 209
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-205 |
4.10e-13 |
|
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: 65.73 E-value: 4.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAG--FVPYQHGTIHLEGKRVTgPGAER--GVVFQNEGLLPWRNV 87
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD-KNFQRstGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 88 QENVAFGLQLAGvareqrlntardmlkkvglegaekrfiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
Cdd:cd03232 97 REALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNI 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 493863201 168 QTLLLRLwHETGKQVLLITHDIEEAVF-MATELVLLSPG 205
Cdd:cd03232 148 VRFLKKL-ADSGQAILCTIHQPSASIFeKFDRLLLLKRG 185
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-190 |
5.76e-13 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 65.98 E-value: 5.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADY--GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERgvVFQNEGLLP 83
Cdd:cd03244 7 NVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD--LRSRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 wrnvQENVAFG------LQLAGVAREQRLNTArdmLKKVGLegaeKRFIWQLSG---------------GQRQRVGIARA 142
Cdd:cd03244 85 ----QDPVLFSgtirsnLDPFGEYSDEELWQA---LERVGL----KEFVESLPGgldtvveeggenlsvGQRQLLCLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLRlwHETGKQVLLITHDIE 190
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLD 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-205 |
6.35e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 6.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 20 INLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTgPGAE-----RGVVFQNE-----GLLPWRNVQE 89
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS-PRSPldavkKGMAYITEsrrdnGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 90 NVAFG--LQLAGV---------AREQRlnTARDMLKKVGLEGAE-KRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:PRK09700 361 NMAISrsLKDGGYkgamglfheVDEQR--TAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 158 ALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK09700 439 GIDVGAKAEIYKVMRQL-ADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-163 |
1.02e-12 |
|
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: 64.98 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 13 GKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPyqhGTIHLEGKrVTGPG---------AERGVVFQNEGLL- 82
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEGD-IHYNGipykefaekYPGEIIYVSEEDVh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 83 -PWRNVQENVAFGLQLAGvareqrlntaRDMLKKVglegaekrfiwqlSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
Cdd:cd03233 95 fPTLTVRETLDFALRCKG----------NEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
..
gi 493863201 162 FT 163
Cdd:cd03233 152 ST 153
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-188 |
2.02e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 20 INLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAER-----GVVFQNegllpwrnvqenvaFG 94
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyrqlfSAVFSD--------------FH 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 95 L--QLAGVAREQRLNTARDMLKKVGLEG----AEKRFI-WQLSGGQRQRVGIARALAANPQLLLLDEpfGALD---AFTR 164
Cdd:COG4615 417 LfdRLLGLDGEADPARARELLERLELDHkvsvEDGRFStTDLSQGQRKRLALLVALLEDRPILVFDE--WAADqdpEFRR 494
|
170 180
....*....|....*....|....
gi 493863201 165 EQMQTLLLRLwHETGKQVLLITHD 188
Cdd:COG4615 495 VFYTELLPEL-KARGKTVIAISHD 517
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-191 |
2.42e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.18 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGAER----GV 74
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfnGPKSSQeagiGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 75 VFQNEGLLPWRNVQENVAFGLQLA---GVAREQRLNTARD-MLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLL 150
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVnrfGRIDWKKMYAEADkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVI 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493863201 151 LLDEPfgaLDAFTREQMQTL--LLRLWHETGKQVLLITHDIEE 191
Cdd:PRK10762 164 IMDEP---TDALTDTETESLfrVIRELKSQGRGIVYISHRLKE 203
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
16-188 |
2.88e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.76 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTG--PGAER---GVVFQN----EGLLPWRN 86
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAeqPEDYRklfSAVFTDfhlfDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 87 VQENVAfglqlAGVAREQRLNtardMLKKVGLEGAEKRFIwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
Cdd:PRK10522 418 KPANPA-----LVEKWLERLK----MAHKLELEDGRISNL-KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180
....*....|....*....|..
gi 493863201 167 MQTLLLRLWHETGKQVLLITHD 188
Cdd:PRK10522 488 FYQVLLPLLQEMGKTIFAISHD 509
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-205 |
2.91e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 2.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRV----TGPGAERGV--VFQ 77
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALENGIsmVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 78 NEGLLPWRNVQENVAFG---LQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDE 154
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGrypTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 155 PFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-201 |
3.41e-12 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 62.39 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 26 SGELLVVLGPSGCGKTTLLNLIAGFVPYQHGtihlegkrvtgpgaerGVVFQNegllpwrnvqenvafglqlagvareqr 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG----------------GVIYID--------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 106 LNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ-----TLLLRLWHETGK 180
Cdd:smart00382 38 GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLLLLLKSEKNL 117
|
170 180
....*....|....*....|.
gi 493863201 181 QVLLITHDIEEAVFMATELVL 201
Cdd:smart00382 118 TVILTTNDEKDLGPALLRRRF 138
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
14-209 |
3.90e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.96 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHlegkrvtgpgAERGVVFQNEGllPW---RNVQEN 90
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW----------AERSIAYVPQQ--AWimnATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAF-----GLQLAGVAREQRLNTARDMLKKvGLEG--AEKRFiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
Cdd:PTZ00243 741 ILFfdeedAARLADAVRVSQLEADLAQLGG-GLETeiGEKGV--NLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 493863201 164 REQ-MQTLLLRlwHETGKQVLLITHDIeEAVFMATELVLLspGPGRV 209
Cdd:PTZ00243 818 GERvVEECFLG--ALAGKTRVLATHQV-HVVPRADYVVAL--GDGRV 859
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-187 |
6.17e-12 |
|
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: 64.84 E-value: 6.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEG---KRVTgPGAER---GVVFQ-----NEGLLp 83
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVT-QASLRaaiGIVPQdtvlfNDTIA- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 wrnvqENVAFGLqlAGVAREQRLNTAR--------DMLKK-----VGlEGAEKrfiwqLSGGQRQRVGIARALAANPQLL 150
Cdd:COG5265 450 -----YNIAYGR--PDASEEEVEAAARaaqihdfiESLPDgydtrVG-ERGLK-----LSGGEKQRVAIARTLLKNPPIL 516
|
170 180 190
....*....|....*....|....*....|....*..
gi 493863201 151 LLDEPFGALDAFTREQMQTLLLRLwhETGKQVLLITH 187
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREV--ARGRTTLVIAH 551
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-160 |
9.45e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 6 NLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLegkrvtGPGAERGVVFQN-EGLLPW 84
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI------GETVKLAYVDQSrDALDPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 RNVQENVAFGL---QLAGVAREQRLNTAR------DMLKKVGlegaekrfiwQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:PRK11819 403 KTVWEEISGGLdiiKVGNREIPSRAYVGRfnfkggDQQKKVG----------VLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
....*
gi 493863201 156 FGALD 160
Cdd:PRK11819 473 TNDLD 477
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-163 |
1.42e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.97 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 27 GELLVVLGPSGCGKTTLLNLIA----GFVPYQHGTIHLEG-------KRVTGPgaergVVF--QNEGLLPWRNVQENVAF 93
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpeeikKHYRGD-----VVYnaETDVHFPHLTVGETLDF 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 94 -------GLQLAGVAREQRLNTARDML-----------KKVGLEgaekrFIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:TIGR00956 162 aarcktpQNRPDGVSREEYAKHIADVYmatyglshtrnTKVGND-----FVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
|
....*...
gi 493863201 156 FGALDAFT 163
Cdd:TIGR00956 237 TRGLDSAT 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-196 |
2.68e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 20 INLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGA----ERGVVF-----QNEGL-----LPWr 85
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedrQSSGLyldapLAW- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 86 NV----QENVAFGLQlagVAREQR-LNTARDMLKkVGLEGAEKRfIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK15439 361 NVcaltHNRRGFWIK---PARENAvLERYRRALN-IKFNHAEQA-ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190
....*....|....*....|....*....|....*.
gi 493863201 161 AFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMA 196
Cdd:PRK15439 436 VSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMA 470
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-192 |
2.77e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.72 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 11 YGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGT-IHLEGKRvTGPGAERGVVFQNEGL------LP 83
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNdLTLFGRR-RGSGETIWDIKKHIGYvssslhLD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 84 WRnVQENV----------AFGLQLAGVAREQRLntARDMLKKVGLEG--AEKRFiWQLSGGQRQRVGIARALAANPQLLL 151
Cdd:PRK10938 349 YR-VSTSVrnvilsgffdSIGIYQAVSDRQQKL--AQQWLDILGIDKrtADAPF-HSLSWGQQRLALIVRALVKHPTLLI 424
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493863201 152 LDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEA 192
Cdd:PRK10938 425 LDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-188 |
5.59e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 4 ITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHlegkrvTGPGAERGVVFQ-NEGLL 82
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH------CGTKLEVAYFDQhRAELD 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 83 PWRNVQENVAFGLQLAGVAREQR--LNTARDMLKkvglegAEKRF---IWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:PRK11147 396 PEKTVMDNLAEGKQEVMVNGRPRhvLGYLQDFLF------HPKRAmtpVKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|...
gi 493863201 158 ALDAFTREQMQTLLlrlwheTGKQ--VLLITHD 188
Cdd:PRK11147 470 DLDVETLELLEELL------DSYQgtVLLVSHD 496
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
16-191 |
5.63e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 5.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKrVTGPGAERGVVFQNEGLlpwrnvqENVAFGL 95
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-AALIAISSGLNGQLTGI-------ENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 96 QLAGVAREQrlntARDMLKKVgLEGAE-KRFIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALD-AFTREQMQT 169
Cdd:PRK13545 111 LMMGLTKEK----IKEIIPEI-IEFADiGKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVGDqTFTKKCLDK 185
|
170 180
....*....|....*....|..
gi 493863201 170 llLRLWHETGKQVLLITHDIEE 191
Cdd:PRK13545 186 --MNEFKEQGKTIFFISHSLSQ 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-172 |
7.85e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.72 E-value: 7.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQNEG 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRNVqenvafgLQLAGVAREQRLntaRDMLKKVGLEG-----AEKRFiwqlSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:PRK10636 392 ESPLQHL-------ARLAPQELEQKL---RDYLGGFGFQGdkvteETRRF----SGGEKARLVLALIVWQRPNLLLLDEP 457
|
170
....*....|....*..
gi 493863201 156 FGALDAFTREQMQTLLL 172
Cdd:PRK10636 458 TNHLDLDMRQALTEALI 474
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-215 |
1.03e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.40 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 27 GELLVVLGPSGCGKTTLLNLIAGFVP--YQHGTIHLEG--KRVTGPGAERGVVFQNEGLLPWRNVQENVAFG--LQLAG- 99
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDIRISGfpKKQETFARISGYCEQNDIHSPQVTVRESLIYSafLRLPKe 985
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 100 VAREQRLN--------TARDMLKK--VGLEGaekrfIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE-QMQ 168
Cdd:PLN03140 986 VSKEEKMMfvdevmelVELDNLKDaiVGLPG-----VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAiVMR 1060
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 493863201 169 TllLRLWHETGKQVLLITH----DIEEAVfmaTELVLLSPGpGRVLERLPL 215
Cdd:PLN03140 1061 T--VRNTVDTGRTVVCTIHqpsiDIFEAF---DELLLMKRG-GQVIYSGPL 1105
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
14-166 |
1.09e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 61.68 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVP-YQHGTIHLEGKRVTGPGaergvvfqneglLPW---RNVQE 89
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPpRSDASVVIRGTVAYVPQ------------VSWifnATVRD 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 90 NVAFG-----------LQLAGVAREQRLNTARDmLKKVGLEGAekrfiwQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
Cdd:PLN03130 698 NILFGspfdperyeraIDVTALQHDLDLLPGGD-LTEIGERGV------NISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
|
....*...
gi 493863201 159 LDAFTREQ 166
Cdd:PLN03130 771 LDAHVGRQ 778
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2-189 |
1.11e-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: 61.34 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGkpaleaINLTLDSGEL-----LVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGK-----RVTGPGAE 71
Cdd:COG1245 342 VEYPDLTKSYGG------FSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpQYISPDYD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 72 RGVvfqnEGLLpwRNV----------QENVAFGLQLagvareQRLntardMLKKVGlegaekrfiwQLSGGQRQRVGIAR 141
Cdd:COG1245 416 GTV----EEFL--RSAntddfgssyyKTEIIKPLGL------EKL-----LDKNVK----------DLSGGELQRVAIAA 468
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
15-189 |
2.07e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT---------------------------- 66
Cdd:PTZ00265 1182 PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTndmtneqdyqgdeeqnvgmknvnefslt 1261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 67 --GPGAERGVVFQNEG-------------LLPWRNV-----QENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFI 126
Cdd:PTZ00265 1262 keGGSGEDSTVFKNSGkilldgvdicdynLKDLRNLfsivsQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFI 1341
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 127 WQL---------------SGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PTZ00265 1342 ESLpnkydtnvgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-188 |
3.83e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPAL-EAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKrvtgpgaERGVVFQne 79
Cdd:PLN03073 508 IISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-------VRMAVFS-- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 gllpwrnvQENVAfGLQLA------------GVArEQRLntaRDMLKKVGLEGA-EKRFIWQLSGGQRQRVGIARALAAN 146
Cdd:PLN03073 579 --------QHHVD-GLDLSsnpllymmrcfpGVP-EQKL---RAHLGSFGVTGNlALQPMYTLSGGQKSRVAFAKITFKK 645
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493863201 147 PQLLLLDEPFGALDAFTREQM-QTLLLrlwHETGkqVLLITHD 188
Cdd:PLN03073 646 PHILLLDEPSNHLDLDAVEALiQGLVL---FQGG--VLMVSHD 683
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-193 |
3.90e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGtihlegkrvtgpgaERGVVFQNEG 80
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSG--------------ERQSQFSHIT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 LLPWRNVQENVA-----------------FGLQLAGVAREQRLNTAR--DMLKKVGLEGA-EKRFIwQLSGGQRQRVGIA 140
Cdd:PRK10938 69 RLSFEQLQKLVSdewqrnntdmlspgeddTGRTTAEIIQDEVKDPARceQLAQQFGITALlDRRFK-YLSTGETRKTLLC 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLIT--HDIEEAV 193
Cdd:PRK10938 148 QALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNrfDEIPDFV 202
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-205 |
7.05e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 58.59 E-value: 7.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGK------TTLLNLIAGFVPYQHGT--IHLEGKRVTgPGAERG 73
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**rgalpAHV*GPDAGRRPWRF*TwcANRRALRRT-IG*HRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 74 VVFQNEGLLPWRnvqENVAFGLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:NF000106 93 VR*GRRESFSGR---ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 493863201 154 EPFGALDAFTREQmqtlllrLWHET------GKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:NF000106 170 EPTTGLDPRTRNE-------VWDEVrsmvrdGATVLLTTQYMEEAEQLAHELTVIDRG 220
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
26-189 |
9.21e-10 |
|
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: 57.38 E-value: 9.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 26 SGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVVFQN-------EGLLPWRNVQ-----ENVAF 93
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNyftklleGDVKVIVKPQyvdliPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 94 GLQLAGVAREQRLNTARDMLKKVGLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLR 173
Cdd:cd03236 105 GKVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRE 184
|
170
....*....|....*.
gi 493863201 174 LwHETGKQVLLITHDI 189
Cdd:cd03236 185 L-AEDDNYVLVVEHDL 199
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
12-188 |
9.23e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.21 E-value: 9.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 12 GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGF-VPYqhgtihlEGKRVTGPGAERGVVFQNEGLLPWRNVQEN 90
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVdKEF-------EGEARPAPGIKVGYLPQEPQLDPEKTVREN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAFGLQ--LAGVAR-------------------------------------EQRLNTARDMLK------KVGlegaekrf 125
Cdd:PRK11819 91 VEEGVAevKAALDRfneiyaayaepdadfdalaaeqgelqeiidaadawdlDSQLEIAMDALRcppwdaKVT-------- 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 493863201 126 iwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLlrlwHETGKQVLLITHD 188
Cdd:PRK11819 163 --KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-205 |
1.52e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSAdyggkPAL-EAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVT--GPGA--ERGVVF 76
Cdd:PRK11288 258 LRLDGLKG-----PGLrEPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDaiRAGIML 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 -----QNEGLLPWRNVQENVA---------FGLQLAGvAREQRlnTARDMLKKVGLEGAEKR-FIWQLSGGQRQRVGIAR 141
Cdd:PRK11288 333 cpedrKAEGIIPVHSVADNINisarrhhlrAGCLINN-RWEAE--NADRFIRSLNIKTPSREqLIMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863201 142 ALAANPQLLLLDEPFGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREG 472
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
16-205 |
2.62e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.36 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGkrvtgpgaERGVVFQNEGLLPWRNVQENVAFGL 95
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG--------EVSVIAISAGLSGQLTGIENIEFKM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 96 QLAGVAREQrlntARDMLKKVgLEGAE-KRFIWQ----LSGGQRQRVGIARALAANPQLLLLDEPFGALD-AFTREQMQT 169
Cdd:PRK13546 111 LCMGFKRKE----IKAMTPKI-IEFSElGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQKCLDK 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 493863201 170 llLRLWHETGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK13546 186 --IYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGG 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-189 |
3.03e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.74 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKpALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGP----GAERGVVf 76
Cdd:PRK13409 340 LVEYPDLTKKLGDF-SLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPqyikPDYDGTV- 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 77 qnEGLLpwRNVQENVA---FGLQLAgvareQRLNTARDMLKKVGlegaekrfiwQLSGGQRQRVGIARALAANPQLLLLD 153
Cdd:PRK13409 418 --EDLL--RSITDDLGssyYKSEII-----KPLQLERLLDKNVK----------DLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190
....*....|....*....|....*....|....*.
gi 493863201 154 EPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDI 189
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-187 |
3.65e-09 |
|
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: 55.11 E-value: 3.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGK--PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERgvVFQNE 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED--LRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GLLPwrnvQENVAFGLQLagvareqRLNTAR-DMLKKVGL-------EGAEkrfiwQLSGGQRQRVGIARALAANPQLLL 151
Cdd:cd03369 85 TIIP----QDPTLFSGTI-------RSNLDPfDEYSDEEIygalrvsEGGL-----NLSQGQRQLLCLARALLKRPRVLV 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 493863201 152 LDEPFGALDAFTREQMQtlllRLWHE--TGKQVLLITH 187
Cdd:cd03369 149 LDEATASIDYATDALIQ----KTIREefTNSTILTIAH 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-205 |
3.66e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAIN---LTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQH-GTIHLEGK----RVTGPGAER 72
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDdvsFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFeGNVFINGKpvdiRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 73 GVVFQNE-----GLLPWRNVQENVAFGLqLAGVAREQRLNTARDM------LKKVGLEGAEKRF-IWQLSGGQRQRVGIA 140
Cdd:TIGR02633 337 GIAMVPEdrkrhGIVPILGVGKNITLSV-LKSFCFKMRIDAAAELqiigsaIQRLKVKTASPFLpIGRLSGGNQQKAVLA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-205 |
3.67e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 3.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 27 GELLVVLGPSGCGKTTLLNLIAGFVpyQHGTIHLEGKRVTGPGAER------GVVFQNEGLLPWRNVQENVAFGLQL--- 97
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPLDSsfqrsiGYVQQQDLHLPTSTVRESLRFSAYLrqp 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 98 AGVAREQRLNTARDMLKKVGLEGAEKRFIWQ----LSGGQRQRVGIARALAANPQLLL-LDEPFGALDAFTREQMQTLLL 172
Cdd:TIGR00956 867 KSVSKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMR 946
|
170 180 190
....*....|....*....|....*....|....*
gi 493863201 173 RLwHETGKQVLLITHDiEEAVFMAT--ELVLLSPG 205
Cdd:TIGR00956 947 KL-ADHGQAILCTIHQ-PSAILFEEfdRLLLLQKG 979
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-155 |
5.00e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 20 INLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQH-GTIHLEGKRVT--GP--GAERGVVFQNE-----GLLPWRNVQE 89
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKirNPqqAIAQGIAMVPEdrkrdGIVPVMGVGK 360
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493863201 90 NVAFGL--QLAGVAR---EQRLNTARDMLKKVGLEGAEKRF-IWQLSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:PRK13549 361 NITLAAldRFTGGSRiddAAELKTILESIQRLKVKTASPELaIARLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-58 |
5.13e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 5.13e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTI 58
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-189 |
5.26e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 23 TLDSGELLVVLGPSGCGKTTLLNLIAG-FVPyqhgtiHLeGKRVTGPGAE------RGVVFQN--EGLlpwRNVQENVAF 93
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGeLIP------NL-GDYEEEPSWDevlkrfRGTELQNyfKKL---YNGEIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 94 GLQLAGVAREQRLNTARDMLKKV-------------GLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK13409 165 KPQYVDLIPKVFKGKVRELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*....
gi 493863201 161 AFTREQMQTLLLRLwhETGKQVLLITHDI 189
Cdd:PRK13409 245 IRQRLNVARLIREL--AEGKYVLVVEHDL 271
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-160 |
5.90e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQ--HGTIHLEGKRVTgpgaergvvfqn 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLL------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 eGLLPWRNVQENVAFGLQ----LAGVAREQRLNTARDMLKKVGLEGAEKRFIWQ------------------------LS 130
Cdd:PRK09580 69 -ELSPEDRAGEGIFMAFQypveIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQdlmeekiallkmpedlltrsvnvgFS 147
|
170 180 190
....*....|....*....|....*....|
gi 493863201 131 GGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK09580 148 GGEKKRNDILQMAVLEPELCILDESDSGLD 177
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
18-208 |
9.28e-09 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 54.20 E-value: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 18 EAINLT-LDSGELLVVLGPSGCGKTTLLNLIagfvpyqhgTIHLEGK--RVTGPGAERGVVFQNEGLLpwrnvqeNVAFG 94
Cdd:cd03279 18 QVIDFTgLDNNGLFLICGPTGAGKSTILDAI---------TYALYGKtpRYGRQENLRSVFAPGEDTA-------EVSFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 95 LQLAG----VAREQRLNtARDMLKKVGL-EGAEKRFIWQ----LSGGQRQRVGIARALA----------ANPQLLLLDEP 155
Cdd:cd03279 82 FQLGGkkyrVERSRGLD-YDQFTRIVLLpQGEFDRFLARpvstLSGGETFLASLSLALAlsevlqnrggARLEALFIDEG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 493863201 156 FGALDAFTREQMQTLLLRLwHETGKQVLLITHDIEEAVFMATELVlLSPGPGR 208
Cdd:cd03279 161 FGTLDPEALEAVATALELI-RTENRMVGVISHVEELKERIPQRLE-VIKTPGG 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-207 |
1.29e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.96 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 27 GELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVtgpgaergvvfqnegllpwrnvqenvafglqlagVAREQRL 106
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP----------------------------------VYKPQYI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 107 NtardmlkkvglegaekrfiwqLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLIT 186
Cdd:cd03222 71 D---------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVE 129
|
170 180
....*....|....*....|.
gi 493863201 187 HDIEEAVFMATELVLLSPGPG 207
Cdd:cd03222 130 HDLAVLDYLSDRIHVFEGEPG 150
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-189 |
3.22e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.63 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 23 TLDSGELLVVLGPSGCGKTTLLNLIAG-FVPyqhgtiHLeGKRVTGPGAE------RGVVFQNEgllpWRNVQEN---VA 92
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGeLKP------NL-GDYDEEPSWDevlkrfRGTELQDY----FKKLANGeikVA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 93 FGLQLAGVAREQRLNTARDMLKKV-------------GLEGAEKRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
Cdd:COG1245 164 HKPQYVDLIPKVFKGTVRELLEKVdergkldelaeklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180 190
....*....|....*....|....*....|
gi 493863201 160 DAFTREQMQTLLLRLwHETGKQVLLITHDI 189
Cdd:COG1245 244 DIYQRLNVARLIREL-AEEGKYVLVVEHDL 272
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
128-201 |
1.53e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.95 E-value: 1.53e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493863201 128 QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHETGKQVLLITHDIEEAVFMATELVL 201
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-190 |
2.16e-07 |
|
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: 50.62 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADY--GGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVpYQHGTIHLEgkrvtgpgaerGVVFQNE 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQID-----------GVSWNSV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 80 GLLPWRNvqenvAFGLQ------LAGVAReQRLN-----TARDMLK---KVGLEGAEKRFIWQ-----------LSGGQR 134
Cdd:cd03289 71 PLQKWRK-----AFGVIpqkvfiFSGTFR-KNLDpygkwSDEEIWKvaeEVGLKSVIEQFPGQldfvlvdggcvLSHGHK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 493863201 135 QRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWheTGKQVLLITHDIE 190
Cdd:cd03289 145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAF--ADCTVILSEHRIE 198
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
16-208 |
2.28e-07 |
|
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: 49.63 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 16 ALEAINLTLDSGELLVVLGPSGCGKTTLLNliAGFvpYQHGTIHLEGKRVTGPgaERGVVFQNEgllpwrnVQENVAFGL 95
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGL--YASGKARLISFLPKFS--RNKLIFIDQ-------LQFLIDVGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 96 QLagVAREQRLNTardmlkkvglegaekrfiwqLSGGQRQRVGIARALAANPQ--LLLLDEPFGALDAFTREQMQTLLLR 173
Cdd:cd03238 77 GY--LTLGQKLST--------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKG 134
|
170 180 190
....*....|....*....|....*....|....*
gi 493863201 174 LWHEtGKQVLLITHDiEEAVFMATELVLLSPGPGR 208
Cdd:cd03238 135 LIDL-GNTVILIEHN-LDVLSSADWIIDFGPGSGK 167
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-205 |
5.61e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.11 E-value: 5.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADygGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAERGVvfqneg 80
Cdd:PRK10982 250 ILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAI------ 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 llpwrnvqeNVAFGLqlagVAREQR---------------LNTARDMLKKVGLEGAEK--------------------RF 125
Cdd:PRK10982 322 ---------NHGFAL----VTEERRstgiyayldigfnslISNIRNYKNKVGLLDNSRmksdtqwvidsmrvktpghrTQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 126 IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRLWHEtGKQVLLITHDIEEAVFMATELVLLSPG 205
Cdd:PRK10982 389 IGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-202 |
9.92e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 2 LNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGF----VPYQHGTIHLEgKRVTGPGA------- 70
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHaidgIPKNCQILHVE-QEVVGDDTtalqcvl 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 71 ----ERGVVFQNEGLL--PWRNVQENVAFGL----QLAGVARE---QRLNTARDMLKKVGLEGAE--------------- 122
Cdd:PLN03073 257 ntdiERTQLLEEEAQLvaQQRELEFETETGKgkgaNKDGVDKDavsQRLEEIYKRLELIDAYTAEaraasilaglsftpe 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 123 --KRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLRlWHETgkqVLLITHDIEEAVFMATELV 200
Cdd:PLN03073 337 mqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK-WPKT---FIVVSHAREFLNTVVTDIL 412
|
..
gi 493863201 201 LL 202
Cdd:PLN03073 413 HL 414
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
17-208 |
2.70e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.87 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLlnliaGFvpyqhGTIHLEGKR--VTGPGA---------ERGVVFQNEGLLPW- 84
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSL-----AF-----DTIYAEGQRryVESLSAyarqflgqmDKPDVDSIEGLSPAi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 85 --------RNVQENVA--------FGLQLAGVAREQRLNtardMLKKVGLEGAE-KRFIWQLSGGQRQRVGIARALAANP 147
Cdd:cd03270 81 aidqkttsRNPRSTVGtvteiydyLRLLFARVGIRERLG----FLVDVGLGYLTlSRSAPTLSGGEAQRIRLATQIGSGL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 493863201 148 Q--LLLLDEP-FGALDAFTREQMQTL-LLRlwhETGKQVLLITHDiEEAVFMATELVLLSPGPGR 208
Cdd:cd03270 157 TgvLYVLDEPsIGLHPRDNDRLIETLkRLR---DLGNTVLVVEHD-EDTIRAADHVIDIGPGAGV 217
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
128-204 |
3.67e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 46.45 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 128 QLSGGQRQ------RVGIARALAANPQLLLLDEPFGALDAFTRE-QMQTLLLRLWHETGKQVLLITHDiEEAVFMATELV 200
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFQLIVITHD-EELVDAADHIY 193
|
....
gi 493863201 201 LLSP 204
Cdd:cd03240 194 RVEK 197
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-154 |
3.84e-06 |
|
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: 47.44 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPyqhgtihLEGKRVTGPgaERGVVFqnegLLPWRNVQENvafglq 96
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP-------VYGGRLTKP--AKGKLF----YVPQRPYMTL------ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 97 laGVAREQRL--NTARDMLKK-------------VGLEGAEKRFI-------WQ--LSGGQRQRVGIARALAANPQLLLL 152
Cdd:TIGR00954 529 --GTLRDQIIypDSSEDMKRRglsdkdleqildnVQLTHILEREGgwsavqdWMdvLSGGEKQRIAMARLFYHKPQFAIL 606
|
..
gi 493863201 153 DE 154
Cdd:TIGR00954 607 DE 608
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-252 |
6.67e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.89 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 15 PALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPGAE--RGVVfqneGLLPWRNV--QEN 90
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlRRVL----SIIPQSPVlfSGT 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAFGLQLAGVAREQRLNTA--RDMLKKV------GL-----EGAEkrfiwQLSGGQRQRVGIARALAANPQLLLLDEPFG 157
Cdd:PLN03232 1326 VRFNIDPFSEHNDADLWEAleRAHIKDVidrnpfGLdaevsEGGE-----NFSVGQRQLLSLARALLRRSKILVLDEATA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 158 ALDAFTreqmQTLLLRLWHETGKQ--VLLITH------DIEEAVFMATELVLLSPGPGRVLERLPLEFARRYVAGEPvrs 229
Cdd:PLN03232 1401 SVDVRT----DSLIQRTIREEFKSctMLVIAHrlntiiDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGP--- 1473
|
250 260
....*....|....*....|...
gi 493863201 230 iksdplfiEQREYVLSRVFEQRE 252
Cdd:PLN03232 1474 --------ANAQYLSNLVFERRE 1488
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
18-189 |
1.26e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 45.00 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 18 EAINLTLDSGeLLVVLGPSGCGKTTLLNLIAgFVPY-QHGTIHLEGKRVTGPGAERG---VVFQNEG------------- 80
Cdd:COG0419 15 DTETIDFDDG-LNLIVGPNGAGKSTILEAIR-YALYgKARSRSKLRSDLINVGSEEAsveLEFEHGGkryrierrqgefa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 ---LLPWRNVQENVA--FGLQLAGVAREqRLNTARDMLKK-----VGLEGAEKRF---------IWQLSGGQRQRVGIAR 141
Cdd:COG0419 93 eflEAKPSERKEALKrlLGLEIYEELKE-RLKELEEALESaleelAELQKLKQEIlaqlsgldpIETLSGGERLRLALAD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493863201 142 ALAanpqlLLLDepFGALDAFTREQMQTLLLRLwhetgkqvLLITHDI 189
Cdd:COG0419 172 LLS-----LILD--FGSLDEERLERLLDALEEL--------AIITHVI 204
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-188 |
1.65e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.89 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 14 KPALEAINLTLDSGELLVVLGPSGCGKTTLLN---LIAGFvPYQHGTIHLEGKRvtgpgaergvvfqnegllpwrnvQEN 90
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGG-AQSATRRRSGVKA-----------------------GCI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 91 VAfglqlagvAREQRLNTARDmlkkvglegaekrfiwQLSGGQRQRVGIARALA----ANPQLLLLDEPFGALDAFTREQ 166
Cdd:cd03227 64 VA--------AVSAELIFTRL----------------QLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQA 119
|
170 180
....*....|....*....|..
gi 493863201 167 MQTLLLRLWHEtGKQVLLITHD 188
Cdd:cd03227 120 LAEAILEHLVK-GAQVIVITHL 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-187 |
2.15e-05 |
|
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: 45.32 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 17 LEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEGKRVTGPG-----------AERGVVFQNE---GLL 82
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGlhdlrfkitiiPQDPVLFSGSlrmNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 83 PWRNV-QENVAFGLQLAGVarEQRLNTARDMLKKVGLEGAEkrfiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
Cdd:TIGR00957 1382 PFSQYsDEEVWWALELAHL--KTFVSALPDKLDHECAEGGE-----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170 180
....*....|....*....|....*.
gi 493863201 162 FTREQMQTlLLRLWHETGkQVLLITH 187
Cdd:TIGR00957 1455 ETDNLIQS-TIRTQFEDC-TVLTIAH 1478
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-160 |
6.51e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.65 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGFVPYQHGTIHLEgkrvtgPGAERGVVFQN-- 78
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD------PNERLGKLRQDqf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 79 ---------------EGLlpWRNVQE---------------------NVAFGlQLAGVAREQRlntARDMLKKVGLEgAE 122
Cdd:PRK15064 75 afeeftvldtvimghTEL--WEVKQErdriyalpemseedgmkvadlEVKFA-EMDGYTAEAR---AGELLLGVGIP-EE 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 493863201 123 KRF--IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK15064 148 QHYglMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
113-234 |
2.90e-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: 38.84 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 113 LKKVGLEGAE-KRFIWQLSGGQRQRVGIARALAANPQ--LLLLDEP-FGALDAFTREQMQTLL-LRlwhETGKQVLLITH 187
Cdd:TIGR00630 472 LIDVGLDYLSlSRAAGTLSGGEAQRIRLATQIGSGLTgvLYVLDEPsIGLHQRDNRRLINTLKrLR---DLGNTLIVVEH 548
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 493863201 188 DiEEAVFMATELVLLSPGPGrvlerlplEFARRYVAGEPVRSIKSDP 234
Cdd:TIGR00630 549 D-EDTIRAADYVIDIGPGAG--------EHGGEVVASGTPEEILANP 586
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
104-207 |
3.63e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 104 QRLNTARDMLKKVGLEG-AEKRFIWQLSGGQRQRVGIARALAAnpQLL----LLDEPFGALDAFTREQMQTLLLRLwHET 178
Cdd:PRK00635 451 QGLKSRLSILIDLGLPYlTPERALATLSGGEQERTALAKHLGA--ELIgityILDEPSIGLHPQDTHKLINVIKKL-RDQ 527
|
90 100
....*....|....*....|....*....
gi 493863201 179 GKQVLLITHDiEEAVFMATELVLLSPGPG 207
Cdd:PRK00635 528 GNTVLLVEHD-EQMISLADRIIDIGPGAG 555
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-160 |
8.62e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.07 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 1 MLNITNLSADYGGKPALEAINLTLDSGELLVVLGPSGCGKTTLLNLIAGfvpyqhgTIHLEGKRVTGPGAERgvvfqneg 80
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKN-------EISADGGSYTFPGNWQ-------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 81 lLPWRNvQENVAFGL--------------QLagvarEQRLNTARD----------------------------MLKKVGL 118
Cdd:PRK10636 66 -LAWVN-QETPALPQpaleyvidgdreyrQL-----EAQLHDANErndghaiatihgkldaidawtirsraasLLHGLGF 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 493863201 119 EGAE-KRFIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
Cdd:PRK10636 139 SNEQlERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-155 |
9.65e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.08 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493863201 20 INLTLDSGELLVVLGPSGCGKTTLLNLIAG--FVPYQHGTIHLEGKRV---TGPGA-ERGVVFQNE-----GLLPWRNVQ 88
Cdd:NF040905 279 VSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVdvsTVSDAiDAGLAYVTEdrkgyGLNLIDDIK 358
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493863201 89 ENVAFGlQLAGVAREQRLNTARDMlkKVGlEGAEKRF------IWQ----LSGGQRQRVGIARALAANPQLLLLDEP 155
Cdd:NF040905 359 RNITLA-NLGKVSRRGVIDENEEI--KVA-EEYRKKMniktpsVFQkvgnLSGGNQQKVVLSKWLFTDPDVLILDEP 431
|
|
| |
