|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
28-258 |
8.94e-93 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 273.89 E-value: 8.94e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGLLPWRTVMENIALGLEVRsfyg 107
Cdd:COG1116 33 TVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGVVFQEPALLPWLTVLDNVALGLELR---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 108 pdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEL 187
Cdd:COG1116 109 -------GVPKAER-RERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 188 TLKLQAERGLTVITVTHSIEEAAFLGRKILCLGHPPHR--EPVVVEGPPPK----RDHPDFYKVCSKLRSILEEGRR 258
Cdd:COG1116 181 LLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRivEEIDVDLPRPRdrelRTSPEFAALRAEILDLLREEAE 257
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
24-225 |
2.61e-84 |
|
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: 250.85 E-value: 2.61e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 24 NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGLLPWRTVMENIALGLEVR 103
Cdd:cd03293 22 DISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 sfygpdGLHAPKRplpeapDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRES 183
Cdd:cd03293 102 ------GVPKAEA------RERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490467399 184 LEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGHPPHR 225
Cdd:cd03293 170 LQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGR 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
29-244 |
4.30e-65 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 203.56 E-value: 4.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGLLPWRTVMENIALGLEVRsfygp 108
Cdd:COG4525 30 IESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGVVFQKDALLPWLNVLDNVAFGLRLR----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 dGLHAPKRplpeapDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELT 188
Cdd:COG4525 105 -GVPKAER------RARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 189 LKLQAERGLTVITVTHSIEEAAFLGRKILCLGHPPHRepvVVEgpppkRDHPDFYK 244
Cdd:COG4525 178 LDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGR---IVE-----RLELDFSR 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-219 |
5.01e-65 |
|
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: 201.59 E-value: 5.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHlPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRP---DSALILQ 82
Cdd:cd03259 1 LELKGLSKTYGSV-RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPerrNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 83 DFGLLPWRTVMENIALGLEVRsfygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVL 162
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLR-----------GVPKAEI-RARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 163 GPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVM 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
27-216 |
2.63e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 195.26 E-value: 2.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERpRPDSAL----------ILQDFGLLPWRTVMENI 96
Cdd:COG1136 29 LSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS-LSERELarlrrrhigfVFQFFNLLPELTALENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALGLEVRsfygpdGLHAPKRplpeapDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:COG1136 108 ALPLLLA------GVSRKER------RERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:COG1136 176 DSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVI 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
28-209 |
7.63e-61 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 195.32 E-value: 7.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER--P-RPDSALILQDFGLLPWRTVMENIALGLEVRs 104
Cdd:COG3842 27 SIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGlpPeKRNVGMVFQDYALFPHLTVAENVAFGLRMR- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:COG3842 106 ----------GVPKAEI-RARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEM 174
|
170 180
....*....|....*....|....*
gi 1490467399 185 EELTLKLQAERGLTVITVTHSIEEA 209
Cdd:COG3842 175 REELRRLQRELGITFIYVTHDQEEA 199
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-216 |
2.97e-59 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 191.44 E-value: 2.97e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFAWKphlplflnfwwhlkKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV---KLERPRPDSALILQDF 84
Cdd:COG3839 19 LKDIDLDIE--------------DGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtDLPPKDRNIAMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 GLLPWRTVMENIALGLEVRsfygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGP 164
Cdd:COG3839 85 ALYPHMTVYENIAFPLKLR-----------KVPKAEI-DRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 165 DLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRI 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
28-216 |
8.87e-58 |
|
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: 183.07 E-value: 8.87e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPrPDSAL----------ILQDFGLLPWRTVMENIA 97
Cdd:cd03255 26 SIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKL-SEKELaafrrrhigfVFQSFNLLPDLTALENVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 LGLEVRsfygpdglhapKRPLPEAPDAlVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:cd03255 105 LPLLLA-----------GVPKKERRER-AEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLD 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1490467399 178 APTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:cd03255 173 SETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRII 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
29-243 |
6.95e-54 |
|
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: 173.81 E-value: 6.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGLLPWRTVMENIALglevrsfygp 108
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIAL---------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 dglhAPKRPLPEAP----DALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:TIGR01184 78 ----AVDRVLPDLSkserRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 185 EELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGHPPHR---EPVVVEGPPPKR-----DHPDFY 243
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAAnigQILEVPFPRPRDrlevvEDPSYY 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-221 |
8.30e-54 |
|
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: 172.82 E-value: 8.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLfLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRP---DSALILQ 82
Cdd:cd03301 1 VELENVTKRFGNVTAL-DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPkdrDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 83 DFGLLPWRTVMENIALGLEVRsfygpdglHAPKRPLpeapDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVL 162
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLR--------KVPKDEI----DERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490467399 163 GPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMND 206
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-242 |
3.82e-53 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 172.58 E-value: 3.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGLLPWRTVMENIALGLEVRsfygp 108
Cdd:PRK11248 24 LESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAFGLQLA----- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 dGLHAPKRplpeapDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELT 188
Cdd:PRK11248 99 -GVEKMQR------LEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 189 LKLQAERGLTVITVTHSIEEAAFLGRKILCLGHPPHRepvVVEgpppkRDHPDF 242
Cdd:PRK11248 172 LKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGR---VVE-----RLPLNF 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-234 |
5.82e-52 |
|
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: 168.66 E-value: 5.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLF--LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP-----RPDSA 78
Cdd:COG1122 1 IELENLSFSYPGGTPALddVSL--SIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnlrelRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQD-----FGllpwRTVMENIALGLEVRsfygpdGLhapkrPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQR 153
Cdd:COG1122 79 LVFQNpddqlFA----PTVEEDVAFGPENL------GL-----PREEI-RERVEEALELVGLEHLADRPPHELSGGQKQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 154 TAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAErGLTVITVTHSIEEAAFLGRKILCLGHppHRepVVVEGP 233
Cdd:COG1122 143 VAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDD--GR--IVADGT 217
|
.
gi 1490467399 234 P 234
Cdd:COG1122 218 P 218
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
30-216 |
7.96e-52 |
|
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: 169.75 E-value: 7.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL---------ERPRPDSALILQDFGLLPWRTVMENIALGL 100
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsrkelrELRRKKISMVFQSFALLPHRTVLENVAFGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRsfygpdGLHAPKRpLPEAPDALvdywlKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:cd03294 128 EVQ------GVPRAER-EERAAEAL-----ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190
....*....|....*....|....*....|....*.
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDLDEALRLGDRI 231
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
28-207 |
5.12e-51 |
|
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: 166.60 E-value: 5.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV--------KLERPRPDSALILQDFGLLPWRTVMENIALG 99
Cdd:cd03258 27 SVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTdltllsgkELRKARRRIGMIFQHFNLLSSRTVFENVALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVrsfygpdgLHAPKRPLPEAPDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:cd03258 107 LEI--------AGVPKAEIEERVLEL----LELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180
....*....|....*....|....*...
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIE 207
Cdd:cd03258 175 TTQSILALLRDINRELGLTIVLITHEME 202
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
28-222 |
1.58e-50 |
|
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: 163.51 E-value: 1.58e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-------PRPDSALILQDFGLLPWRTVMENIALGL 100
Cdd:cd03229 22 NIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledelppLRRRIGMVFQDFALFPHLTVLENIALGL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 evrsfygpdglhapkrplpeapdalvdywlkrlgleavadhypsqiSGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:cd03229 102 ----------------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGHP 222
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
36-209 |
3.22e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 168.02 E-value: 3.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRP----DSALILQDFGLLPWRTVMENIALGLEVRsfygpdgl 111
Cdd:COG1118 32 ALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPprerRVGFVFQHYALFPHMTVAENIAFGLRVR-------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 112 hapkRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKL 191
Cdd:COG1118 104 ----PPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRL 179
|
170
....*....|....*...
gi 1490467399 192 QAERGLTVITVTHSIEEA 209
Cdd:COG1118 180 HDELGGTTVFVTHDQEEA 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
6-221 |
7.41e-50 |
|
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: 163.63 E-value: 7.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG--------VKLERprpDS 77
Cdd:cd03295 1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpVELRR---KI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 78 ALILQDFGLLPWRTVMENIALGlevrsfygPDGLHAPKrplpEAPDALVDYWLKRLGLEAV--ADHYPSQISGGQRQRTA 155
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALV--------PKLLKWPK----EKIRERADELLALVGLDPAefADRYPHELSGGQQQRVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 156 IGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKN 211
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
30-221 |
7.87e-50 |
|
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: 167.14 E-value: 7.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRP---DSALILQDFGLLPWRTVMENIALGLEvrsfy 106
Cdd:TIGR03265 28 KKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPqkrDYGIVFQSYALFPNLTVADNIAYGLK----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 gpdglhaPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEE 186
Cdd:TIGR03265 103 -------NRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVREHLRT 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 187 LTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:TIGR03265 176 EIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNH 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-204 |
2.02e-49 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 162.47 E-value: 2.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 9 KGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP-------RPDSALIL 81
Cdd:COG1126 18 KGISL--------------DVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSkkdinklRRKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 82 QDFGLLPWRTVMENIALGLevrsfygpdgLHAPKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALV 161
Cdd:COG1126 84 QQFNLFPHLTVLENVTLAP----------IKVKKMSKAEA-EERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 162 LGPDLLLMDEPFSSLDaP--TRESLEelTLKLQAERGLTVITVTH 204
Cdd:COG1126 153 MEPKVMLFDEPTSALD-PelVGEVLD--VMRDLAKEGMTMVVVTH 194
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
28-234 |
4.44e-49 |
|
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: 161.69 E-value: 4.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-PRPDSALILQDFG-------LLPWRTVMENIALG 99
Cdd:COG1127 27 DVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYELRRRIGmlfqggaLFDSLTVFENVAFP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVRSfygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:COG1127 107 LREHT----------DLSEAEI-RELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:COG1127 176 TSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVL----ADGKIIAEGTP 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
9-210 |
3.58e-48 |
|
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: 159.14 E-value: 3.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 9 KGIDFAwkphlplflnfwwhLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL----ERPRpdSAL----- 79
Cdd:COG4181 29 KGISLE--------------VEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDAR--ARLrarhv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 --ILQDFGLLPWRTVMENIALGLEVRSfygpdglHAPKRPLPEApdalvdyWLKRLGLEAVADHYPSQISGGQRQRTAIG 157
Cdd:COG4181 93 gfVFQSFQLLPTLTALENVMLPLELAG-------RRDARARARA-------LLERVGLGHRLDHYPAQLSGGEQQRVALA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:COG4181 159 RAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAA 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
27-219 |
1.00e-47 |
|
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: 157.24 E-value: 1.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV-----KLERPRPDSALILQD-----FGLlpwrTVMENI 96
Cdd:cd03225 22 LTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKdltklSLKELRRKVGLVFQNpddqfFGP----TVEEEV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALGLEvrsfygpdglhapKRPLPEAP-DALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:cd03225 98 AFGLE-------------NLGLPEEEiEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1490467399 176 LDAPTRESLEELTLKLQAErGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:cd03225 165 LDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-217 |
1.34e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 157.61 E-value: 1.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL------ERPrpdSALILQDFGLLPWRTVMENI 96
Cdd:COG3840 16 LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLtalppaERP---VSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALGLevrsfygpdglhAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:COG3840 93 GLGL------------RPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKIL 217
Cdd:COG3840 161 DPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVL 201
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
6-222 |
1.99e-47 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 157.56 E-value: 1.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLF-LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDF 84
Cdd:COG1121 7 IELENLTVSYGGRPVLEdVSL--TIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 GLlPWR---TVMENIALGLevrsfYGPDGLHapkRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALV 161
Cdd:COG1121 85 EV-DWDfpiTVRDVVLMGR-----YGRRGLF---RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 162 LGPDLLLMDEPFSSLDAPTRESLEELtLKLQAERGLTVITVTHSIEEA-------AFLGRKILCLGHP 222
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYEL-LRELRREGKTILVVTHDLGAVreyfdrvLLLNRGLVAHGPP 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
29-240 |
2.90e-47 |
|
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: 156.89 E-value: 2.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS--------ALILQDFGLLPWRTVMENIALGL 100
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyrlrrrmGMLFQSGALFDSLTVFENVAFPL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSfygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:cd03261 103 REHT----------RLSEEEI-REIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPPP---KRDHP 240
Cdd:cd03261 172 SGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVL----YDGKIVAEGTPEelrASDDP 230
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
23-216 |
7.69e-47 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 157.95 E-value: 7.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG--------VKLERPrpdsalI---LQDFGLLPWRT 91
Cdd:COG1125 21 LSL--TIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGedirdldpVELRRR------IgyvIQQIGLFPHMT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 92 VMENIALgleVrsfygPDGLHAPKrplpEAPDALVDYWLKRLGLEA--VADHYPSQISGGQRQRTAIGRALVLGPDLLLM 169
Cdd:COG1125 93 VAENIAT---V-----PRLLGWDK----ERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADPPILLM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490467399 170 DEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:COG1125 161 DEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRI 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
30-211 |
1.45e-46 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 154.22 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALI-------LQDFGLLPWRTVMENIALGL-E 101
Cdd:cd03262 24 KKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkvgmvFQQFNLFPHLTVLENITLAPiK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 VRsfygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT- 180
Cdd:cd03262 104 VK-----------GMSKAEA-EERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELv 171
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 181 RESLEelTLKLQAERGLTVITVTHsieEAAF 211
Cdd:cd03262 172 GEVLD--VMKDLAEEGMTMVVVTH---EMGF 197
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-209 |
3.22e-46 |
|
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: 154.32 E-value: 3.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 5 FVEVKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL------ERPrpdSA 78
Cdd:cd03300 13 FVALDGVSL--------------DIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItnlpphKRP---VN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQDFGLLPWRTVMENIALGLEVRSfygpdglhapkrpLPEAP-DALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIG 157
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKK-------------LPKAEiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIA 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEA 209
Cdd:cd03300 143 RALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEA 194
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
6-219 |
4.42e-46 |
|
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: 154.03 E-value: 4.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRP---DSALILQ 82
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSL--EVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPekrDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 83 DFGLLPWRTVMENIALGLEVRsfygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVL 162
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKR-----------KVDKKEI-ERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 163 GPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIM 203
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
8-221 |
4.83e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.68 E-value: 4.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER----PRPDSALILQD 83
Cdd:COG1131 16 LDGVSL--------------TVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARdpaeVRRRIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 84 FGLLPWRTVMENIALgleVRSFYGPDGLHAPKRplpeapdalVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLG 163
Cdd:COG1131 82 PALYPDLTVRENLRF---FARLYGLPRKEARER---------IDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 164 PDLLLMDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDK 206
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-212 |
2.16e-45 |
|
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: 158.91 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFAwkphlplflnfwwhLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS--------AL 79
Cdd:COG1123 281 VDDVSLT--------------LRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSlrelrrrvQM 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQD-FG-LLPWRTVMENIALGLEVRSFYGPdglhapkrplpEAPDALVDYWLKRLGL-EAVADHYPSQISGGQRQRTAI 156
Cdd:COG1123 347 VFQDpYSsLNPRMTVGDIIAEPLRLHGLLSR-----------AERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 157 GRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFL 212
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYI 471
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
8-217 |
3.71e-45 |
|
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: 151.12 E-value: 3.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP--------RPDSAL 79
Cdd:cd03257 21 LDDVSF--------------SIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrrlrkirRKEIQM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQD-FGLL-PWRTVMENIALGLEVrsfygpdglHAPKRPlPEAPDALVDYWLKRLGL-EAVADHYPSQISGGQRQRTAI 156
Cdd:cd03257 87 VFQDpMSSLnPRMTIGEQIAEPLRI---------HGKLSK-KEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 157 GRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKIL 217
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-217 |
6.14e-45 |
|
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: 150.14 E-value: 6.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 31 KGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV-------KLERPRPDS--ALILQDFGLLPWRTVMENIALGLE 101
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsrkKINLPPQQRkiGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 VRSfygpdglhapKRPLPEAPDALVDYwlkrLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:cd03297 102 RKR----------NREDRISVDELLDL----LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190
....*....|....*....|....*....|....*.
gi 1490467399 182 ESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKIL 217
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
6-216 |
6.23e-45 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 154.08 E-value: 6.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS---ALILQ 82
Cdd:NF040840 2 IRIENLSKDWKEFKLRDISL--EVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKrgiAYVYQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 83 DFGLLPWRTVMENIALGLEVRsfygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVL 162
Cdd:NF040840 80 NYMLFPHKTVFENIAFGLKLR-----------KVPKEEI-ERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALII 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 163 GPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:NF040840 148 EPKLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLADRV 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
29-224 |
1.43e-44 |
|
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: 149.22 E-value: 1.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPR------PDSALILQDFGLlpwrTVMENIALGLev 102
Cdd:cd03235 22 VKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERkrigyvPQRRSIDRDFPI----SVRDVVLMGL-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsfYGPDGLHapkRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRE 182
Cdd:cd03235 96 ---YGHKGLF---RRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490467399 183 SLEELTLKLQAErGLTVITVTHSIEEAAFLGRKILCLGHPPH 224
Cdd:cd03235 170 DIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
28-219 |
5.68e-44 |
|
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: 148.64 E-value: 5.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS---ALILQDFGLLPWRTVMENIALGLEVRs 104
Cdd:cd03296 24 DIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQErnvGFVFQHYALFRHMTVFDNVAFGLRVK- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdglHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:cd03296 103 -------PRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKEL 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 185 EELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:cd03296 176 RRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVM 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
28-207 |
9.16e-44 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 151.00 E-value: 9.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERpRPDSAL---------ILQDFGLLPWRTVMENIAL 98
Cdd:COG1135 27 TIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA-LSERELraarrkigmIFQHFNLLSSRTVAENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 GLEVrsfygpDGLHAPKRplpeapDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:COG1135 106 PLEI------AGVPKAEI------RKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180
....*....|....*....|....*....
gi 1490467399 179 PTRESLEELTLKLQAERGLTVITVTHSIE 207
Cdd:COG1135 174 ETTRSILDLLKDINRELGLTIVLITHEMD 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
28-217 |
1.57e-43 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 147.90 E-value: 1.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGLLPWRTVMENIALGLevRSFYG 107
Cdd:PRK11247 34 HIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLMFQDARLLPWKKVIDNVGLGL--KGQWR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 108 PDGLHApkrplpeapdalvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEL 187
Cdd:PRK11247 112 DAALQA----------------LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 188 TLKLQAERGLTVITVTHSIEEA-AFLGRKIL 217
Cdd:PRK11247 176 IESLWQQHGFTVLLVTHDVSEAvAMADRVLL 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-207 |
1.79e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 146.74 E-value: 1.79e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGEsWA-IIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-PRPDSAL-------ILQDFGLLPWRTVM 93
Cdd:COG2884 21 VSL--EIEKGE-FVfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYlrrrigvVFQDFRLLPDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 94 ENIALGLEVRsfygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPF 173
Cdd:COG2884 98 ENVALPLRVT-----------GKSRKEI-RRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190
....*....|....*....|....*....|....
gi 1490467399 174 SSLDAPTRESLEELTLKLQAeRGLTVITVTHSIE 207
Cdd:COG2884 166 GNLDPETSWEIMELLEEINR-RGTTVLIATHDLE 198
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-221 |
2.41e-43 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.11 E-value: 2.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 7 EVKGIDFAWKpHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----ALIL 81
Cdd:COG4619 2 ELEGLSFRVG-GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrrqvAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 82 QDFGLlpWR-TVMENIALGLEVRSfygpdglhapKRPLPEApdalVDYWLKRLGL-EAVADHYPSQISGGQRQRTAIGRA 159
Cdd:COG4619 81 QEPAL--WGgTVRDNLPFPFQLRE----------RKFDRER----ALELLERLGLpPDILDKPVERLSGGERQRLALIRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 160 LVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:COG4619 145 LLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
28-221 |
3.33e-43 |
|
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: 146.87 E-value: 3.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----ALILQD-FGLL-PWRTVMENIALGL 100
Cdd:COG1124 27 EVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrrrvQMVFQDpYASLhPRHTVDRILAEPL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 evRSFYGPDglhapkrplpeaPDALVDYWLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:COG1124 107 --RIHGLPD------------REERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:COG1124 173 VQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQN 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-210 |
1.87e-42 |
|
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: 144.62 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 7 EVKGIDFAWKpHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERpRPDSAL-----IL 81
Cdd:COG4555 3 EVENLSKKYG-KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARrqigvLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 82 QDFGLLPWRTVMENIALgleVRSFYGPDGLHAPKRplpeapdalVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALV 161
Cdd:COG4555 81 DERGLYDRLTVRENIRY---FAELYGLFDEELKKR---------IEELIELLGLEEFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490467399 162 LGPDLLLMDEPFSSLDAPTRESLEELtLKLQAERGLTVITVTHSIEEAA 210
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREI-LRALKKEGKTVLFSSHIMQEVE 196
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-234 |
2.42e-42 |
|
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: 147.55 E-value: 2.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-----------VKLERpRPdSALILQDFGLLPWRTVMENIALGLEvrs 104
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlqdsargifLPPHR-RR-IGYVFQEARLFPHLSVRGNLLYGRK--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdglHAPKRPLPEAPDALVDywlkRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:COG4148 104 -------RAPRAERRISFDEVVE----LLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 185 EELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL--GHpphrepVVVEGPP 234
Cdd:COG4148 173 LPYLERLRDELDIPILYVSHSLDEVARLADHVVLLeqGR------VVASGPL 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
28-209 |
4.14e-42 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 144.04 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV--------KLERPRPDSALILQDFGLLPWRTVMENIALG 99
Cdd:COG3638 25 EIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQdvtalrgrALRRLRRRIGMIFQQFNLVPRLSVLTNVLAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 L-----EVRSFYGpdglHAPKRPLPEAPDALvdywlKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:COG3638 105 RlgrtsTWRSLLG----LFPPEDRERALEAL-----ERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVA 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 175 SLDAPTRESLEELTLKLQAERGLTVITVTHSIEEA 209
Cdd:COG3638 176 SLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLA 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
28-234 |
2.14e-41 |
|
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: 142.49 E-value: 2.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-PRPDSA----LILQD----FGLlpwrTVMENIAL 98
Cdd:COG1120 23 SLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELArriaYVPQEppapFGL----TVRELVAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 GlevRSFYgpdglHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:COG1120 99 G---RYPH-----LGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 179 PTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL--GHpphrepVVVEGPP 234
Cdd:COG1120 171 AHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLkdGR------IVAQGPP 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
28-234 |
6.04e-41 |
|
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: 140.78 E-value: 6.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV--------KLERPRPDSALILQDFGLLPWRTVMENIALG 99
Cdd:cd03256 23 SINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinklkgkALRQLRRQIGMIFQQFNLIERLSVLENVLSG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 -LEVRSFygpdgLHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:cd03256 103 rLGRRST-----WRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 179 PTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL--GHpphrepVVVEGPP 234
Cdd:cd03256 178 ASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLkdGR------IVFDGPP 229
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-216 |
9.91e-41 |
|
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: 142.63 E-value: 9.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 37 IIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL-ERP---RPdSALILQDFGLLPWRTVMENIALGLEVRsfygpdglh 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVtNVPphlRH-INMVFQSYALFPHMTVEENVAFGLKMR--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 113 apKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQ 192
Cdd:TIGR01187 71 --KVPRAEI-KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQ 147
|
170 180
....*....|....*....|....
gi 1490467399 193 AERGLTVITVTHSIEEAAFLGRKI 216
Cdd:TIGR01187 148 EQLGITFVFVTHDQEEAMTMSDRI 171
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
31-219 |
2.35e-40 |
|
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: 138.39 E-value: 2.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 31 KGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL------ERPrpdSALILQDFGLLPWRTVMENIALGLevrs 104
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVtaappaDRP---VSMLFQENNLFAHLTVEQNVGLGL---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdglhAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:cd03298 96 --------SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 185 EELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:cd03298 168 LDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
8-234 |
9.19e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 143.89 E-value: 9.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQG---GEVRIGGVKLERPRP-----DSAL 79
Cdd:COG1123 22 VDGVSL--------------TIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEalrgrRIGM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFG--LLPWrTVMENIALGLEVRSFYgpdglhapkrplPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIG 157
Cdd:COG1123 88 VFQDPMtqLNPV-TVGDQIAEALENLGLS------------RAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVM----DDGRIVEDGPP 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
29-234 |
1.09e-39 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 137.53 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALI-------LQDFGLLPWRTVMENIALG-L 100
Cdd:PRK09493 24 IDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeagmvFQQFYLFPHLTALENVMFGpL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSfygpdglhAPKrplpEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:PRK09493 104 RVRG--------ASK----EEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 181 REslEELT-LKLQAERGLTVITVTHSIEEAAFLGRKILCL--GHpphrepVVVEGPP 234
Cdd:PRK09493 172 RH--EVLKvMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIdkGR------IAEDGDP 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
20-221 |
1.10e-39 |
|
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: 136.45 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS----ALILQDFGLLPWRTVMEN 95
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYrrrlAYLGHADGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 96 IALgleVRSFYGPDglhapkrplpeAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:COG4133 96 LRF---WAALYGLR-----------ADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1490467399 176 LDAPTRESLEELtLKLQAERGLTVITVTHSIEEAAFLgrKILCLGH 221
Cdd:COG4133 162 LDAAGVALLAEL-IAAHLARGGAVLLTTHQPLELAAA--RVLDLGD 204
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-207 |
3.12e-39 |
|
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: 134.05 E-value: 3.12e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL---NFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS----- 77
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLkdvSL--TIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESlrkni 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 78 ALILQDFGLLPwRTVMENIalglevrsfygpdglhapkrplpeapdalvdywlkrlgleavadhypsqISGGQRQRTAIG 157
Cdd:cd03228 79 AYVPQDPFLFS-GTIRENI-------------------------------------------------LSGGQRQRIAIA 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERglTVITVTHSIE 207
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLS 156
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
28-207 |
4.65e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.78 E-value: 4.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV--------KLERPRPDSALILQDFGLLPWRTVMENIALG 99
Cdd:PRK11153 27 HIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdltalsekELRKARRQIGMIFQHFNLLSSRTVFDNVALP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVrsfygpDGLhaPKrplpEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:PRK11153 107 LEL------AGT--PK----AEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
|
170 180
....*....|....*....|....*...
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIE 207
Cdd:PRK11153 175 TTRSILELLKDINRELGLTIVLITHEMD 202
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
18-210 |
5.08e-39 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 135.48 E-value: 5.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 18 HLPLFLNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP----RPDSALiLQDFGLLPWRTVM 93
Cdd:PRK10771 13 HLPMRFDL--TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTppsrRPVSML-FQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 94 ENIALGLevrsfygpdglhAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPF 173
Cdd:PRK10771 90 QNIGLGL------------NPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1490467399 174 SSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAA 194
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-209 |
9.62e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 141.84 E-value: 9.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLF--LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----A 78
Cdd:COG1132 340 IEFENVSFSYPGDRPVLkdISL--TIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESlrrqiG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQDFGLLPwRTVMENIALGlevrsfygpdglhapkrpLPEAPDALVDYWLKRLGLEAVADHYP-----------SQIS 147
Cdd:COG1132 418 VVPQDTFLFS-GTIRENIRYG------------------RPDATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLS 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490467399 148 GGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT----RESLEELTlklqaeRGLTVITVTH---SIEEA 209
Cdd:COG1132 479 GGQRQRIAIARALLKDPPILILDEATSALDTETealiQEALERLM------KGRTTIVIAHrlsTIRNA 541
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
7-219 |
1.22e-38 |
|
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: 132.37 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 7 EVKGIDFAWKPHlPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPdsALILQDFGL 86
Cdd:cd00267 1 EIENLSFRYGGR-TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL--EELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 87 LPwrtvmenialglevrsfygpdglhapkrplpeapdalvdywlkrlgleavadhypsQISGGQRQRTAIGRALVLGPDL 166
Cdd:cd00267 78 VP--------------------------------------------------------QLSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 167 LLMDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
29-204 |
1.64e-38 |
|
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: 133.99 E-value: 1.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP--------RPDSALILQDFGLLPWRTVMENIALGL 100
Cdd:TIGR02982 28 INPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGAskkqlvqlRRRIGYIFQAHNLLGFLTARQNVQMAL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSFYGPdglhapkrplpEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:TIGR02982 108 ELQPNLSY-----------QEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKS 176
|
170 180
....*....|....*....|....
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTH 204
Cdd:TIGR02982 177 GRDVVELMQKLAKEQGCTILMVTH 200
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
6-204 |
2.00e-38 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 141.90 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL---NFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS----- 77
Cdd:COG2274 474 IELENVSFRYPGDSPPVLdniSL--TIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASlrrqi 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 78 ALILQDFGLLPwRTVMENIALGlevrsfygpdglhapkrpLPEAPDALVDYWLKRLGLEAVADHYP-----------SQI 146
Cdd:COG2274 552 GVVLQDVFLFS-GTIRENITLG------------------DPDATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNL 612
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 147 SGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEElTLKlQAERGLTVITVTH 204
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILE-NLR-RLLKGRTVIIIAH 668
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
29-209 |
8.50e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 136.23 E-value: 8.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSA---LILQDFGLLPWRTVMENIALGLEVRsf 105
Cdd:PRK09452 37 INNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRhvnTVFQSYALFPHMTVFENVAFGLRMQ-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 106 ygpdglhapKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLe 185
Cdd:PRK09452 115 ---------KTPAAEI-TPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM- 183
|
170 180
....*....|....*....|....*
gi 1490467399 186 ELTLK-LQAERGLTVITVTHSIEEA 209
Cdd:PRK09452 184 QNELKaLQRKLGITFVFVTHDQEEA 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
29-204 |
1.06e-37 |
|
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: 132.86 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPD--SAL-------ILQDFGLLpwrTVMENIALG 99
Cdd:COG0411 27 VERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHriARLgiartfqNPRLFPEL---TVLENVLVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVR--SFYGPDGLHAPKRPLPEAP-DALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:COG0411 104 AHARlgRGLLAALLRLPRARREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGL 183
|
170 180
....*....|....*....|....*...
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:COG0411 184 NPEETEELAELIRRLRDERGITILLIEH 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-221 |
1.22e-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: 138.74 E-value: 1.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLF--LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----A 78
Cdd:COG4988 337 IELEDVSFSYPGGRPALdgLSL--TIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrrqiA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQDFGLLPWrTVMENIALGlevrsfygpdglhapkrpLPEAPDALVDYWLKRLGLEAVADHYP-----------SQIS 147
Cdd:COG4988 415 WVPQNPYLFAG-TIRENLRLG------------------RPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLS 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 148 GGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERglTVITVTHSIEEAAFLGRkILCLGH 221
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADR-ILVLDD 546
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
29-214 |
2.05e-37 |
|
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: 130.93 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER--PRPDSALILQDFG-------LLPWRTVMENIALG 99
Cdd:TIGR02211 28 IGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKlsSNERAKLRNKKLGfiyqfhhLLPDFTALENVAMP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVRsfygpdglHAPKRPLPEAPDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:TIGR02211 108 LLIG--------KKSVKEAKERAYEM----LEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNN 175
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIEEAAFLGR 214
Cdd:TIGR02211 176 NAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDR 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
30-245 |
2.13e-37 |
|
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: 131.65 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV--------RIGGVKLERPRPDSALILQDFGLLPWRTVMENIALGle 101
Cdd:TIGR02315 26 NPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIllegtditKLRGKKLRKLRRRIGMIFQHYNLIERLTVLENVLHG-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 vRSFYGPdGLHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:TIGR02315 104 -RLGYKP-TWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTS 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 182 ESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL--GHpphrepVVVEGPPPKRDHPDFYKV 245
Cdd:TIGR02315 182 KQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLkaGE------IVFDGAPSELDDEVLRHI 241
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
27-174 |
2.96e-37 |
|
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: 128.53 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL-----ERPRPDSALILQDFGLLPWRTVMENIALGLE 101
Cdd:pfam00005 6 LTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderKSLRKEIGYVFQDPQLFPRLTVRENLRLGLL 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 102 VrsfygpdglhapKRPLPEAPDALVDYWLKRLGLEAVADH----YPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:pfam00005 86 L------------KGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
32-237 |
4.10e-36 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 131.27 E-value: 4.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQG--GEVRIGGVKLERPRPDS---ALILQDFGLLPWRTVMENIALGLEVRsfy 106
Cdd:TIGR03258 31 GELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADRDLTHAPPHKrglALLFQNYALFPHLKVEDNVAFGLRAQ--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 gpdglhapKRPLPEAPDALVDYwLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEE 186
Cdd:TIGR03258 108 --------KMPKADIAERVADA-LKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMRE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 187 LTLKLQAE-RGLTVITVTHSIEEAAFLGRKILCLGH---PPHREPVVVEGPPPKR 237
Cdd:TIGR03258 179 EIAALHEElPELTILCVTHDQDDALTLADKAGIMKDgrlAAHGEPQALYDAPADG 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
29-210 |
4.23e-36 |
|
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: 127.68 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLI-----RPQGGEVRIGGVKLERPRPDSALILQDFGLL-----PWR-TVMENIA 97
Cdd:cd03260 23 IPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLELRRRVGMVfqkpnPFPgSIYDNVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 LGLEVRsfygpdGLHapkrpLPEAPDALVDYWLKRLGL-EAVADH-YPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:cd03260 103 YGLRLH------GIK-----LKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSA 171
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 176 LDAPTRESLEELTLKLQAErgLTVITVTHSIEEAA 210
Cdd:cd03260 172 LDPISTAKIEELIAELKKE--YTIVIVTHNMQQAA 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
6-204 |
4.42e-36 |
|
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: 134.51 E-value: 4.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPH-LPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSalILQDF 84
Cdd:COG4987 334 LELEDVSFRYPGAgRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD--LRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 GLLPWR------TVMENIALGlevrsfygpdglhapkrpLPEAPDALV---------DYWLKRL--GLEAVADHYPSQIS 147
Cdd:COG4987 412 AVVPQRphlfdtTLRENLRLA------------------RPDATDEELwaalervglGDWLAALpdGLDTWLGEGGRRLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 148 GGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLeeLTLKLQAERGLTVITVTH 204
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL--LADLLEALAGRTVLLITH 528
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
28-234 |
6.36e-36 |
|
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: 127.55 E-value: 6.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALIL------QDFGLLPWRTVMENIALGLE 101
Cdd:cd03219 22 SVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrtfQIPRLFPELTVLENVMVAAQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 VRSFYGPDGLHAPKRpLPEAPDAlVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:cd03219 102 ARTGSGLLLARARRE-EREARER-AEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEET 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 182 ESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:cd03219 180 EELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVL----DQGRVIAEGTP 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
27-208 |
7.80e-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: 7.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRP-QGGEVRI-----GGVKLERPRP-----DSALILQdfglLPWRTVMEN 95
Cdd:COG1119 24 WTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLfgerrGGEDVWELRKriglvSPALQLR----FPRDETVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 96 IalgleVRS-FYGPDGLHapkRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:COG1119 100 V-----VLSgFFDSIGLY---REPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTA 171
|
170 180 190
....*....|....*....|....*....|....
gi 1490467399 175 SLDAPTRESLEELTLKLQAERGLTVITVTHSIEE 208
Cdd:COG1119 172 GLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE 205
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-216 |
9.13e-36 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 131.31 E-value: 9.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL---------ERPRPDSALILQDFGLLPWRTVMENIALG 99
Cdd:PRK10070 51 IEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakisdaelrEVRRKKIAMVFQSFALMPHMTVLDNTAFG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVRsfygpdGLHAPKRPlPEAPDALvdywlKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:PRK10070 131 MELA------GINAEERR-EKALDAL-----RQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190
....*....|....*....|....*....|....*..
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRI 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-209 |
1.49e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 129.84 E-value: 1.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 1 MENFFVEVKGIDFAWKPHLPL-FLNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG---VKLERPRPD 76
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTVIdNLNL--TIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedvTHRSIQQRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 77 SALILQDFGLLPWRTVMENIALGLEVRsfygpdGLHAPKRP--LPEAPdALVDywlkrlgLEAVADHYPSQISGGQRQRT 154
Cdd:PRK11432 80 ICMVFQSYALFPHMSLGENVGYGLKML------GVPKEERKqrVKEAL-ELVD-------LAGFEDRYVDQISGGQQQRV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 155 AIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEA 209
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEA 200
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
8-219 |
2.51e-35 |
|
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: 124.05 E-value: 2.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFAwkphlplflnfwwhLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS----ALILQD 83
Cdd:cd03230 16 LDDISLT--------------VEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVkrriGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 84 FGLLPWRTVMENIALglevrsfygpdglhapkrplpeapdalvdywlkrlgleavadhypsqiSGGQRQRTAIGRALVLG 163
Cdd:cd03230 82 PSLYENLTVRENLKL------------------------------------------------SGGMKQRLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 164 PDLLLMDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
29-221 |
2.81e-35 |
|
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: 125.21 E-value: 2.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER------P--RPDSALILQDFGLLPWRTVMENIALGL 100
Cdd:cd03292 24 ISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgraiPylRRKIGVVFQDFRLLPDRNVYENVAFAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVrsfygpdgLHAPKRPLPE-APDALvdywlKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:cd03292 104 EV--------TGVPPREIRKrVPAAL-----ELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490467399 180 TRESLEELtLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:cd03292 171 TTWEIMNL-LKKINKAGTTVVVATHAKELVDTTRHRVIALER 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-217 |
2.82e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.05 E-value: 2.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 1 MENFFVEVKGIDFAWKPHLPLFL-NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLE-------R 72
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAATYALkDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeetvwdvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 73 PR-------PDSalilQDFGllpwRTVMENIALGLEVRSFygpdglhaPKRPLPEApdalVDYWLKRLGLEAVADHYPSQ 145
Cdd:PRK13635 81 RQvgmvfqnPDN----QFVG----ATVQDDVAFGLENIGV--------PREEMVER----VDQALRQVGMEDFLNREPHR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 146 ISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKIL 217
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIV 212
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-214 |
3.40e-35 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 124.90 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQ---GGEVRIGGVKLERPRPDS---ALILQDFGLLPWRTVM 93
Cdd:COG4136 15 PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQrriGILFQDDLLFPHLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 94 ENIALGLevrsfygPDGLHAPKRplpeapDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPF 173
Cdd:COG4136 95 ENLAFAL-------PPTIGRAQR------RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1490467399 174 SSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGR 214
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGR 202
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-221 |
3.45e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 128.66 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS---ALILQDFGLLPWRTVMENIALGLEVrs 104
Cdd:PRK10851 24 DIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDrkvGFVFQHYALFRHMTVFDNIAFGLTV-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdgLHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:PRK10851 102 ------LPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKEL 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 1490467399 185 EELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:PRK10851 176 RRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQ 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
23-210 |
2.89e-34 |
|
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: 121.77 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERprpdsalilqdfglLPWRTVMENIALglev 102
Cdd:cd03214 18 LSL--SIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------LSPKELARKIAY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsfygpdglhapkrpLPEApdalvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRE 182
Cdd:cd03214 78 ---------------VPQA--------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180
....*....|....*....|....*...
gi 1490467399 183 SLEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:cd03214 135 ELLELLRRLARERGKTVVMVLHDLNLAA 162
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
29-210 |
6.97e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 121.60 E-value: 6.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG--VKLERPRPDSALILQD-----FGllpwRTVMENIALGLe 101
Cdd:cd03226 23 LYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGkpIKAKERRKSIGYVMQDvdyqlFT----DSVREELLLGL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 vrsfygpdglhapkrPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:cd03226 98 ---------------KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180
....*....|....*....|....*....
gi 1490467399 182 ESLEELTLKLQAErGLTVITVTHSIEEAA 210
Cdd:cd03226 163 ERVGELIRELAAQ-GKAVIVITHDYEFLA 190
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
18-219 |
9.34e-34 |
|
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: 121.51 E-value: 9.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 18 HLPLFLNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS---ALILQDFGLLPWRTVME 94
Cdd:TIGR01277 12 HLPMEFDL--NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQrpvSMLFQENNLFAHLTVRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 95 NIALGLEvrsfygpdglhaPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:TIGR01277 90 NIGLGLH------------PGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 175 SLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:TIGR01277 158 ALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
28-234 |
1.45e-33 |
|
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: 122.56 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLeRPRPDSAL--ILQDFGL--------LPWRTVMENIA 97
Cdd:TIGR04521 27 TIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDI-TAKKKKKLkdLRKKVGLvfqfpehqLFEETVYKDIA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 lglevrsfYGPDGLHAPKRplpEApDALVDYWLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:TIGR04521 106 --------FGPKNLGLSEE---EA-EERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:TIGR04521 174 DPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVM----HKGKIVLDGTP 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
36-219 |
1.83e-33 |
|
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: 124.07 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAL---------ILQDFGLLPWRTVMENIALGLevrsfy 106
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLppekrrigyVFQEARLFPHLSVRGNLRYGM------ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 gpdglhapKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEE 186
Cdd:TIGR02142 101 --------KRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190
....*....|....*....|....*....|...
gi 1490467399 187 LTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
6-216 |
1.83e-33 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 121.27 E-value: 1.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLF-LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSA------ 78
Cdd:COG4161 3 IQLKNINCFYGSHQALFdINL--ECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEkairll 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 -----LILQDFGLLPWRTVMENIalglevrsfygpdgLHAPKRPL---PEAPDALVDYWLKRLGLEAVADHYPSQISGGQ 150
Cdd:COG4161 81 rqkvgMVFQQYNLWPHLTVMENL--------------IEAPCKVLglsKEQAREKAMKLLARLRLTDKADRFPLHLSGGQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 151 RQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTHSIEEAaflgRKI 216
Cdd:COG4161 147 QQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFA----RKV 207
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-204 |
2.00e-33 |
|
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: 126.72 E-value: 2.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 5 FVEVKGIDFAwkphlplflnfwwhLKKGESWAIIGPSGCGKTTLLYLLSGLIrPQGGEVRIGGVKLE-------RP-RPD 76
Cdd:COG4172 299 VKAVDGVSLT--------------LRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDglsrralRPlRRR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 77 SALILQD-FGLL-PWRTVMENIALGLEVrsfygpdglHAPKRPlPEAPDALVDYWLKRLGL-EAVADHYPSQISGGQRQR 153
Cdd:COG4172 364 MQVVFQDpFGSLsPRMTVGQIIAEGLRV---------HGPGLS-AAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQR 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 154 TAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISH 484
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
28-210 |
3.74e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 119.26 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvkLERPrpdsALILQDfGLLPWR---TVMENIALGLevrs 104
Cdd:NF040873 14 TIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG--GARV----AYVPQR-SEVPDSlplTVRDLVAMGR---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fYGPDGlhaPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:NF040873 83 -WARRG---LWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERI 158
|
170 180
....*....|....*....|....*.
gi 1490467399 185 EELtLKLQAERGLTVITVTHSIEEAA 210
Cdd:NF040873 159 IAL-LAEEHARGATVVVVTHDLELVR 183
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
8-217 |
1.79e-32 |
|
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: 120.54 E-value: 1.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQG---GEVRIGGVKL-----ERPRP---- 75
Cdd:COG0444 21 VDGVSF--------------DVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLlklseKELRKirgr 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 76 DSALILQD-FGLL-PWRTVMENIALGLEVRsfygpdgLHAPKRplpEApDALVDYWLKRLGL---EAVADHYPSQISGGQ 150
Cdd:COG0444 87 EIQMIFQDpMTSLnPVMTVGDQIAEPLRIH-------GGLSKA---EA-RERAIELLERVGLpdpERRLDRYPHELSGGM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 151 RQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKIL 217
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
29-204 |
2.39e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 118.70 E-value: 2.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSA-------------LILQDFGLLPWRTVMEN 95
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLSQqkglirqlrqhvgFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 96 IalglevrsFYGPdgLHAPKRPLPEApDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:PRK11264 106 I--------IEGP--VIVKGEPKEEA-TARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSA 174
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 176 LDAptrESLEEL--TLKLQAERGLTVITVTH 204
Cdd:PRK11264 175 LDP---ELVGEVlnTIRQLAQEKRTMVIVTH 202
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
29-216 |
4.10e-32 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 117.61 E-value: 4.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLE----------RPRpDSALILQDFGLLPWRTVMENIAL 98
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssaakaelRNQ-KLGFIYQFHHLLPDFTALENVAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 GLEVrsfygpdGLHAPKRPLPEAPDALvdywlKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:PRK11629 111 PLLI-------GKKKPAEINSRALEML-----AAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDA 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490467399 179 PTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:PRK11629 179 RNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
6-216 |
7.33e-32 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 117.42 E-value: 7.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLF-LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL---ERP-------- 73
Cdd:PRK11124 3 IQLNGINCFYGAHQALFdITL--DCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPsdkairel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 74 RPDSALILQDFGLLPWRTVMENIalglevrsfygpdgLHAPKRPL---PEAPDALVDYWLKRLGLEAVADHYPSQISGGQ 150
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNL--------------IEAPCRVLglsKDQALARAEKLLERLRLKPYADRFPLHLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 151 RQRTAIGRALVLGPDLLLMDEPFSSLD----APTRESLEELtlklqAERGLTVITVTHSIEEAaflgRKI 216
Cdd:PRK11124 147 QQRVAIARALMMEPQVLLFDEPTAALDpeitAQIVSIIREL-----AETGITQVIVTHEVEVA----RKT 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-204 |
1.32e-31 |
|
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: 116.17 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 5 FVEVKGIDFAWKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-----VKLERPRPDSAL 79
Cdd:cd03254 2 EIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFGLLPwRTVMENIALGlevrsfygpdglhapkrpLPEAPDALV---------DYWLKRL--GLEAVADHYPSQISG 148
Cdd:cd03254 82 VLQDTFLFS-GTIMENIRLG------------------RPNATDEEVieaakeagaHDFIMKLpnGYDTVLGENGGNLSQ 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 149 GQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERglTVITVTH 204
Cdd:cd03254 143 GERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR--TSIIIAH 196
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
24-224 |
2.20e-31 |
|
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: 115.29 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 24 NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG----VKLERPRPDSALILQDFGLLPWRTVMENIALg 99
Cdd:cd03263 20 DLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQSLGYCPQFDALFDELTVREHLRF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 levrsfygpdglHAPKRPLPEAP-DALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:cd03263 99 ------------YARLKGLPKSEiKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 179 PTRESLEELTLKLQAERglTVITVTHSIEEAAFLG-R-------KILCLGHPPH 224
Cdd:cd03263 167 ASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCdRiaimsdgKLRCIGSPQE 218
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
30-211 |
4.26e-31 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 115.67 E-value: 4.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV------------------KLERPRPDSALILQDFGLLPWRT 91
Cdd:COG4598 32 RKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgelvpadrrQLQRIRTRLGMVFQSFNLWSHMT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 92 VMENIalgLEvrsfyGPdgLHAPKRPLPEAPDALVDYwLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDE 171
Cdd:COG4598 112 VLENV---IE-----AP--VHVLGRPKAEAIERAEAL-LAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1490467399 172 PFSSLDaPtresleEL---TLKLQ---AERGLTVITVTHsieEAAF 211
Cdd:COG4598 181 PTSALD-P------ELvgeVLKVMrdlAEEGRTMLVVTH---EMGF 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
6-252 |
5.42e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.86 E-value: 5.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKP-HLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP-----RPDSAL 79
Cdd:PRK13632 8 IKVENVSFSYPNsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlkeiRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQD-----FGLlpwrTVMENIALGLEvrsfygpdglhaPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRT 154
Cdd:PRK13632 88 IFQNpdnqfIGA----TVEDDIAFGLE------------NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 155 AIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEaAFLGRKILCLGHpphrEPVVVEGPP 234
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDE-AILADKVIVFSE----GKLIAQGKP 226
|
250 260 270
....*....|....*....|....*....|
gi 1490467399 235 ------------PKRDHPDFYKVCSKLRSI 252
Cdd:PRK13632 227 keilnnkeilekAKIDSPFIYKLSKKLKGI 256
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
31-216 |
5.77e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 118.01 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 31 KGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER----PRPDSaLILQDFGLLPWRTVMENIALGLEvrsfy 106
Cdd:PRK11607 44 KGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppyQRPIN-MMFQSYALFPHMTVEQNIAFGLK----- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 gpdglhapKRPLPEAP-DALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLE 185
Cdd:PRK11607 118 --------QDKLPKAEiASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQ 189
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 186 ELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:PRK11607 190 LEVVDILERVGVTCVMVTHDQEEAMTMAGRI 220
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-210 |
9.93e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 114.55 E-value: 9.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 35 WAIIGPSGCGKTTLLYLLSGLIRPQG-----GEVRIGGVKLERPRPDSALILQDFGLL-------PWRTVMENIALGLEV 102
Cdd:PRK14267 33 FALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPIEVRREVGMVfqypnpfPHLTIYDNVAIGVKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsfygpDGLHAPKRPLPEapdaLVDYWLKRLGL-EAVADH---YPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:PRK14267 113 ------NGLVKSKKELDE----RVEWALKKAALwDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180 190
....*....|....*....|....*....|..
gi 1490467399 179 PTRESLEELTLKLQAErgLTVITVTHSIEEAA 210
Cdd:PRK14267 183 VGTAKIEELLFELKKE--YTIVLVTHSPAQAA 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-234 |
2.41e-30 |
|
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: 112.85 E-value: 2.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 5 FVEVKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP----RPDSALI 80
Cdd:cd03265 13 FEAVRGVSF--------------RVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREprevRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 81 LQDFGLLPWRTVMENIALGLEVrsfYGPDGLHAPKRplpeapdalVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRAL 160
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARL---YGVPGAERRER---------IDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 161 VLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAII----DHGRIIAEGTP 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-209 |
4.33e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 115.33 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG--VKLERPRP-DSALILQDFGLLPWRTVMENIALGLEVRSFygp 108
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVNELEPADrDIAMVFQNYALYPHMSVRENMAYGLKIRGM--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 dglhaPKrplpEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELT 188
Cdd:PRK11650 107 -----PK----AEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEI 177
|
170 180
....*....|....*....|.
gi 1490467399 189 LKLQAERGLTVITVTHSIEEA 209
Cdd:PRK11650 178 QRLHRRLKTTSLYVTHDQVEA 198
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
28-204 |
7.06e-30 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 114.06 E-value: 7.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV--------KLERPRPDSALILQD-FGLL-PWRTVMENIA 97
Cdd:COG4608 40 DIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQditglsgrELRPLRRRMQMVFQDpYASLnPRMTVGDIIA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 LGLEVRsfygpdGLHAPKrplpeAPDALVDYWLKRLGLEA-VADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:COG4608 120 EPLRIH------GLASKA-----ERRERVAELLELVGLRPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180
....*....|....*....|....*...
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:COG4608 189 DVSIQAQVLNLLEDLQDELGLTYLFISH 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
6-205 |
9.95e-30 |
|
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: 116.31 E-value: 9.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDsaLILQDFG 85
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD--EVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 86 LLPWR------TVMENIALGlevrsfygpdglhapkrpLPEAPDALVDYWLKRLGLEAVADHYP-----------SQISG 148
Cdd:TIGR02868 413 VCAQDahlfdtTVRENLRLA------------------RPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSG 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 149 GQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLeeLTLKLQAERGLTVITVTHS 205
Cdd:TIGR02868 475 GERQRLALARALLADAPILLLDEPTEHLDAETADEL--LEDLLAALSGRTVVLITHH 529
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-219 |
1.19e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 114.36 E-value: 1.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS---ALILQDFGLLPWRTVMENIALGLEVRsf 105
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAErgvGMVFQSYALYPHLSVAENMSFGLKLA-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 106 yGPDGLHAPKRplpeapdalVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLE 185
Cdd:PRK11000 104 -GAKKEEINQR---------VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMR 173
|
170 180 190
....*....|....*....|....*....|....
gi 1490467399 186 ELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:PRK11000 174 IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-209 |
1.83e-29 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 109.43 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLE-------RPRPDSALILQDF-GLLPWRTVME 94
Cdd:TIGR01166 11 LNF--AAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrkgllERRQRVGLVFQDPdDQLFAADVDQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 95 NIAlglevrsfYGPDGLHAPkrplPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:TIGR01166 89 DVA--------FGPLNLGLS----EAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 175 SLDAPTRESLEELTLKLQAErGLTVITVTHSIEEA 209
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAE-GMTVVISTHDVDLA 190
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
29-222 |
2.27e-29 |
|
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: 110.33 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQ------DFGLLPWRTVMEnialglev 102
Cdd:TIGR03771 3 ADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGYVPQrhefawDFPISVAHTVMS-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsfyGPDGLHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRE 182
Cdd:TIGR03771 75 ----GRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490467399 183 SLEELTLKLQAErGLTVITVTHSIEEA-------AFLGRKILCLGHP 222
Cdd:TIGR03771 151 LLTELFIELAGA-GTAILMTTHDLAQAmatcdrvVLLNGRVIADGTP 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
28-208 |
2.33e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.12 E-value: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAL------ILQDFGLLPWRTVMENIALGLE 101
Cdd:COG1129 26 ELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQaagiaiIHQELNLVPNLSVAENIFLGRE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 VRSFygpdGLHAPKRPLPEAPDAlvdywLKRLGLE-----AVADhypsqISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:COG1129 106 PRRG----GLIDWRAMRRRAREL-----LARLGLDidpdtPVGD-----LSVAQQQLVEIARALSRDARVLILDEPTASL 171
|
170 180 190
....*....|....*....|....*....|..
gi 1490467399 177 DAPTRESLEELTLKLQAeRGLTVITVTHSIEE 208
Cdd:COG1129 172 TEREVERLFRIIRRLKA-QGVAIIYISHRLDE 202
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
6-210 |
3.00e-29 |
|
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: 115.08 E-value: 3.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----ALI 80
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqiAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 81 LQDFGLLPwRTVMENIALGlevrsfygpdglhapkrpLPEAPDALVDYWLKR-----------LGLEAVADHYPSQISGG 149
Cdd:TIGR02857 402 PQHPFLFA-GTIAENIRLA------------------RPDASDAEIREALERagldefvaalpQGLDTPIGEGGAGLSGG 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 150 QRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQaeRGLTVITVTHSIEEAA 210
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAA 521
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-208 |
3.01e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 112.66 E-value: 3.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAL---------ILQDFGLLPWRTVMENIALGLevrsfy 106
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppekrrigyVFQDARLFPHYKVRGNLRYGM------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 gpdglhAPKRPlpeapdALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP-TRESLE 185
Cdd:PRK11144 102 ------AKSMV------AQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPrKRELLP 169
|
170 180
....*....|....*....|...
gi 1490467399 186 ELTlKLQAERGLTVITVTHSIEE 208
Cdd:PRK11144 170 YLE-RLAREINIPILYVSHSLDE 191
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-207 |
3.02e-28 |
|
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: 105.76 E-value: 3.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 7 EVKGIDFAW---KPhlPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----A 78
Cdd:cd03246 2 EVENVSFRYpgaEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNElgdhvG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQDFGLLPwRTVMENIalglevrsfygpdglhapkrplpeapdalvdywlkrlgleavadhypsqISGGQRQRTAIGR 158
Cdd:cd03246 80 YLPQDDELFS-GSIAENI-------------------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490467399 159 ALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAeRGLTVITVTHSIE 207
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPE 157
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
6-204 |
3.67e-28 |
|
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: 107.24 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAW--KPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVK-----LERPRPDSA 78
Cdd:cd03249 1 IEFKNVSFRYpsRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDirdlnLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQDFGLLPwRTVMENIALGlevrsfygpdglhAPKRPLPEAPDALVDYWLKRL------GLEAVADHYPSQISGGQRQ 152
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYG-------------KPDATDEEVEEAAKKANIHDFimslpdGYDTLVGERGSQLSGGQKQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 153 RTAIGRALVLGPDLLLMDEPFSSLDAptrESLEELTLKL-QAERGLTVITVTH 204
Cdd:cd03249 147 RIAIARALLRNPKILLLDEATSALDA---ESEKLVQEALdRAMKGRTTIVIAH 196
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
5-232 |
6.82e-28 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 106.30 E-value: 6.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 5 FVEVKGIDFAWKPhlplflnfwwhlkkGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERpRPDSAL----I 80
Cdd:cd03266 18 VQAVDGVSFTVKP--------------GEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARrrlgF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 81 LQD-FGLLPWRTVMENIAlglevrsFYGpdGLHAPKRplpEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRA 159
Cdd:cd03266 83 VSDsTGLYDRLTARENLE-------YFA--GLYGLKG---DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 160 LVLGPDLLLMDEPFSSLDAPTRESLEELtLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEG 232
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREF-IRQLRALGKCILFSTHIMQEVERLCDRVVVL----HRGRVVYEG 218
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-204 |
7.44e-28 |
|
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: 106.13 E-value: 7.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL-NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPdsALILQDF 84
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALdNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP--ADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 GLLP------WRTVMENIALGLevrsfygpdglhapkrplPEAPDALVDYWLKRLGLEAVADHYP-----------SQIS 147
Cdd:cd03245 81 GYVPqdvtlfYGTLRDNITLGA------------------PLADDERILRAAELAGVTDFVNKHPngldlqigergRGLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 148 GGQRQRTAIGRALVLGPDLLLMDEPFSSLDaptRESLEELTLKLQAE-RGLTVITVTH 204
Cdd:cd03245 143 GGQRQAVALARALLNDPPILLLDEPTSAMD---MNSEERLKERLRQLlGDKTLIIITH 197
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
32-235 |
5.66e-27 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.04 E-value: 5.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS---------ALILQDFGLLPWRTVMENIalglEV 102
Cdd:PRK10535 34 GEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAlaqlrrehfGFIFQRYHLLSHLTAAQNV----EV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RSFYGpdGLHAPKRPlpEAPDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAptrE 182
Cdd:PRK10535 110 PAVYA--GLERKQRL--LRAQEL----LQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS---H 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 183 SLEEL--TLKLQAERGLTVITVTHSIEEAAFLGRKI------LCLGHPPHREPVVVEGPPP 235
Cdd:PRK10535 179 SGEEVmaILHQLRDRGHTVIIVTHDPQVAAQAERVIeirdgeIVRNPPAQEKVNVAGGTEP 239
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
28-209 |
6.12e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 102.12 E-value: 6.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALilqdfgllpwrtvmenialglevrsfyg 107
Cdd:cd03216 22 SVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDAR---------------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 108 pdglhapkrplpeapdalvdywlkRLGLEAVadhypSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEL 187
Cdd:cd03216 74 ------------------------RAGIAMV-----YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKV 124
|
170 180
....*....|....*....|..
gi 1490467399 188 tLKLQAERGLTVITVTHSIEEA 209
Cdd:cd03216 125 -IRRLRAQGVAVIFISHRLDEV 145
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
28-209 |
7.70e-27 |
|
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: 103.67 E-value: 7.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS------ALILQDFGLLPWRTVMENIALGLE 101
Cdd:cd03224 22 TVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHEraragiGYVPEGRRIFPELTVEENLLLGAY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 VRsfygpdglhaPKRPLPEAPDALVDYW------LKRLGleavadhypSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:cd03224 102 AR----------RRAKRKARLERVYELFprlkerRKQLA---------GTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 176 LdAPT-RESLEELTLKLqAERGLTVITVTHSIEEA 209
Cdd:cd03224 163 L-APKiVEEIFEAIREL-RDEGVTILLVEQNARFA 195
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-234 |
8.23e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 8.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIG------GVK---LERPRPDSALILQdF--GLLPWRTVMENIA 97
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKnkkLKPLRKKVGIVFQ-FpeHQLFEETVEKDIC 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 lglevrsfYGPDGLHAPKrplpEAPDALVDYWLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:PRK13634 109 --------FGPMNFGVSE----EDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVM----HKGTVFLQGTP 230
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
29-221 |
1.32e-26 |
|
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: 103.18 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvklERPRPDSALILQDFGL-------LPWR-TVMENIALgl 100
Cdd:cd03267 44 IEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG---LVPWKRRKKFLRRIGVvfgqktqLWWDlPVIDSFYL-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 eVRSFYGPDGLHAPKRPlpeapDALVDYwlkrLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:cd03267 119 -LAAIYDLPPARFKKRL-----DELSEL----LDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:cd03267 189 QENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDK 229
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
6-223 |
3.79e-26 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 102.92 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAwKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG--------VKLERPRPDS 77
Cdd:PRK11831 8 VDMRGVSFT-RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrSRLYTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 78 ALILQDFGLLPWRTVMENIALGLEVRSFYGPDGLHApkrplpeapdaLVDYWLKRLGLEAVADHYPSQISGGQRQRTAIG 157
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHS-----------TVMMKLEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTH------SIEEAAFL--GRKILCLGHPP 223
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHdvpevlSIADHAYIvaDKKIVAHGSAQ 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-234 |
7.64e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.37 E-value: 7.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV------KLERPRPDSAL 79
Cdd:PRK13644 2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgdfsKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQD-----FGllpwRTVMENIAlglevrsfYGPDGLHAPkrplPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRT 154
Cdd:PRK13644 82 VFQNpetqfVG----RTVEEDLA--------FGPENLCLP----PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 155 AIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQaERGLTVITVTHSIEEAAFLGRKILClghppHREPVVVEGPP 234
Cdd:PRK13644 146 ALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVM-----DRGKIVLEGEP 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
29-216 |
8.38e-26 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 101.01 E-value: 8.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL----ERPRP-----DSALILQDFGLLPWRTVMENIALG 99
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAklrakHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVRSfygpdglhAPKRPLPEAPDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:PRK10584 113 ALLRG--------ESSRQSRNGAKAL----LEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKI 216
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
6-221 |
1.58e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.83 E-value: 1.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPL----FLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVK---------LER 72
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpetgnknLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 73 PRPDSALILQdfglLPWRTVMENIALGlEVRsfYGPDGLHAPKRplpEAPDALVDyWLKRLGL-EAVADHYPSQISGGQR 151
Cdd:PRK13641 83 LRKKVSLVFQ----FPEAQLFENTVLK-DVE--FGPKNFGFSED---EAKEKALK-WLKKVGLsEDLISKSPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 152 QRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAErGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEH 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-210 |
1.68e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.98 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 1 MENFFVEVKGIDFAWKPHLPLFLN-FWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV-----RIGGVKLERPR 74
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKdVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqAITDDNFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 75 PDSALILQD-----FGllpwRTVMENIALGLEVRSFygP-DGLHapkRPLPEApdalvdywLKRLGLEAVADHYPSQISG 148
Cdd:PRK13648 83 KHIGIVFQNpdnqfVG----SIVKYDVAFGLENHAV--PyDEMH---RRVSEA--------LKQVDMLERADYEPNALSG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 149 GQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAM 207
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
28-204 |
2.03e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.92 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP--------RPDSALILQD-FGLL-PWRTVMENIA 97
Cdd:PRK10419 34 SLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkafRRDIQMVFQDsISAVnPRKTVREIIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 lglevrsfygpdglhAPKRPL----PEAPDALVDYWLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEP 172
Cdd:PRK10419 114 ---------------EPLRHLlsldKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190
....*....|....*....|....*....|..
gi 1490467399 173 FSSLDAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQFGTACLFITH 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
29-209 |
2.73e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 99.28 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvklerpRPDSALILQDFGLLPW-------RTVMEN-IALGl 100
Cdd:cd03269 23 VEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG------KPLDIAARNRIGYLPEerglypkMKVIDQlVYLA- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 evrSFYGPDGLHAPKRplpeapdalVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:cd03269 96 ---QLKGLKKEEARRR---------IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180
....*....|....*....|....*....
gi 1490467399 181 RESLEELTLKLqAERGLTVITVTHSIEEA 209
Cdd:cd03269 164 VELLKDVIREL-ARAGKTVILSTHQMELV 191
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
36-210 |
3.25e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 100.11 E-value: 3.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLI--RPQG---GEVRIGGVKLERPRPDSALILQDFGL-------LPWrTVMENIALGLEVR 103
Cdd:COG1117 41 ALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGEDIYDPDVDVVELRRRVGMvfqkpnpFPK-SIYDNVAYGLRLH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 sfygpdGLHaPKRPLpeapDALVDYWLKRLGL-EAVAD---HYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:COG1117 120 ------GIK-SKSEL----DEIVEESLRKAALwDEVKDrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI 188
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 180 TRESLEELTLKLQAErgLTVITVTHSIEEAA 210
Cdd:COG1117 189 STAKIEELILELKKD--YTIVIVTHNMQQAA 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
28-234 |
3.92e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.85 E-value: 3.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-PRPDSALIL----QDFGL-LPWrTVMENIALGLe 101
Cdd:PRK13548 24 TLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRavlpQHSSLsFPF-TVEEVVAMGR- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 vrsfygpdglhAPKRPLPEAPDALVDYWLKRLGLEAVAD-HYPsQISGGQRQRTAIGRALV------LGPDLLLMDEPFS 174
Cdd:PRK13548 102 -----------APHGLSRAEDDALVAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 175 SLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:PRK13548 170 ALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLL----HQGRLVADGTP 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
20-204 |
5.27e-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: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRI-GGVKLerprpdsALILQDFGLLPWRTVMENIAL 98
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLRI-------GYLPQEPPLDDDLTVLDTVLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 GLEVR--------------SFYGPDGLHAPKrpLPEAPDALvDYW---------LKRLGLEAvADHY--PSQISGGQRQR 153
Cdd:COG0488 85 GDAELraleaeleeleaklAEPDEDLERLAE--LQEEFEAL-GGWeaearaeeiLSGLGFPE-EDLDrpVSELSGGWRRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 154 TAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELtlkLQAERGlTVITVTH 204
Cdd:COG0488 161 VALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LKNYPG-TVLVVSH 207
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
28-205 |
5.45e-25 |
|
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: 98.01 E-value: 5.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQG--GEVRIGG--VKLERPRPDSALILQDFGLLPWRTVMENIALGLEVR 103
Cdd:cd03213 31 KAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGrpLDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 SfygpdglhapkrplpeapdalvdywlkrlgleavadhypsqISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRES 183
Cdd:cd03213 111 G-----------------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180
....*....|....*....|..
gi 1490467399 184 LEElTLKLQAERGLTVITVTHS 205
Cdd:cd03213 150 VMS-LLRRLADTGRTIICSIHQ 170
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-204 |
6.61e-25 |
|
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: 98.50 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQG---GEVRIGGVKLERP--RPDSALILQDFGLLPWRTVMENIAlglev 102
Cdd:cd03234 29 HVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDqfQKCVAYVRQDDILLPGLTVRETLT----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsFYGPDGLHAPKR---PLPEAPDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:cd03234 104 --YTAILRLPRKSSdaiRKKRVEDVL----LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSF 177
|
170 180
....*....|....*....|....*
gi 1490467399 180 TRESLEElTLKLQAERGLTVITVTH 204
Cdd:cd03234 178 TALNLVS-TLSQLARRNRIVILTIH 201
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
27-220 |
7.11e-25 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.41 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER------P--RPDSALILQDFGLLPWRTVMENIAL 98
Cdd:PRK10908 23 FHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrevPflRRQIGMIFQDHHLLMDRTVYDNVAI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 GLEVRSFYGPDglhaPKRPLPEApdalvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDa 178
Cdd:PRK10908 103 PLIIAGASGDD----IRRRVSAA--------LDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD- 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 179 ptrESLEELTLKLQAE---RGLTVITVTHSIEEAAFLGRKILCLG 220
Cdd:PRK10908 170 ---DALSEGILRLFEEfnrVGVTVLMATHDIGLISRRSYRMLTLS 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
6-209 |
8.34e-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: 98.46 E-value: 8.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL-NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-----VKLERPRPDSAL 79
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLrDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFGLLPwRTVMENIALGL------EVRSFYGPDGLHAPKRPLPEapdalvdywlkrlGLEAVADHYPSQISGGQRQR 153
Cdd:cd03251 81 VSQDVFLFN-DTVAENIAYGRpgatreEVEEAARAANAHEFIMELPE-------------GYDTVIGERGVKLSGGQRQR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1490467399 154 TAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERglTVITVTH---SIEEA 209
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHrlsTIENA 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
29-252 |
1.95e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.58 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-------VKLERPRPDSALILQ--DFGLLPwRTVMENIAlg 99
Cdd:PRK13637 30 IEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkVKLSDIRKKVGLVFQypEYQLFE-ETIEKDIA-- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 levrsfYGPDGLHAPKRPLPEApdalVDYWLKRLGL--EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:PRK13637 107 ------FGPINLGLSEEEIENR----VKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 178 APTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPPpkrdhPDFYKVCSKLRSI 252
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVM----NKGKCELQGTP-----REVFKEVETLESI 242
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-207 |
2.35e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 101.42 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGE--VRIGG--VKLERPRPDS--------ALILQDFGLLPWRTVMENI 96
Cdd:TIGR03269 307 VKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDewVDMTKPGPDGrgrakryiGILHQEYDLYPHRTVLDNL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 --ALGLEVrsfygPDGLhAPKRPLpeapdalvdYWLKRLGL-----EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLM 169
Cdd:TIGR03269 387 teAIGLEL-----PDEL-ARMKAV---------ITLKMVGFdeekaEEILDKYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490467399 170 DEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIE 207
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMD 489
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
35-219 |
2.38e-24 |
|
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: 96.49 E-value: 2.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 35 WAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVK-LERPRPDSALI---LQDFGLLPWRTVMENIalglevrsfygpDG 110
Cdd:cd03264 28 YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDvLKQPQKLRRRIgylPQEFGVYPNFTVREFL------------DY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 111 LHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLK 190
Cdd:cd03264 96 IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSE 175
|
170 180
....*....|....*....|....*....
gi 1490467399 191 LQAERglTVITVTHSIEEAAFLGRKILCL 219
Cdd:cd03264 176 LGEDR--IVILSTHIVEDVESLCNQVAVL 202
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
28-204 |
3.29e-24 |
|
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: 101.10 E-value: 3.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPrpDSALILQDFGLLP------WRTVMENIALGLe 101
Cdd:TIGR03375 487 TIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI--DPADLRRNIGYVPqdprlfYGTLRDNIALGA- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 vrsfygpdglhapkrplPEAPDALVDYWLKRLGLEAVADHYPS----QI-------SGGQRQRTAIGRALVLGPDLLLMD 170
Cdd:TIGR03375 564 -----------------PYADDEEILRAAELAGVTEFVRRHPDgldmQIgergrslSGGQRQAVALARALLRDPPILLLD 626
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 171 EPFSSLDAPTRESLEEltlKLQAE-RGLTVITVTH 204
Cdd:TIGR03375 627 EPTSAMDNRSEERFKD---RLKRWlAGKTLVLVTH 658
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
28-208 |
3.82e-24 |
|
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: 96.46 E-value: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL------ERPR------PDSALILQDFgllpwrTVMEN 95
Cdd:cd03218 22 SVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItklpmhKRARlgigylPQEASIFRKL------TVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 96 IALGLEVRSFygpdglhaPKRPLPEAPDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:cd03218 96 ILAVLEIRGL--------SKKEREEKLEEL----LEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190
....*....|....*....|....*....|...
gi 1490467399 176 LDAPTRESLEELTLKLqAERGLTVITVTHSIEE 208
Cdd:cd03218 164 VDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRE 195
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
8-204 |
4.12e-24 |
|
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: 100.59 E-value: 4.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFAwkphlplflnfwwhLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS--ALI--L-Q 82
Cdd:COG4618 348 LRGVSFS--------------LEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREElgRHIgyLpQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 83 DFGLLPwRTVMENIAlglevRsfygpdglhapkrpLPEAPDALVdywlkrlgLEA--VAD-H---------YPSQI---- 146
Cdd:COG4618 414 DVELFD-GTIAENIA-----R--------------FGDADPEKV--------VAAakLAGvHemilrlpdgYDTRIgegg 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 147 ---SGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEElTLKLQAERGLTVITVTH 204
Cdd:COG4618 466 arlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA-AIRALKARGATVVVITH 525
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
5-204 |
4.98e-24 |
|
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: 100.79 E-value: 4.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 5 FVEVKGIDFAWKP-HLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-PRPDS----A 78
Cdd:TIGR03796 477 YVELRNITFGYSPlEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEiPREVLansvA 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQDFGLLPwRTVMENIALGlevrsfygpDGLHAPKRPLPEAPDALV-DYWLKRLG-LEAVADHYPSQISGGQRQRTAI 156
Cdd:TIGR03796 557 MVDQDIFLFE-GTVRDNLTLW---------DPTIPDADLVRACKDAAIhDVITSRPGgYDAELAEGGANLSGGQRQRLEI 626
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490467399 157 GRALVLGPDLLLMDEPFSSLDAPTRESLEElTLKlqaERGLTVITVTH 204
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDPETEKIIDD-NLR---RRGCTCIIVAH 670
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
28-202 |
5.86e-24 |
|
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: 96.20 E-value: 5.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS------ALILQD---FGLLpwrTVMENIAL 98
Cdd:COG0410 25 EVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRiarlgiGYVPEGrriFPSL---TVEENLLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 GLEVRSfygpdglhaPKRPLPEAPDALVDY--WLK-RLGLEAvadhypSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:COG0410 102 GAYARR---------DRAEVRADLERVYELfpRLKeRRRQRA------GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
170 180 190
....*....|....*....|....*....|..
gi 1490467399 176 LdAP-----TRESLEELtlklqAERGLTVITV 202
Cdd:COG0410 167 L-APliveeIFEIIRRL-----NREGVTILLV 192
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
23-208 |
8.18e-24 |
|
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: 94.98 E-value: 8.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG---VKLERPRPDSALILQDFGLLPWRTVMENIALg 99
Cdd:cd03268 19 ISL--HVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGksyQKNIEALRRIGALIEAPGFYPNLTARENLRL- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 levrsfygpdglhapKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:cd03268 96 ---------------LARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160
|
170 180
....*....|....*....|....*....
gi 1490467399 180 TRESLEELTLKLQAErGLTVITVTHSIEE 208
Cdd:cd03268 161 GIKELRELILSLRDQ-GITVLISSHLLSE 188
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-214 |
1.06e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 96.72 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 1 MENFfVEVKGIDFAWKPHL--PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP----- 73
Cdd:PRK13650 1 MSNI-IEVKNLTFKYKEDQekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnvwdi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 74 RPDSALILQD-----FGllpwRTVMENIALGLEVRsfygpdGLhapkrPLPEAPDAlVDYWLKRLGLEAVADHYPSQISG 148
Cdd:PRK13650 80 RHKIGMVFQNpdnqfVG----ATVEDDVAFGLENK------GI-----PHEEMKER-VNEALELVGMQDFKEREPARLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 149 GQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGR 214
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDR 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-210 |
1.43e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.41 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 1 MENFFVEVKGIDFAWK-PHLPLFLNFWWHLKKGeSW-AIIGPSGCGKTTLLYLLSGLIRPQGGE---VRIGGVKLE---- 71
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPdSKKPALNDISFSIPRG-SWtALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTaktv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 72 ---RPR-------PDSALIlqdfgllpWRTVMENIALGLEVRSFygpdglhapkrPLPEApDALVDYWLKRLGLEAVADH 141
Cdd:PRK13640 80 wdiREKvgivfqnPDNQFV--------GATVGDDVAFGLENRAV-----------PRPEM-IKIVRDVLADVGMLDYIDS 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490467399 142 YPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:PRK13640 140 EPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN 208
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
30-234 |
1.79e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.42 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG--VKLERP----------------RPDSALILQDFGLLPWRT 91
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtINLVRDkdgqlkvadknqlrllRTRLTMVFQHFNLWSHMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 92 VMENIalglevrsfygpdgLHAPKRPL----PEAPDALVDYwLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDL 166
Cdd:PRK10619 109 VLENV--------------MEAPIQVLglskQEARERAVKY-LAKVGIdERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 167 LLMDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFL----HQGKIEEEGAP 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
28-204 |
1.84e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 96.70 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV--------RIGGVKLERPRPDSALILQD--FGLLPWRTVMENIA 97
Cdd:PRK15079 43 RLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVawlgkdllGMKDDEWRAVRSDIQMIFQDplASLNPRMTIGEIIA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 LGLevRSFYgpdglhaPKRPLPEAPDAlVDYWLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:PRK15079 123 EPL--RTYH-------PKLSRQEVKDR-VKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180
....*....|....*....|....*...
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAH 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
6-204 |
2.61e-23 |
|
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: 94.60 E-value: 2.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-----VKLERPRPDSALI 80
Cdd:cd03253 1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdireVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 81 LQDFGLLPwRTVMENIALG------LEVRSFYGPDGLHAPKRPLPEAPDALVDywlKRlGLeavadhypsQISGGQRQRT 154
Cdd:cd03253 81 PQDTVLFN-DTIGYNIRYGrpdatdEEVIEAAKAAQIHDKIMRFPDGYDTIVG---ER-GL---------KLSGGEKQRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1490467399 155 AIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERglTVITVTH 204
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAH 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
6-204 |
2.68e-23 |
|
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: 94.48 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL-NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL-----ERPRPDSAL 79
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILdNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaladpAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFGLLPwRTVMENIALGLEvrsfyGPD-----------GLHAPKRPLPEAPDALVdywlkrlGLEAVAdhypsqISG 148
Cdd:cd03252 81 VLQENVLFN-RSIRDNIALADP-----GMSmervieaaklaGAHDFISELPEGYDTIV-------GEQGAG------LSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 149 GQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERglTVITVTH 204
Cdd:cd03252 142 GQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAH 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
19-204 |
1.30e-22 |
|
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: 91.65 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 19 LPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPD----SALILQDFGLLPWRTVME 94
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphenILYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 95 NIalglevrSFYGPDglHAPKRPLPEapDAlvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:TIGR01189 93 NL-------HFWAAI--HGGAQRTIE--DA-----LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 175 SLDAPTRESLEELtLKLQAERGLTVITVTH 204
Cdd:TIGR01189 157 ALDKAGVALLAGL-LRAHLARGGIVLLTTH 185
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
30-187 |
1.31e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.57 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-----VKLERPRPDSALILQDFGLLPwRTVMENIALGlevrs 104
Cdd:PRK13657 359 KPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtVTRASLRRNIAVVFQDAGLFN-RSIEDNIRVG----- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fyGPDGLHAPKRPLPEAPDALvDYWLKR-LGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT--- 180
Cdd:PRK13657 433 --RPDATDEEMRAAAERAQAH-DFIERKpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETeak 509
|
....*...
gi 1490467399 181 -RESLEEL 187
Cdd:PRK13657 510 vKAALDEL 517
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-207 |
1.45e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.31 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGK-TTLLYLLSgLIRPQGgEVRIGGVKLERPRPDSAL--------ILQD--FGLLPWRTVMENIA 97
Cdd:PRK15134 309 LRPGETLGLVGESGSGKsTTGLALLR-LINSQG-EIWFDGQPLHNLNRRQLLpvrhriqvVFQDpnSSLNPRLNVLQIIE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 LGLEVrsfygpdglHAPKRPlPEAPDALVDYWLKRLGLEAVADH-YPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:PRK15134 387 EGLRV---------HQPTLS-AAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTHSIE 207
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKHQLAYLFISHDLH 487
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-204 |
1.66e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWkPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIG-GVKLerprpdsALILQDF 84
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGeTVKI-------GYFDQHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 GLL-PWRTVMENIALG------LEVRSFYG-----PDGLHAPKRPLpeapdalvdywlkrlgleavadhypsqiSGGQRQ 152
Cdd:COG0488 388 EELdPDKTVLDELRDGapggteQEVRGYLGrflfsGDDAFKPVGVL----------------------------SGGEKA 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 153 RTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELtlkLQAERGlTVITVTH 204
Cdd:COG0488 440 RLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA---LDDFPG-TVLLVSH 487
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
29-209 |
1.84e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALIL------QDFGLLPWRTVMENIALGLEv 102
Cdd:COG3845 28 VRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgigmvhQHFMLVPNLTVAENIVLGLE- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsfygpdGLHAPKRPLPEAPDALVDYwLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLdapTRE 182
Cdd:COG3845 107 -------PTKGGRLDRKAARARIREL-SERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL---TPQ 175
|
170 180
....*....|....*....|....*....
gi 1490467399 183 SLEEL--TLKLQAERGLTVITVTHSIEEA 209
Cdd:COG3845 176 EADELfeILRRLAAEGKSIIFITHKLREV 204
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
28-201 |
2.65e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.01 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL------ERPRpdsalilqdFGL--LP-----WR--TV 92
Cdd:COG1137 25 EVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhKRAR---------LGIgyLPqeasiFRklTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 93 MENIALGLEVRsfyGPDglhapkrplPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEP 172
Cdd:COG1137 96 EDNILAVLELR---KLS---------KKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 173 FSSLDAPTRESLEELTLKLqAERGLTV-IT 201
Cdd:COG1137 164 FAGVDPIAVADIQKIIRHL-KERGIGVlIT 192
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
23-208 |
2.86e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 95.30 E-value: 2.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIrPQGGEVRIGGVKLERPRPDS-----ALILQDfGLLPWRTVMENIA 97
Cdd:PRK11174 369 LNF--TLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESwrkhlSWVGQN-PQLPHGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 98 LGLevrsfygpdglhapkrplPEAPDALVDYWLKR-----------LGLE-AVADHyPSQISGGQRQRTAIGRALVLGPD 165
Cdd:PRK11174 445 LGN------------------PDASDEQLQQALENawvseflpllpQGLDtPIGDQ-AAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 166 LLLMDEPFSSLDAPTreslEELTLK--LQAERGLTVITVTHSIEE 208
Cdd:PRK11174 506 LLLLDEPTASLDAHS----EQLVMQalNAASRRQTTLMVTHQLED 546
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
24-210 |
4.54e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.77 E-value: 4.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 24 NFWWHLKKGESWAIIGPSGCGKTTLLYL---LSGLI---RPQGgEVRIGGVKLERPRPDSALILQDFGLL-----PW-RT 91
Cdd:PRK14243 28 NVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIpgfRVEG-KVTFHGKNLYAPDVDPVEVRRRIGMVfqkpnPFpKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 92 VMENIALGLEVRSFYGPdglhapkrplpeaPDALVDYWLKRLGL-EAVADHYP---SQISGGQRQRTAIGRALVLGPDLL 167
Cdd:PRK14243 107 IYDNIAYGARINGYKGD-------------MDELVERSLRQAALwDEVKDKLKqsgLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490467399 168 LMDEPFSSLDAPTRESLEELTLKLQaeRGLTVITVTHSIEEAA 210
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELK--EQYTIIIVTHNMQQAA 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
30-209 |
5.78e-22 |
|
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: 90.66 E-value: 5.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS------ALILQDFGLLPWRTVMENIALGLEVR 103
Cdd:TIGR03410 24 PKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHEraragiAYVPQGREIFPRLTVEENLLTGLAAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 SfygpdglhAPKRPLP-EAPD---ALVDYwLKRLGleavadhypSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:TIGR03410 104 P--------RRSRKIPdEIYElfpVLKEM-LGRRG---------GDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIEEA 209
Cdd:TIGR03410 166 IIKDIGRVIRRLRAEGGMAILLVEQYLDFA 195
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-205 |
7.25e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 7.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSA---LILQDfGLLPWRTVMENI 96
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchyLGHRN-AMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALGlevRSFYGPDGLHApkrplPEApdalvdywLKRLGLEAVAdHYPSQ-ISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:PRK13539 95 EFW---AAFLGGEELDI-----AAA--------LEAVGLAPLA-HLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 176 LDAPTRESLEELtLKLQAERGLTVITVTHS 205
Cdd:PRK13539 158 LDAAAVALFAEL-IRAHLAQGGIVIAATHI 186
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
28-210 |
8.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.76 E-value: 8.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAL--ILQDFGLL---PWRTVMENialGLEV 102
Cdd:PRK13646 29 EFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrpVRKRIGMVfqfPESQLFED---TVER 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RSFYGPDGLhapKRPLPEAPDALVDYwLKRLGLEA-VADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:PRK13646 106 EIIFGPKNF---KMNLDEVKNYAHRL-LMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSK 181
|
170 180
....*....|....*....|....*....
gi 1490467399 182 ESLEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:PRK13646 182 RQVMRLLKSLQTDENKTIILVSHDMNEVA 210
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
6-204 |
8.33e-22 |
|
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: 94.04 E-value: 8.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL-NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----AL 79
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLsNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWlrrqmGV 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDfGLLPWRTVMENIALGLevrsfygpdglhapkrplPEAPDALVDYWLKRLG----LEAVADHYPSQI-------SG 148
Cdd:TIGR01846 536 VLQE-NVLFSRSIRDNIALCN------------------PGAPFEHVIHAAKLAGahdfISELPQGYNTEVgekganlSG 596
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 149 GQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQaeRGLTVITVTH 204
Cdd:TIGR01846 597 GQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREIC--RGRTVIIIAH 650
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
29-234 |
1.02e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 91.30 E-value: 1.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP------RPDSALILQ--DFGLLPwRTVMENIAlgl 100
Cdd:PRK13633 33 VKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEenlwdiRNKAGMVFQnpDNQIVA-TIVEEDVA--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 evrsfYGPDGLHAPkrplPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:PRK13633 109 -----FGPENLGIP----PEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILClghppHREPVVVEGPP 234
Cdd:PRK13633 180 RREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVM-----DSGKVVMEGTP 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
6-201 |
1.10e-21 |
|
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: 89.84 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAW--KPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvkleRPRPDS------ 77
Cdd:cd03248 12 VKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG----KPISQYehkylh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 78 ---ALILQDFGLLPwRTVMENIALGLEVRSF----YGPDGLHAPKRpLPEAPDalvdywlkrlGLEAVADHYPSQISGGQ 150
Cdd:cd03248 88 skvSLVGQEPVLFA-RSLQDNIAYGLQSCSFecvkEAAQKAHAHSF-ISELAS----------GYDTEVGEKGSQLSGGQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 151 RQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVIT 201
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA 206
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
29-221 |
1.13e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.84 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLI---RPQGGEVRIGGVKLER----------PRPDSALILQDFGLLPWRTVMEN 95
Cdd:PRK09984 27 IHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlardirkSRANTGYIFQQFNLVNRLSVLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 96 IALG-LEVRSFYGPDGLHAPKRPLPEAPDALVdywlkRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:PRK09984 107 VLIGaLGSTPFWRTCFSWFTREQKQRALQALT-----RVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490467399 175 SLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL--GH 221
Cdd:PRK09984 182 SLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALrqGH 230
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
6-221 |
1.61e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAW--KPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-----PRPDSA 78
Cdd:TIGR00958 479 IEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQydhhyLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQDfGLLPWRTVMENIALGL------EVRSFYGPDGLHAPKRPLPEapdalvdywlkrlGLEAVADHYPSQISGGQRQ 152
Cdd:TIGR00958 559 LVGQE-PVLFSGSVRENIAYGLtdtpdeEIMAAAKAANAHDFIMEFPN-------------GYDTEVGEKGSQLSGGQKQ 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 153 RTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEltLKLQAERglTVITVTH--SIEEAAflgRKILCLGH 221
Cdd:TIGR00958 625 RIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASR--TVLLIAHrlSTVERA---DQILVLKK 688
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
29-244 |
1.68e-21 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.05 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERpRPDSAL-------ILQDFGLLPWRTVMENIALG-- 99
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-LPGHQIarmgvvrTFQHVRLFREMTVIENLLVAqh 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 --LEVRSFYGPDGLHAPKRPLPEAPDALVdYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:PRK11300 107 qqLKTGLFSGLLKTPAFRRAESEALDRAA-TWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLN 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 178 APTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLGHPphrEPVVVEGPPPKRDHPDFYK 244
Cdd:PRK11300 186 PKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG---TPLANGTPEEIRNNPDVIK 249
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
29-204 |
3.31e-21 |
|
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: 87.93 E-value: 3.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGLLP----WRTVMENIalglevrS 104
Cdd:cd03231 23 LAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPgiktTLSVLENL-------R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 FYGPDGlhapkrplpeaPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:cd03231 96 FWHADH-----------SDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 1490467399 185 EELtLKLQAERGLTVITVTH 204
Cdd:cd03231 165 AEA-MAGHCARGGMVVLTTH 183
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-204 |
3.43e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 90.41 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP--------RPDSALILQD-FGLL-PWRTVMENIAL 98
Cdd:PRK11308 38 LERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAdpeaqkllRQKIQIVFQNpYGSLnPRKKVGQILEE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 GLEVRSfygpdGLHAPKRplpeapDALVDYWLKRLGLEAV-ADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:PRK11308 118 PLLINT-----SLSAAER------REKALAMMAKVGLRPEhYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180
....*....|....*....|....*..
gi 1490467399 178 APTRESLEELTLKLQAERGLTVITVTH 204
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISH 213
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
27-234 |
5.39e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.79 E-value: 5.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRiggvkleRPRPDSALilqdfgLLPWRTvmenialglevrsfY 106
Cdd:COG4178 384 LSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA-------RPAGARVL------FLPQRP--------------Y 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 GPDG-----LHAPKRPlPEAPDALVDYWLKRLGLEAVADHYP-----SQI-SGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:COG4178 437 LPLGtlreaLLYPATA-EAFSDAELREALEAVGLGHLAERLDeeadwDQVlSLGEQQRLAFARLLLHKPDWLFLDEATSA 515
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 176 LDAPTRESLEELtlkLQAE-RGLTVITVTHSIEEAAFLGRKiLCLGHPPHREPVVVEGPP 234
Cdd:COG4178 516 LDEENEAALYQL---LREElPGTTVISVGHRSTLAAFHDRV-LELTGDGSWQLLPAEAPA 571
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
29-204 |
6.76e-21 |
|
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: 91.26 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----ALILQDFGLLPwRTVMENIAlglevR 103
Cdd:TIGR01842 341 LQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETfgkhiGYLPQDVELFP-GTVAENIA-----R 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 SFYGPDglhaPKRPLPEAPDALVDYWLKRL--GLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:TIGR01842 415 FGENAD----PEKIIEAAKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGE 490
|
170 180
....*....|....*....|...
gi 1490467399 182 ESLEELTLKLQAeRGLTVITVTH 204
Cdd:TIGR01842 491 QALANAIKALKA-RGITVVVITH 512
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
6-195 |
7.38e-21 |
|
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: 91.56 E-value: 7.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL-NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV-----RIGGVKLERPRPDSAL 79
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLILdDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVfydgqDLAGLDVQAVRRQLGV 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFGLLPwRTVMENIALGlevrSFYGPD---------GLHAPKRPLPeapdalvdywlkrLGLEAVADHYPSQISGGQ 150
Cdd:TIGR03797 532 VLQNGRLMS-GSIFENIAGG----APLTLDeaweaarmaGLAEDIRAMP-------------MGMHTVISEGGGTLSGGQ 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 151 RQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAER 195
Cdd:TIGR03797 594 RQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR 638
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
29-207 |
1.01e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGL--------LPWRTVMENIAlgl 100
Cdd:PRK13636 29 IKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVGMvfqdpdnqLFSASVYQDVS--- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 evrsfYGPDGLHAPKRPLPEApdalVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:PRK13636 106 -----FGAVNLKLPEDEVRKR----VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180
....*....|....*....|....*..
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTHSIE 207
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDID 203
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
30-208 |
1.52e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 88.24 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvklerpRPDSALILQDFGLLP-WR------TVMENIA-LGlE 101
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG------EPLDPEDRRRIGYLPeERglypkmKVGEQLVyLA-R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 VRsfygpdGLhapkrPLPEAPDALvDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:COG4152 98 LK------GL-----SKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNV 165
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 182 ESLEELTLKLqAERGLTVITVTH---SIEE 208
Cdd:COG4152 166 ELLKDVIREL-AAKGTTVIFSSHqmeLVEE 194
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
29-219 |
1.78e-20 |
|
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: 87.19 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRI---GGVKLE---RPRPDSALILQDfgllPWRTVMENIALGLEV 102
Cdd:TIGR02323 26 LYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELElyqLSEAERRRLMRT----EWGFVHQNPRDGLRM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RSfygPDGLHAPKRPLPEAPD------ALVDYWLKRLGLEAV-ADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:TIGR02323 102 RV---SAGANIGERLMAIGARhygnirATAQDWLEEVEIDPTrIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGG 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1490467399 176 LDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:TIGR02323 179 LDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
32-204 |
1.82e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 90.30 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG--------VKLERPRPDSALILQD--FGLLPWRTVMENIALGLE 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqridtlspGKLQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 VRSFYgpDGLHAPKRplpeapdalVDYWLKRLGLEAV-ADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:PRK10261 430 VHGLL--PGKAAAAR---------VAWLLERVGLLPEhAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180
....*....|....*....|....
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTH 204
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISH 522
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
29-206 |
2.13e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.54 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLErprpdsalilqdFGLLPWRT-----VMENIALGLEVR 103
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLH------------FGDYSYRSqrirmIFQDPSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 SFYGpDGLHAPKR----PLPEAPDALVDYWLKRLGLeaVADH---YPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:PRK15112 104 QRIS-QILDFPLRlntdLEPEQREKQIIETLRQVGL--LPDHasyYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 177 DAPTRESLEELTLKLQAERGLTVITVTHSI 206
Cdd:PRK15112 181 DMSMRSQLINLMLELQEKQGISYIYVTQHL 210
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
28-210 |
2.80e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 2.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-PRPDSALIL----QDfgllpwrtvmENIALGLEV 102
Cdd:COG4604 23 TIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLailrQE----------NHINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 R---SFyG--PdglHAPKRPLPEapD-ALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIgrALVL--GPDLLLMDEPFS 174
Cdd:COG4604 93 RelvAF-GrfP---YSKGRLTAE--DrEIIDEAIAYLDLEDLADRYLDELSGGQRQRAFI--AMVLaqDTDYVLLDEPLN 164
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490467399 175 SLDapTRESLEELTL--KLQAERGLTVITVTHSIEEAA 210
Cdd:COG4604 165 NLD--MKHSVQMMKLlrRLADELGKTVVIVLHDINFAS 200
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
20-204 |
2.95e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 85.63 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLF--LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDsalILQDF-------GLLPWR 90
Cdd:PRK13538 15 ILFsgLSF--TLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---YHQDLlylghqpGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 91 TVMENIAlglevrsFYGPdgLHAPKRplpeaPDALVDYwLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMD 170
Cdd:PRK13538 90 TALENLR-------FYQR--LHGPGD-----DEALWEA-LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170 180 190
....*....|....*....|....*....|....
gi 1490467399 171 EPFSSLDAPTRESLEELtLKLQAERGLTVITVTH 204
Cdd:PRK13538 155 EPFTAIDKQGVARLEAL-LAQHAEQGGMVILTTH 187
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-233 |
3.77e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 86.51 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIR--PQG---GEVRIGG-----VKLERPRPDSALILQDFGLLPWRTVMENIALGLEVrsf 105
Cdd:PRK14247 33 ALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGqdifkMDVIELRRRVQMVFQIPNPIPNLSIFENVALGLKL--- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 106 ygpDGLHAPKRPLPEApdalVDYWLKRLGL-EAVADHYPS---QISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:PRK14247 110 ---NRLVKSKKELQER----VRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 182 ESLEELTLKLQAErgLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGP 233
Cdd:PRK14247 183 AKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFL----YKGQIVEWGP 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
29-209 |
4.42e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.22 E-value: 4.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSalILQDFGLLPWR-------TVMENIALGle 101
Cdd:PRK11231 25 LPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQ--LARRLALLPQHhltpegiTVRELVAYG-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 vRSFYgpdgLHAPKRpLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIgrALVLGPD--LLLMDEPFSSLDAP 179
Cdd:PRK11231 101 -RSPW----LSLWGR-LSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFL--AMVLAQDtpVVLLDEPTTYLDIN 172
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 180 TRESLEELTLKLQAErGLTVITVTHSIEEA 209
Cdd:PRK11231 173 HQVELMRLMRELNTQ-GKTVVTVLHDLNQA 201
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
29-208 |
5.44e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 85.54 E-value: 5.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-----VKLERPRPDSALILQD---FGllpwRTVMENIALGL 100
Cdd:PRK10247 30 LRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistLKPEIYRQQVSYCAQTptlFG----DTVYDNLIFPW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSfygpdglhapKRPlpeAPDALVDYwLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:PRK10247 106 QIRN----------QQP---DPAIFLDD-LERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
|
170 180
....*....|....*....|....*....
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIEE 208
Cdd:PRK10247 172 NKHNVNEIIHRYVREQNIAVLWVTHDKDE 200
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
28-216 |
6.13e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.78 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG----VKLERPRPDSALILQDFGLLPWRTVMENiaLGLEVR 103
Cdd:PRK13537 29 HVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVVPQFDNLDPDFTVREN--LLVFGR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 SFygpdGLHApkrplpEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRES 183
Cdd:PRK13537 107 YF----GLSA------AAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1490467399 184 LEELTLKLQAeRGLTVITVTHSIEEAAFL---------GRKI 216
Cdd:PRK13537 177 MWERLRSLLA-RGKTILLTTHFMEEAERLcdrlcvieeGRKI 217
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-208 |
7.30e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 85.86 E-value: 7.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGgEVRIGG-------------VKLERPRPDSALILQDFGLLPwRTVMENIALGLEV 102
Cdd:PRK14258 37 AIIGPSGCGKSTFLKCLNRMNELES-EVRVEGrveffnqniyerrVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RSFYgpdglhaPKRPLpeapDALVDYWLKRLGLEAVADH--YPS--QISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:PRK14258 115 VGWR-------PKLEI----DDIVESALKDADLWDEIKHkiHKSalDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDP 183
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 179 PTRESLEELTLKLQAERGLTVITVTHSIEE 208
Cdd:PRK14258 184 IASMKVESLIQSLRLRSELTMVIVSHNLHQ 213
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
28-209 |
1.14e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 85.14 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERpRPD---SALI---LQD--FGLLPWRTVMENIALG 99
Cdd:COG1101 28 TIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LPEykrAKYIgrvFQDpmMGTAPSMTIEENLALA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 L---EVRSFyGPdGLHAPKRplpeapDALVDYwLKRL--GLEavaDHYPSQI---SGGQRQRTAIGRALVLGPDLLLMDE 171
Cdd:COG1101 107 YrrgKRRGL-RR-GLTKKRR------ELFREL-LATLglGLE---NRLDTKVgllSGGQRQALSLLMATLTKPKLLLLDE 174
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490467399 172 PFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEA 209
Cdd:COG1101 175 HTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQA 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-204 |
1.19e-19 |
|
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: 83.52 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL-NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLerprpdsaLILQDf 84
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLkNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--------SDLEK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 gllpwrTVMENIALglevrsfygpdglhapkrpLPEAPDALVDYWLKRLGLeavadhypsQISGGQRQRTAIGRALVLGP 164
Cdd:cd03247 72 ------ALSSLISV-------------------LNQRPYLFDTTLRNNLGR---------RFSGGERQRLALARILLQDA 117
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1490467399 165 DLLLMDEPFSSLDAPTRESLeeLTLKLQAERGLTVITVTH 204
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQL--LSLIFEVLKDKTLIWITH 155
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
23-207 |
1.20e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.51 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFGLL----------PwrTV 92
Cdd:PRK13639 21 INF--KAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVGIVfqnpddqlfaP--TV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 93 MENIAlglevrsfYGPDGLHAPKrplpEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEP 172
Cdd:PRK13639 97 EEDVA--------FGPLNLGLSK----EEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEP 164
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 173 FSSLDAPTRESLEELTLKLQaERGLTVITVTHSIE 207
Cdd:PRK13639 165 TSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVD 198
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
32-253 |
1.29e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.42 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRpdSALILQDFGLLPWR-------TVMENIALGlevrs 104
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYA--SKEVARRIGLLAQNattpgdiTVQELVARG----- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdglHAPKRPL-----PEAPDAlVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:PRK10253 106 -------RYPHQPLftrwrKEDEEA-VTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghpphRE-PVVVEGPPPKRDHPDFYKVCSKLRSIL 253
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL-----REgKIVAQGAPKEIVTAELIERIYGLRCMI 247
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
36-210 |
1.39e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.83 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLS--GLIRPQ---GGEVRIGGVKLERPRPDSALILQDFGLL-----PW-RTVMENIALGLEVRs 104
Cdd:PRK14239 35 ALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYSPRTDTVDLRKEIGMVfqqpnPFpMSIYENVVYGLRLK- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdGLHaPKRPLpeapDALVDYWLKRLGL-EAVADH-YPSQI--SGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:PRK14239 114 -----GIK-DKQVL----DEAVEKSLKGASIwDEVKDRlHDSALglSGGQQQRVCIARVLATSPKIILLDEPTSALDPIS 183
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 181 RESLEELTLKLQAErgLTVITVTHSIEEAA 210
Cdd:PRK14239 184 AGKIEETLLGLKDD--YTMLLVTRSMQQAS 211
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
30-210 |
1.47e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.82 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPrpDSALILQDFGLLPWRTvmeNIALGLEVRSFYgPD 109
Cdd:PRK09536 27 REGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL--SARAASRRVASVPQDT---SLSFEFDVRQVV-EM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 110 GLHaPKR----PLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD----APTR 181
Cdd:PRK09536 101 GRT-PHRsrfdTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDinhqVRTL 179
|
170 180
....*....|....*....|....*....
gi 1490467399 182 ESLEELtlklqAERGLTVITVTHSIEEAA 210
Cdd:PRK09536 180 ELVRRL-----VDDGKTAVAAIHDLDLAA 203
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
6-204 |
1.63e-19 |
|
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: 82.11 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHlPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVklerprpdsalilqdfg 85
Cdd:cd03221 1 IELENLSKTYGGK-LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 86 llpwrtvmENIAlglevrsfygpdglhapkrplpeapdalvdywlkrlgleavadhYPSQISGGQRQRTAIGRALVLGPD 165
Cdd:cd03221 63 --------VKIG--------------------------------------------YFEQLSGGEKMRLALAKLLLENPN 90
|
170 180 190
....*....|....*....|....*....|....*....
gi 1490467399 166 LLLMDEPFSSLDAPTRESLEELtlkLQAERGlTVITVTH 204
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEA---LKEYPG-TVILVSH 125
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-210 |
1.70e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 84.71 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 35 WAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLE-----------RPRPDSALILQDFGLLPWRTVMENIALGLEVR 103
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifqidaiKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 SFygpdglhAPKRPLPEapdaLVDYWLKRLGL-EAVADHY---PSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:PRK14246 119 GI-------KEKREIKK----IVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIV 187
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 180 TRESLEELTLKLQAErgLTVITVTHSIEEAA 210
Cdd:PRK14246 188 NSQAIEKLITELKNE--IAIVIVSHNPQQVA 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-207 |
1.96e-19 |
|
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: 83.29 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHL----PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvklerprpDSALIL 81
Cdd:cd03250 1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------SIAYVS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 82 QdfglLPW---RTVMENIALGLEVRS-FYgpdglhapKRPLpEA----PDalvdywlkrlgLEAVADHYPSQI------- 146
Cdd:cd03250 73 Q----EPWiqnGTIRENILFGKPFDEeRY--------EKVI-KAcalePD-----------LEILPDGDLTEIgekginl 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 147 SGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIE 207
Cdd:cd03250 129 SGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQ 189
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
6-209 |
4.00e-19 |
|
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: 86.31 E-value: 4.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPH-LPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----AL 79
Cdd:TIGR02203 331 VEFRNVTFRYPGRdRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrrqvAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFGLLPwRTVMENIAlglevrsfYG-PDGLhapkrPLPEAPDALVDYWLKR------LGLEAVADHYPSQISGGQRQ 152
Cdd:TIGR02203 411 VSQDVVLFN-DTIANNIA--------YGrTEQA-----DRAEIERALAAAYAQDfvdklpLGLDTPIGENGVLLSGGQRQ 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 153 RTAIGRALVLGPDLLLMDEPFSSLDAPT----RESLEELTlklqaeRGLTVITVTH---SIEEA 209
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESerlvQAALERLM------QGRTTLVIAHrlsTIEKA 534
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-208 |
4.53e-19 |
|
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: 81.71 E-value: 4.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALIL---------QDFGLLPWRTVMENIALg 99
Cdd:cd03215 23 VRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedrKREGLVLDLSVAENIAL- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 levrsfygpdglhapkrplpeapdalvdywlkrlgleavadhyPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:cd03215 102 -------------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180
....*....|....*....|....*....
gi 1490467399 180 TRESLEELTLKLqAERGLTVITVTHSIEE 208
Cdd:cd03215 139 AKAEIYRLIREL-ADAGKAVLLISSELDE 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
32-217 |
5.11e-19 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 83.44 E-value: 5.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvKLERPRPDSALILQDFGLLpWRT----VMENIALGLEVR-SFY 106
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRM-RDGQLRDLYALSEAERRRL-LRTewgfVHQHPRDGLRMQvSAG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 GPDG---LHAPKRPLPEAPDALVDyWLKRLGLEAV-ADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRE 182
Cdd:PRK11701 110 GNIGerlMAVGARHYGDIRATAGD-WLERVEIDAArIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQA 188
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 183 SLEELTLKLQAERGLTVITVTHSIEEAAFLGRKIL 217
Cdd:PRK11701 189 RLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLL 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-210 |
1.77e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPL----FLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV---------KLER 72
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 73 PRPDSALILQ-DFGLLPWRTVMENIAlglevrsfYGPDGLHAPKrplpEAPDALVDYWLKRLGL-EAVADHYPSQISGGQ 150
Cdd:PRK13643 82 VRKKVGVVFQfPESQLFEETVLKDVA--------FGPQNFGIPK----EKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 151 RQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQaERGLTVITVTHSIEEAA 210
Cdd:PRK13643 150 MRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVA 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
31-208 |
1.96e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.19 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 31 KGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAL------ILQDFGLLPWRTVMENIALGlevrs 104
Cdd:PRK11288 29 AGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALaagvaiIYQELHLVPEMTVAENLYLG----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdglHAPKRplpeapDALVD-----YW----LKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:PRK11288 104 -------QLPHK------GGIVNrrllnYEareqLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190
....*....|....*....|....*....|...
gi 1490467399 176 LDAPTRESLEELTLKLQAErGLTVITVTHSIEE 208
Cdd:PRK11288 171 LSAREIEQLFRVIRELRAE-GRVILYVSHRMEE 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-204 |
4.94e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRP---QGGEVRIGGVKLERP--RPDSALILQDFGLLPWRTVMENIALGLEV 102
Cdd:TIGR00955 47 VAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKemRAISAYVQQDDLFIPTLTVREHLMFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RsfygpdglhAPKRPLPEAPDALVDYWLKRLGLEAVAD---HYPSQ---ISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:TIGR00955 127 R---------MPRRVTKKEKRERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180
....*....|....*....|....*...
gi 1490467399 177 DAPTRESLEElTLKLQAERGLTVITVTH 204
Cdd:TIGR00955 198 DSFMAYSVVQ-VLKGLAQKGKTIICTIH 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
31-210 |
7.27e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.55 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 31 KGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP-----RPDSALILQD-----FGLlpwrTVMENIAlgl 100
Cdd:PRK13647 30 EGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnekwvRSKVGLVFQDpddqvFSS----TVWDDVA--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 evrsfYGPDGLH-APKRPLPEAPDALvdywlKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:PRK13647 103 -----FGPVNMGlDKDEVERRVEEAL-----KAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 180 TRESLEELTLKLQAErGLTVITVTHSIEEAA 210
Cdd:PRK13647 173 GQETLMEILDRLHNQ-GKTVIVATHDVDLAA 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-207 |
1.09e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 24 NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIG----GVKLERPRPDSALI---LQDFGLLpwRTVMENI 96
Cdd:PRK13631 44 NISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYskkIKNFKEL--RRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALGLEVRSF---------YGPDGLHAPKrplpEAPDALVDYWLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDL 166
Cdd:PRK13631 122 FQFPEYQLFkdtiekdimFGPVALGVKK----SEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEI 197
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1490467399 167 LLMDEPFSSLDAPTRESLEELTLKLQAErGLTVITVTHSIE 207
Cdd:PRK13631 198 LIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTME 237
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
29-210 |
1.48e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 79.79 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL--ERPRPDSALILQDFGL--------LPWRTVMENIAl 98
Cdd:PRK13649 30 IEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItsTSKNKDIKQIRKKVGLvfqfpesqLFEETVLKDVA- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 glevrsfYGPDGLHAPKrplpEAPDALVDYWLKRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:PRK13649 109 -------FGPQNFGVSQ----EEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190
....*....|....*....|....*....|...
gi 1490467399 178 APTRESLEELTLKLQaERGLTVITVTHSIEEAA 210
Cdd:PRK13649 178 PKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVA 209
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-204 |
1.74e-17 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.54 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 24 NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIgGVKLERPRPDSALILQDfgllPWRTVMENIALG---L 100
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAELD----PEKTVMDNLAEGkqeV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSF------YGPDGLHAPKRPLpeAPdalvdywLKRLgleavadhypsqiSGGQRQRTAIGRaLVLGP-DLLLMDEPF 173
Cdd:PRK11147 412 MVNGRprhvlgYLQDFLFHPKRAM--TP-------VKAL-------------SGGERNRLLLAR-LFLKPsNLLILDEPT 468
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 174 SSLDAPTRESLEELTLKLQAerglTVITVTH 204
Cdd:PRK11147 469 NDLDVETLELLEELLDSYQG----TVLLVSH 495
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-207 |
1.77e-17 |
|
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: 78.63 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 19 LPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIggvklerpRPDSALIlqDFGLLPWRTVmenial 98
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV--------RHDGGWV--DLAQASPREI------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 gLEVR--------SFygpdgLHAPKR---------PL------PEAPDALVDYWLKRLGL-EAVADHYPSQISGGQRQRT 154
Cdd:COG4778 88 -LALRrrtigyvsQF-----LRVIPRvsaldvvaePLlergvdREEARARARELLARLNLpERLWDLPPATFSGGEQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 155 AIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAeRGLTVITVTHSIE 207
Cdd:COG4778 162 NIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKA-RGTAIIGIFHDEE 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-204 |
3.23e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.64 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKP-HLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERpRPDSALiLQDF 84
Cdd:PRK11160 339 LTLNNVSFTYPDqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIAD-YSEAAL-RQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 GLLPWR------TVMENIALGLevrsfygpdglhapkrplPEAPDALVDYWLKRLGLEAVADHYPS----------QISG 148
Cdd:PRK11160 417 SVVSQRvhlfsaTLRDNLLLAA------------------PNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSG 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 149 GQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTREslEELTLKLQAERGLTVITVTH 204
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETER--QILELLAEHAQNKTVLMITH 532
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
8-219 |
4.06e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 4.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFAWK---PHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPR---------- 74
Cdd:PRK10261 15 VENLNIAFMqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqvielseqs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 75 ---------PDSALILQD--FGLLPWRTVMENIALGLEV-RSFYGPDGLHAPKRPLPEA--PDAlvdywlkrlglEAVAD 140
Cdd:PRK10261 95 aaqmrhvrgADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVriPEA-----------QTILS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490467399 141 HYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCL 219
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
8-204 |
4.20e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.11 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKT----TLLYLLSGLIRPQGGEVRIGGVKLERpRPDSAL---- 79
Cdd:COG4172 26 VKGVSF--------------DIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG-LSERELrrir 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ------ILQD--FGLLPWRTVMENIALGLEvrsfygpdgLHAPKRPlpEAPDALVDYWLKRLGL---EAVADHYPSQISG 148
Cdd:COG4172 91 gnriamIFQEpmTSLNPLHTIGKQIAEVLR---------LHRGLSG--AAARARALELLERVGIpdpERRLDAYPHQLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 149 GQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
6-207 |
4.34e-17 |
|
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: 77.53 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL---NFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVK-----LERPRPDS 77
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLkniSF--SIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDiskigLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 78 ALILQD----FGllpwrTVMENIAlglevrsfygPDGLHAPKrplpEAPDALVDYWLKRL------GLEAVADHYPSQIS 147
Cdd:cd03244 81 SIIPQDpvlfSG-----TIRSNLD----------PFGEYSDE----ELWQALERVGLKEFveslpgGLDTVVEEGGENLS 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 148 GGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEElTLKlQAERGLTVITVTHSIE 207
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK-TIR-EAFKDCTVLTIAHRLD 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-216 |
4.95e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.10 E-value: 4.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVklerPRPDSA--------LILQDFGLLPWRTVMENial 98
Cdd:PRK13536 62 FTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV----PVPARArlararigVVPQFDNLDLEFTVREN--- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 gLEVRSFYGpdGLHApkRPLPEAPDALVDYwlkrLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:PRK13536 135 -LLVFGRYF--GMST--REIEAVIPSLLEF----ARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490467399 179 PTRESLEELTLKLQAeRGLTVITVTHSIEEAAFL---------GRKI 216
Cdd:PRK13536 206 HARHLIWERLRSLLA-RGKTILLTTHFMEEAERLcdrlcvleaGRKI 251
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
36-207 |
5.71e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 78.31 E-value: 5.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP-----RPDSALILQ---DFGLLPwrTVMENIAlglevrsfYG 107
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevRKFVGLVFQnpdDQIFSP--TVEQDIA--------FG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 108 PDGLHAPKrplpEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEL 187
Cdd:PRK13652 104 PINLGLDE----ETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180
....*....|....*....|
gi 1490467399 188 TLKLQAERGLTVITVTHSIE 207
Cdd:PRK13652 180 LNDLPETYGMTVIFSTHQLD 199
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-251 |
3.24e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.20 E-value: 3.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL----------ERPRPDSALILQ--DFGLLPwRTVMENI 96
Cdd:PRK13645 34 FKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkikevKRLRKEIGLVFQfpEYQLFQ-ETIEKDI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 AlglevrsfYGPDGLHAPK----RPLPEAPD--ALVDYWLKRlgleavadhYPSQISGGQRQRTAIGRALVLGPDLLLMD 170
Cdd:PRK13645 113 A--------FGPVNLGENKqeayKKVPELLKlvQLPEDYVKR---------SPFELSGGQKRRVALAGIIAMDGNTLVLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 171 EPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP------------PKRD 238
Cdd:PRK13645 176 EPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM----HEGKVISIGSPfeifsnqelltkIEID 251
|
250
....*....|...
gi 1490467399 239 HPDFYKVCSKLRS 251
Cdd:PRK13645 252 PPKLYQLMYKLKN 264
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
27-210 |
6.49e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.13 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERP-----RPDSALILQD-FGLLPWRTVMENIALGL 100
Cdd:PRK13642 28 FSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnvwnlRRKIGMVFQNpDNQFVGATVEDDVAFGM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSFygpdglhaPKRPLPEApdalVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:PRK13642 108 ENQGI--------PREEMIKR----VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAA 205
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-233 |
1.15e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 74.00 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL-ERPRPDSALI-----LQDFGLLPWRTVMENI 96
Cdd:COG4674 29 LSL--YVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLtGLDEHEIARLgigrkFQKPTVFEELTVFENL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALGL-EVRSFYGpdglhAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:COG4674 107 ELALkGDRGVFA-----SLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAG 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 176 LDAPTRESLEELTLKLQAERglTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGP 233
Cdd:COG4674 182 MTDAETERTAELLKSLAGKH--SVVVVEHDMEFVRQIARKVTVL----HQGSVLAEGS 233
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
32-204 |
1.92e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 75.69 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQG--GEVRIGGVKLERP-RPDSALILQDFGLLPWRTVMENIALGLEVRSfygP 108
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQiLKRTGFVTQDDILYPHLTVRETLVFCSLLRL---P 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 DGLHAPKRPLPeAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLeELT 188
Cdd:PLN03211 171 KSLTKQEKILV-AESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL-VLT 248
|
170
....*....|....*.
gi 1490467399 189 LKLQAERGLTVITVTH 204
Cdd:PLN03211 249 LGSLAQKGKTIVTSMH 264
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-210 |
2.52e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 73.59 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRP-----QGGEVRIGGVKLERPRpDSALILQDFGLLPWR------TVMENIALGLEVRS 104
Cdd:PRK14271 51 SLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYR-DVLEFRRRVGMLFQRpnpfpmSIMDNVLAGVRAHK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 FygpdglhAPKRPLPEAPDALvdywLKRLGL-EAVADHY---PSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:PRK14271 130 L-------VPRKEFRGVAQAR----LTEVGLwDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTT 198
|
170 180 190
....*....|....*....|....*....|
gi 1490467399 181 RESLEELTLKLqAERgLTVITVTHSIEEAA 210
Cdd:PRK14271 199 TEKIEEFIRSL-ADR-LTVIIVTHNLAQAA 226
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
31-234 |
3.43e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 31 KGESWAIIGPSGCGKTTLLYLLSGLIrPQGGEVRIGGVKLERPRPDS-----ALILQDFGLLPWRTVMENIAlglevrsf 105
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAElarhrAYLSQQQSPPFAMPVFQYLA-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 106 ygpdgLHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALV-----LGPD--LLLMDEPFSSLDA 178
Cdd:COG4138 92 -----LHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 179 PTRESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCLghppHREPVVVEGPP 234
Cdd:COG4138 167 AQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLL----KQGKLVASGET 217
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-207 |
5.64e-15 |
|
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: 71.59 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALILQDFG 85
Cdd:cd03290 1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 86 LL-----PW---RTVMENIALGlevrSFYGPDGLHAPKRPLPEAPDalVDywLKRLGLEAVADHYPSQISGGQRQRTAIG 157
Cdd:cd03290 81 VAyaaqkPWllnATVEENITFG----SPFNKQRYKAVTDACSLQPD--ID--LLPFGDQTEIGERGINLSGGQRQRICVA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESL-EELTLKLQAERGLTVITVTHSIE 207
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLmQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-216 |
5.83e-15 |
|
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: 74.28 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLErprPDSALILQDFGLLPWRTVMENIALGLEVRSFYGpdglHAPK 115
Cdd:TIGR01257 960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE---TNLDAVRQSLGMCPQHNILFHHLTVAEHILFYA----QLKG 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 116 RPLPEAPDALvDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAER 195
Cdd:TIGR01257 1033 RSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR 1111
|
170 180
....*....|....*....|.
gi 1490467399 196 glTVITVTHSIEEAAFLGRKI 216
Cdd:TIGR01257 1112 --TIIMSTHHMDEADLLGDRI 1130
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-204 |
1.06e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 73.08 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPD------SAlILQDFGLLpwrtvmenialglev 102
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEdyrklfSA-VFTDFHLF--------------- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RSFYGPDGLhapkrplpEAPDALVDYWLKRLGLE---AVADHYPS--QISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:PRK10522 410 DQLLGPEGK--------PANPALVEKWLERLKMAhklELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180
....*....|....*....|....*..
gi 1490467399 178 APTRESLEELTLKLQAERGLTVITVTH 204
Cdd:PRK10522 482 PHFRREFYQVLLPLLQEMGKTIFAISH 508
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
23-217 |
1.09e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGgevRIGGV--------------KLERPRPDS-ALILQD--FG 85
Cdd:PRK09473 35 LNF--SLRAGETLGIVGESGSGKSQTAFALMGLLAANG---RIGGSatfngreilnlpekELNKLRAEQiSMIFQDpmTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 86 LLPWRTV----MENIAL--GL--------EVRSfygpdgLHAPKrpLPEApdalvdywLKRLGLeavadhYPSQISGGQR 151
Cdd:PRK09473 110 LNPYMRVgeqlMEVLMLhkGMskaeafeeSVRM------LDAVK--MPEA--------RKRMKM------YPHEFSGGMR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 152 QRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAAFLGRKIL 217
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVL 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
23-207 |
1.48e-14 |
|
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: 70.64 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvklerpRPDSALILQdFGLLPWRTVMENIALGLev 102
Cdd:cd03220 41 VSF--EVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGLG-GGFNPELTGRENIYLNG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rSFYGPDglhapkrplPEAPDALVDYWLKRLGLEAVAD----HYpsqiSGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:cd03220 110 -RLLGLS---------RKEIDEKIDEIIEFSELGDFIDlpvkTY----SSGMKARLAFAIATALEPDILLIDEVLAVGDA 175
|
170 180 190
....*....|....*....|....*....|...
gi 1490467399 179 PTRE----SLEELTlklqaERGLTVITVTHSIE 207
Cdd:cd03220 176 AFQEkcqrRLRELL-----KQGKTVILVSHDPS 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-208 |
1.68e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGlIRPQG---GEVRIGGVKL------ERPRPDSALILQDFGLLPWRTVMENIALG 99
Cdd:PRK13549 28 VRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELqasnirDTERAGIAIIHQELALVKELSVLENIFLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVRsfygpdglhapkrplpeaPDALVDY---------WLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMD 170
Cdd:PRK13549 107 NEIT------------------PGGIMDYdamylraqkLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 1490467399 171 EPFSSLDAPTRESLEELTLKLQAeRGLTVITVTHSIEE 208
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNE 205
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-209 |
2.34e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.27 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL----NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV------------------ 63
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 64 -------------RIGGVKLERPRPDSALILQDFGLLPwRTVMENIAlglevrsfYGPDGLHAPKRplpEAPDALVDYwL 130
Cdd:PRK13651 83 vleklviqktrfkKIKKIKEIRRRVGVVFQFAEYQLFE-QTIEKDII--------FGPVSMGVSKE---EAKKRAAKY-I 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 131 KRLGL-EAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD-APTRESLEELTlKLQaERGLTVITVTHSIEE 208
Cdd:PRK13651 150 ELVGLdESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFD-NLN-KQGKTIILVTHDLDN 227
|
.
gi 1490467399 209 A 209
Cdd:PRK13651 228 V 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-204 |
2.39e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHlPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPR----PDSALIL 81
Cdd:PRK13540 2 LDVIELDFDYHDQ-PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLctyqKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 82 QDFGLLPWRTVMENIALGLEVRSfygpdglhapkrplpeaPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALV 161
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSP-----------------GAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWM 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 162 LGPDLLLMDEPFSSLDaptRESLEELTLKLQAER--GLTVITVTH 204
Cdd:PRK13540 144 SKAKLWLLDEPLVALD---ELSLLTIITKIQEHRakGGAVLLTSH 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
5-207 |
3.07e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.11 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 5 FVEVKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-VklerprpdSALIlqD 83
Cdd:COG1134 39 FWALKDVSF--------------EVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrV--------SALL--E 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 84 F--GLLPWRTVMENIALGLevrSFYGpdglhAPKRPLPEAPDALVDYwlkrLGLEAVAD----HYPSqisgGQRQRTAIG 157
Cdd:COG1134 95 LgaGFHPELTGRENIYLNG---RLLG-----LSRKEIDEKFDEIVEF----AELGDFIDqpvkTYSS----GMRARLAFA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRE----SLEELtlklqAERGLTVITVTHSIE 207
Cdd:COG1134 159 VATAVDPDILLVDEVLAVGDAAFQKkclaRIREL-----RESGRTVIFVSHSMG 207
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-208 |
3.93e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 71.62 E-value: 3.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEV-KGIDFAwkphlplflnfwwhLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSA------ 78
Cdd:PRK15439 24 VEVlKGIDFT--------------LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhqlgiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 LILQDFGLLPWRTVMENIALGLevrsfygpdglhaPKRPLPEAPdalVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGR 158
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGL-------------PKRQASMQK---MKQLLAALGCQLDLDSSAGSLEVADRQIVEILR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1490467399 159 ALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAErGLTVITVTHSIEE 208
Cdd:PRK15439 154 GLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPE 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
8-208 |
3.98e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.20 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSALIL------ 81
Cdd:COG1129 268 VRDVSF--------------SVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgiayvp 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 82 ---QDFGLLPWRTVMENIALGLEVRsfYGPDGLHAPKRplpEApdALVDYWLKRLGLEAVADHYP-SQISGGQRQRTAIG 157
Cdd:COG1129 334 edrKGEGLVLDLSIRENITLASLDR--LSRGGLLDRRR---ER--ALAEEYIKRLRIKTPSPEQPvGNLSGGNQQKVVLA 406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTHSIEE 208
Cdd:COG1129 407 KWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPE 456
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
29-208 |
5.00e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKL------ERPRPDSALILQDFGLLPWRTVMENIALGLEV 102
Cdd:PRK10895 26 VNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARARRGIGYLPQEASIFRRLSVYDNLMAVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RsfygpDGLHAPKRPlpEAPDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRE 182
Cdd:PRK10895 106 R-----DDLSAEQRE--DRANEL----MEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
|
170 180
....*....|....*....|....*.
gi 1490467399 183 SLEELTLKLQaERGLTVITVTHSIEE 208
Cdd:PRK10895 175 DIKRIIEHLR-DSGLGVLITDHNVRE 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
37-204 |
5.39e-14 |
|
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: 71.12 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 37 IIGPSGCGKTTLLYLLSGLIRPQGGEVRIG-GVKLerprpdsALILQDFGLLPWRTVMENIALGL-----------EVRS 104
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKV-------GYLPQEPQLDPTKTVRENVEEGVaeikdaldrfnEISA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 FYGP-----DGLHAPKRPLPEAPDAlVDYWLKRLGLEAVAD--HYP------SQISGGQRQRTAIGRALVLGPDLLLMDE 171
Cdd:TIGR03719 109 KYAEpdadfDKLAAEQAELQEIIDA-ADAWDLDSQLEIAMDalRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDE 187
|
170 180 190
....*....|....*....|....*....|...
gi 1490467399 172 PFSSLDAptrESLEELTLKLQAERGlTVITVTH 204
Cdd:TIGR03719 188 PTNHLDA---ESVAWLERHLQEYPG-TVVAVTH 216
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-204 |
5.69e-14 |
|
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: 70.98 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPD------SAlILQDFGLLpwrtvmenialglev 102
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREayrqlfSA-VFSDFHLF--------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RSFYGPDGlhapkrplpEAPDALVDYWLKRLGLE---AVADHYPS--QISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:COG4615 419 DRLLGLDG---------EADPARARELLERLELDhkvSVEDGRFSttDLSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180
....*....|....*....|....*...
gi 1490467399 178 APTRESL-EELTLKLQAeRGLTVITVTH 204
Cdd:COG4615 490 PEFRRVFyTELLPELKA-RGKTVIAISH 516
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-222 |
6.12e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 69.65 E-value: 6.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 21 LFLNFWWHLKKGeswaIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPdsalilqdfGLLPWRTVMENIALGL 100
Cdd:PRK13638 20 LNLDFSLSPVTG----LVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKR---------GLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSFYgpdglhapkrplpEAPDALVDYWLKRLGL----------EAV----ADHYPSQ----ISGGQRQRTAIGRALVL 162
Cdd:PRK13638 87 EQQIFY-------------TDIDSDIAFSLRNLGVpeaeitrrvdEALtlvdAQHFRHQpiqcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490467399 163 GPDLLLMDEPFSSLDAPTRESLEELTLKLQAErGLTVITVTHSIE------EAAFLGRK--ILCLGHP 222
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDliyeisDAVYVLRQgqILTHGAP 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-208 |
6.53e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 70.97 E-value: 6.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSA------LILQDFGLLPWRTVMENIALG-LE 101
Cdd:PRK09700 28 VYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAaqlgigIIYQELSVIDELTVLENLYIGrHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 102 VRSFYGPDglhapkrplpeapdaLVDY---------WLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEP 172
Cdd:PRK09700 108 TKKVCGVN---------------IIDWremrvraamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 1490467399 173 FSSLdapTRESLEELTL---KLQAErGLTVITVTHSIEE 208
Cdd:PRK09700 173 TSSL---TNKEVDYLFLimnQLRKE-GTAIVYISHKLAE 207
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-204 |
6.95e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 17 PHLPLFLNFWWHLKKGESWAIIGPSGCGKT----TLLYLLSGLIRPQGGEVRIGGVKLE----RPRpDSALILQD----F 84
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVApcalRGR-KIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 GllPWRTVMENIALGLEVRsfygpdGLHAPKRPLPEAPDALvdywlkrlGLE---AVADHYPSQISGGQRQRTAIGRALV 161
Cdd:PRK10418 93 N--PLHTMHTHARETCLAL------GKPADDATLTAALEAV--------GLEnaaRVLKLYPFEMSGGMLQRMMIALALL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490467399 162 LGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTH 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-216 |
9.30e-14 |
|
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: 70.24 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGlIRPQG---GEVRIGGVKL------ERPRPDSALILQDFGLLPWRTVMENIALG 99
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLkasnirDTERAGIVIIHQELTLVPELSVAENIFLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVrsfygpdglhapkrplpEAPDALVDY---------WLKRLGLEAVADHYP-SQISGGQRQRTAIGRALVLGPDLLLM 169
Cdd:TIGR02633 103 NEI-----------------TLPGGRMAYnamylraknLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490467399 170 DEPFSSLDAPTRESLEELTLKLQAeRGLTVITVTHSIEEAAFLGRKI 216
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTI 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
30-210 |
1.85e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLErPRpDSAL------ILQDFGLLPWRTVMENiaLGLEVR 103
Cdd:NF033858 290 RRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD-AG-DIATrrrvgyMSQAFSLYGELTVRQN--LELHAR 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 SFygpdglHAPKRPLPEAPDALVDywlkRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRES 183
Cdd:NF033858 366 LF------HLPAAEIAARVAEMLE----RFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180
....*....|....*....|....*..
gi 1490467399 184 LEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:NF033858 436 FWRLLIELSREDGVTIFISTHFMNEAE 462
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-251 |
2.71e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 69.27 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDsalILQDFGLLPWRTVMENIALGLEvrSFYgp 108
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD---VHQNMGYCPQFDAIDDLLTGRE--HLY-- 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 dgLHAPKRPLP-EAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEL 187
Cdd:TIGR01257 2035 --LYARLRGVPaEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 188 TLKLQAErGLTVITVTHSIEEAAFLGRKIL--------CLGHPPHRepvvvegpppKRDHPDFYKVCSKLRS 251
Cdd:TIGR01257 2113 IVSIIRE-GRAVVLTSHSMEECEALCTRLAimvkgafqCLGTIQHL----------KSKFGDGYIVTMKIKS 2173
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-210 |
4.94e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 4.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFwwhlKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPrpDSALILQDFGLLPWR-------TV 92
Cdd:PRK10575 29 PLSLTF----PAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW--SSKAFARKVAYLPQQlpaaegmTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 93 MENIALGLevRSFYGPDG-LHAPKRPLPEAPDALVdywlkrlGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDE 171
Cdd:PRK10575 103 RELVAIGR--YPWHGALGrFGAADREKVEEAISLV-------GLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1490467399 172 PFSSLDAPTRESLEELTLKLQAERGLTVITVTHSIEEAA 210
Cdd:PRK10575 174 PTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAA 212
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-208 |
7.93e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 7.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG--VKLERPRpDS-----ALILQDFGLLPWRTVMENIALGlevRS 104
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPK-SSqeagiGIIHQELNLIPQLTIAENIFLG---RE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 FYGPDGLHAPKRPLPEApDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:PRK10762 106 FVNRFGRIDWKKMYAEA-DKL----LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESL 180
|
170 180
....*....|....*....|....
gi 1490467399 185 EELTLKLQAErGLTVITVTHSIEE 208
Cdd:PRK10762 181 FRVIRELKSQ-GRGIVYISHRLKE 203
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-223 |
8.35e-13 |
|
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: 65.89 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLE-RPR---PDSALILQDFgllpwrtvMENIALGLEVRS 104
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSyKPQyikADYEGTVRDL--------LSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 FYGPDglhapkrplpeapdalvdyWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESL 184
Cdd:cd03237 94 YFKTE-------------------IAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490467399 185 EELTLKLQAERGLTVITVTHSIEEAAFLGRKIL---------CLGHPP 223
Cdd:cd03237 155 SKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIvfegepsvnGVANPP 202
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
27-211 |
9.28e-13 |
|
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: 64.48 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLIRpqggevrIGGVKLERPRPDSALilqdfgLLPWRTvmenialglevrsfY 106
Cdd:cd03223 22 FEIKPGDRLLITGPSGTGKSSLFRALAGLWP-------WGSGRIGMPEGEDLL------FLPQRP--------------Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 GPDGLHApkrplpeapDALVDYWLKRLgleavadhypsqiSGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEE 186
Cdd:cd03223 75 LPLGTLR---------EQLIYPWDDVL-------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170 180
....*....|....*....|....*
gi 1490467399 187 LtLKlqaERGLTVITVTHSIEEAAF 211
Cdd:cd03223 133 L-LK---ELGITVISVGHRPSLWKF 153
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
8-204 |
1.48e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 66.26 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvklERPRPDSALILQDFGL- 86
Cdd:COG4586 38 VDDISF--------------TIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKEFARRIGVv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 87 ----------LPwrtVMENIALgleVRSFYG-PDGLHApKRplpeapdalVDYWLKRLGLEAVADHYPSQISGGQRQRTA 155
Cdd:COG4586 101 fgqrsqlwwdLP---AIDSFRL---LKAIYRiPDAEYK-KR---------LDELVELLDLGELLDTPVRQLSLGQRMRCE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490467399 156 IGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSH 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-181 |
1.58e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.58 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGlIRPQG--------------GEV------RIGGVKlerprpdSALILQdfgl 86
Cdd:PRK10938 281 WQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQGysndltlfgrrrgsGETiwdikkHIGYVS-------SSLHLD---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 87 lpWR---TVMENIALGlevrsFYGPDGLHapkRPLPEAPDALVDYWLKRLGLEA-VADHYPSQISGGQRQRTAIGRALVL 162
Cdd:PRK10938 349 --YRvstSVRNVILSG-----FFDSIGIY---QAVSDRQQKLAQQWLDILGIDKrTADAPFHSLSWGQQRLALIVRALVK 418
|
170
....*....|....*....
gi 1490467399 163 GPDLLLMDEPFSSLDAPTR 181
Cdd:PRK10938 419 HPTLLILDEPLQGLDPLNR 437
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1-204 |
1.65e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.98 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 1 MENFFVEVKGIDFAWKPHLPLflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLI--RPQGGEVRIGGVKLERPRPdsa 78
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNL------EIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGREAS--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 79 lILQDFGLLpwrtvmENIALGLEVrsfygpdgLHAPKrpLPEAPdalvdYWLKRlgleavadhyPSQISGGQRQRTAIGR 158
Cdd:COG2401 102 -LIDAIGRK------GDFKDAVEL--------LNAVG--LSDAV-----LWLRR----------FKELSTGQKFRFRLAL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1490467399 159 ALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
29-204 |
2.08e-12 |
|
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: 66.36 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGL--IRPQGGEV--------RIGGV----KLERPRPDSALILQDFGLLPW----- 89
Cdd:TIGR03269 23 IEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalceKCGYVerpsKVGEPCPVCGGTLEPEEVDFWnlsdk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 90 --RTVMENIALGLEvRSF--YGPD--------GLHAPKRPLPEAPDALVDYwLKRLGLEAVADHYPSQISGGQRQRTAIG 157
Cdd:TIGR03269 103 lrRRIRKRIAIMLQ-RTFalYGDDtvldnvleALEEIGYEGKEAVGRAVDL-IEMVQLSHRITHIARDLSGGEKQRVVLA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTH 204
Cdd:TIGR03269 181 RQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-207 |
2.24e-12 |
|
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: 65.26 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPrpdsalilQDFGLLPwRTVMENIALG 99
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSS--------QFSWIMP-GTIKENIIFG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 LEVRSFYGPDGLHAPKrpLPEAPDALVDYWLKRLGLEAVAdhypsqISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:cd03291 122 VSYDEYRYKSVVKACQ--LEEDITKFPEKDNTVLGEGGIT------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180
....*....|....*....|....*....
gi 1490467399 180 T-RESLEELTLKLQAERglTVITVTHSIE 207
Cdd:cd03291 194 TeKEIFESCVCKLMANK--TRILVTSKME 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-209 |
3.01e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.81 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAW--KPHLPLF-LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGV-----KLERPRPDS 77
Cdd:PRK11176 342 IEFRNVTFTYpgKEVPALRnINF--KIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHdlrdyTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 78 ALILQDFGLLPwRTVMENIAlglevrsfYGPDGLHAPKRPLPEAPDALVDYWLKRL--GLEAVADHYPSQISGGQRQRTA 155
Cdd:PRK11176 420 ALVSQNVHLFN-DTIANNIA--------YARTEQYSREQIEEAARMAYAMDFINKMdnGLDTVIGENGVLLSGGQRQRIA 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 156 IGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERglTVITVTH---SIEEA 209
Cdd:PRK11176 491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHrlsTIEKA 545
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-207 |
3.31e-12 |
|
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: 66.09 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRpdsalilqdfglLPW---RTVMENI 96
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQ------------TSWimpGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALGL-----EVRSFYGPDGLHAPKRPLPEApDALVdywlkrLGLEAVAdhypsqISGGQRQRTAIGRALVLGPDLLLMDE 171
Cdd:TIGR01271 508 IFGLsydeyRYTSVIKACQLEEDIALFPEK-DKTV------LGEGGIT------LSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190
....*....|....*....|....*....|....*..
gi 1490467399 172 PFSSLDAPT-RESLEELTLKLQAERglTVITVTHSIE 207
Cdd:TIGR01271 575 PFTHLDVVTeKEIFESCLCKLMSNK--TRILVTSKLE 609
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
6-200 |
3.33e-12 |
|
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: 63.59 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFL-NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG-----VKLERPRPDSAL 79
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLkNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFGLLpwrtvMENIALGLEVRSFYGPDGLHAPKRplpeapdalvdywLKRLGLeavadhypsQISGGQRQRTAIGRA 159
Cdd:cd03369 87 IPQDPTLF-----SGTIRSNLDPFDEYSDEEIYGALR-------------VSEGGL---------NLSQGQRQLLCLARA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490467399 160 LVLGPDLLLMDEPFSSLDAPT--------RESLEELTLKLQAERGLTVI 200
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATdaliqktiREEFTNSTILTIAHRLRTII 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-177 |
7.66e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.94 E-value: 7.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG---VKLERPRpDSALILQDFGLLPWRTVMENI 96
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktaTRGDRSR-FMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALglevrsFYGPDGLHApkRPLPEAPDALVdywlkrlGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:PRK13543 104 HF------LCGLHGRRA--KQMPGSALAIV-------GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168
|
.
gi 1490467399 177 D 177
Cdd:PRK13543 169 D 169
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-206 |
1.11e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 2 ENFFVEVKGIDFAWKPHLPLFLN-FWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRpdSALI 80
Cdd:TIGR00957 633 EGNSITVHNATFTWARDLPPTLNgITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQ--QAWI 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 81 LQDfgllpwrTVMENIALGLEVRSFYgpdglhapKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRAL 160
Cdd:TIGR00957 711 QND-------SLRENILFGKALNEKY--------YQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1490467399 161 VLGPDLLLMDEPFSSLDAPT-RESLEELTLKLQAERGLTVITVTHSI 206
Cdd:TIGR00957 776 YSNADIYLFDDPLSAVDAHVgKHIFEHVIGPEGVLKNKTRILVTHGI 822
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-204 |
1.28e-11 |
|
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: 61.88 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 3 NFFVEVKGIDfawkphLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLS-----GLIrpqGGEVRIGGVKLERP-RPD 76
Cdd:cd03232 10 NYTVPVKGGK------RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILINGRPLDKNfQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 77 SALILQDFGLLPWRTVMENIALglevrsfygpdglHApkrplpeapdalvdyWLKRLGLEavadhypsqisggQRQRTAI 156
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRF-------------SA---------------LLRGLSVE-------------QRKRLTI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490467399 157 GRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTH 204
Cdd:cd03232 120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIH 166
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
36-232 |
1.34e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvkleRP---------RPDSALILQDFGLLPwRTVMENIALG------- 99
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG----RPlsslshsvlRQGVAMVQQDPVVLA-DTFLANVTLGrdiseeq 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 ----LE-------VRSFygPDGLHApkrplpeapdalvdywlkRLGLEAvadhypSQISGGQRQRTAIGRALVLGPDLLL 168
Cdd:PRK10790 446 vwqaLEtvqlaelARSL--PDGLYT------------------PLGEQG------NNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490467399 169 MDEPFSSLDAPTRESLEElTLKLQAERgLTVITVTH---SIEEAaflgRKILCLghppHREPVVVEG 232
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQ-ALAAVREH-TTLVVIAHrlsTIVEA----DTILVL----HRGQAVEQG 556
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-186 |
1.71e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 63.80 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLpLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIG-GVKLerprpdsALILQDF 84
Cdd:TIGR03719 323 IEAENLTKAFGDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGeTVKL-------AYVDQSR 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 -GLLPWRTVMENIALGL--------EVRS--------FYGPDGlhapkrplpeapdalvdywLKRLGleavadhypsQIS 147
Cdd:TIGR03719 395 dALDPNKTVWEEISGGLdiiklgkrEIPSrayvgrfnFKGSDQ-------------------QKKVG----------QLS 445
|
170 180 190
....*....|....*....|....*....|....*....
gi 1490467399 148 GGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEE 186
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEE 484
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-204 |
1.75e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWkPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV------RIGGVklerPRPDSAL 79
Cdd:PRK15064 320 LEVENLTKGF-DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenaNIGYY----AQDHAYD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFGLLPW----RTVMENIalgLEVRSFYGpdglhapkRPLPEAPDAlvdywLKRlgleavadhyPSQISGGQRQRTA 155
Cdd:PRK15064 395 FENDLTLFDWmsqwRQEGDDE---QAVRGTLG--------RLLFSQDDI-----KKS----------VKVLSGGEKGRML 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490467399 156 IGRALVLGPDLLLMDEPFSSLDAptrESLEELTLKLQAERGlTVITVTH 204
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMALEKYEG-TLIFVSH 493
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-206 |
2.25e-11 |
|
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: 63.26 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVrIGGVKL----ERPRPDSALilqdfgllpwrTVMENIalglevRS 104
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKIsykpQYISPDYDG-----------TVEEFL------RS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 FYGPDglhapkrpLPEApdalvdYW----LKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPT 180
Cdd:COG1245 425 ANTDD--------FGSS------YYkteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 490
|
170 180
....*....|....*....|....*.
gi 1490467399 181 RESLEELTLKLQAERGLTVITVTHSI 206
Cdd:COG1245 491 RLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-206 |
2.25e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV----RIGgVKLERPRPDSALILQDFgllpwrtvmenialglevrs 104
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKIS-YKPQYIKPDYDGTVEDL-------------------- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 fygpdglhapkrpLPEAPDALVDYW-----LKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAP 179
Cdd:PRK13409 421 -------------LRSITDDLGSSYykseiIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
170 180
....*....|....*....|....*..
gi 1490467399 180 TRESLEELTLKLQAERGLTVITVTHSI 206
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDI 514
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-206 |
2.63e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKT-TLLYLLSGLIRPQ----GGEVRIGG--------VKLERPRPDS-ALILQD--FGLLPWRTV 92
Cdd:PRK15134 32 IEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGesllhaseQTLRGVRGNKiAMIFQEpmVSLNPLHTL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 93 MENIAlglEVRSfygpdgLHAPKRPlpEAPDALVDYWLKRLGLEAVADH---YPSQISGGQRQRTAIGRALVLGPDLLLM 169
Cdd:PRK15134 112 EKQLY---EVLS------LHRGMRR--EAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIA 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 1490467399 170 DEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSI 206
Cdd:PRK15134 181 DEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNL 217
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-204 |
3.14e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 62.81 E-value: 3.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS-----ALILQDFGLLPwRTVME 94
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwrsrlAVVSQTPFLFS-DTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 95 NIALGLevrsfygPDglhAPKRPLPEAPD-ALVDYWLKRL--GLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDE 171
Cdd:PRK10789 408 NIALGR-------PD---ATQQEIEHVARlASVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190
....*....|....*....|....*....|....
gi 1490467399 172 PFSSLDAPT-RESLEELTlklQAERGLTVITVTH 204
Cdd:PRK10789 478 ALSAVDGRTeHQILHNLR---QWGEGRTVIISAH 508
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-223 |
3.30e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLS-----GLIrpQGGEVRIGGVKLERPRPDSALILQDFGL-LPWRTVMEnialGLEVR 103
Cdd:TIGR00956 787 KPGTLTALMGASGAGKTTLLNVLAervttGVI--TGGDRLVNGRPLDSSFQRSIGYVQQQDLhLPTSTVRE----SLRFS 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 SFygpdgLHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGG----QRQRTAIGRALVLGPDLLL-MDEPFSSLDA 178
Cdd:TIGR00956 861 AY-----LRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKLLLfLDEPTSGLDS 935
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 179 PTRESLEELTLKLqaergltvitVTHsieeaaflGRKILCLGHPP 223
Cdd:TIGR00956 936 QTAWSICKLMRKL----------ADH--------GQAILCTIHQP 962
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
28-221 |
3.33e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRiggvklerpRPDSALIlqdfGLLPWRTVMEnIALGLEVRSFYg 107
Cdd:PRK09544 26 ELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKLRI----GYVPQKLYLD-TTLPLTVNRFL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 108 pdglhapkRPLPEAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEL 187
Cdd:PRK09544 91 --------RLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDL 162
|
170 180 190
....*....|....*....|....*....|....
gi 1490467399 188 TLKLQAERGLTVITVTHSIEEAAFLGRKILCLGH 221
Cdd:PRK09544 163 IDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-222 |
4.36e-11 |
|
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: 61.23 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGevriggvKLERPrPDsalilqdfgllpWRTVMENIAlGLEVRSFYGP- 108
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLG-------KFDDP-PD------------WDEILDEFR-GSELQNYFTKl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 --DGLHAPKRP-----LPEAPDALV-------------DYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLL 168
Cdd:cd03236 83 leGDVKVIVKPqyvdlIPKAVKGKVgellkkkdergklDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYF 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 169 MDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCL-GHP 222
Cdd:cd03236 163 FDEPSSYLDIKQRLNAARLIREL-AEDDNYVLVVEHDLAVLDYLSDYIHCLyGEP 216
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-208 |
5.36e-11 |
|
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: 59.31 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 31 KGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIggVKLERPRPDSALILQDFGLlpwrtvmenialglevrsfygpdg 110
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIV------------------------ 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 111 lhapkrplpeapdalvdywlkrlgleavaDHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEL--- 187
Cdd:smart00382 55 -----------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
|
170 180
....*....|....*....|...
gi 1490467399 188 --TLKLQAERGLTVITVTHSIEE 208
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKD 128
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
36-210 |
7.22e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.06 E-value: 7.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPR------PDSALILQDFG--LLPWRTVMENIAL-GlevRSFy 106
Cdd:NF033858 31 GLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARhrravcPRIAYMPQGLGknLYPTLSVFENLDFfG---RLF- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 gpdGLHAPKRplpeapDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEE 186
Cdd:NF033858 107 ---GQDAAER------RRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWE 177
|
170 180
....*....|....*....|....*
gi 1490467399 187 LTLKLQAER-GLTVITVTHSIEEAA 210
Cdd:NF033858 178 LIDRIRAERpGMSVLVATAYMEEAE 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-241 |
7.30e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG------VKLERPRPDSALILQDfGLLPWRTVMENI 96
Cdd:PTZ00265 404 LNF--TLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlkdINLKWWRSKIGVVSQD-PLLFSNSIKNNI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 97 ALGL-------EVRSFYGPDG---------------------------------LHAPKRPLPEAPDALVDYWLKRL--- 133
Cdd:PTZ00265 481 KYSLyslkdleALSNYYNEDGndsqenknkrnscrakcagdlndmsnttdsnelIEMRKNYQTIKDSEVVDVSKKVLihd 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 134 GLEAVADHY-------PSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSI 206
Cdd:PTZ00265 561 FVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
250 260 270
....*....|....*....|....*....|....*..
gi 1490467399 207 EEAAFlGRKILCLGHPP--HREPVVVEGPPPKRDHPD 241
Cdd:PTZ00265 641 STIRY-ANTIFVLSNRErgSTVDVDIIGEDPTKDNKE 676
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
28-209 |
1.20e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 59.89 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERpRPDSALILQDFGLLP-------WRTVMENIALGl 100
Cdd:PRK11614 27 HINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-WQTAKIMREAVAIVPegrrvfsRMTVEENLAMG- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 evrsfygpdGLHAPKrplpeapdalvDYWLKRLglEAVADHYP----------SQISGGQRQRTAIGRALVLGPDLLLMD 170
Cdd:PRK11614 105 ---------GFFAER-----------DQFQERI--KWVYELFPrlherriqraGTMSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1490467399 171 EPFSSLdAP-----TRESLEELTlklqaERGLTVITVTHSIEEA 209
Cdd:PRK11614 163 EPSLGL-APiiiqqIFDTIEQLR-----EQGMTIFLVEQNANQA 200
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-206 |
1.57e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.57e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 142 YPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHSI 206
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-204 |
1.58e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 37 IIGPSGCGKTTLLYLLSGLIRPQGGEVRIG-GVKLerprpdsALILQDFGLLPWRTVMENIALGL-----------EVRS 104
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV-------GYLPQEPQLDPEKTVRENVEEGVaevkaaldrfnEIYA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 FYGpdglhapkrplpeAPDALVDYWLKRLG-LEAVADHY------------------P------SQISGGQRQRTAIGRA 159
Cdd:PRK11819 111 AYA-------------EPDADFDALAAEQGeLQEIIDAAdawdldsqleiamdalrcPpwdakvTKLSGGERRRVALCRL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 160 LVLGPDLLLMDEPFSSLDAptrESLEELTLKLQAERGlTVITVTH 204
Cdd:PRK11819 178 LLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPG-TVVAVTH 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-210 |
1.72e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 27 WHLKKGESWAIIGPSGCGKTTLLYLLSGLI----RPQGGEVRIGGVKLERPRP---------DSALILQD--FGLLPWRT 91
Cdd:PRK11022 28 YSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEkerrnlvgaEVAMIFQDpmTSLNPCYT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 92 VMENIALGLEVRSfygpDGLHAPKRplpeapDALVDYwLKRLGLEAVA---DHYPSQISGGQRQRTAIGRALVLGPDLLL 168
Cdd:PRK11022 108 VGFQIMEAIKVHQ----GGNKKTRR------QRAIDL-LNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1490467399 169 MDEPFSSLDAPTRESLEELTLKLQAERGLTVITVTHS---IEEAA 210
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlalVAEAA 221
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
36-206 |
2.25e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPR--------PDSALILQDFGLLPWRTVMeniaLGLevrsfYG 107
Cdd:PRK15056 37 ALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALqknlvayvPQSEEVDWSFPVLVEDVVM----MGR-----YG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 108 PDGLHapKRPLPEaPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEEL 187
Cdd:PRK15056 108 HMGWL--RRAKKR-DRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISL 184
|
170
....*....|....*....
gi 1490467399 188 TLKLQAErGLTVITVTHSI 206
Cdd:PRK15056 185 LRELRDE-GKTMLVSTHNL 202
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
28-202 |
2.62e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV-----RIGGVKLER---------PRPDSALI---LQDFGllpwR 90
Cdd:PRK10938 25 TLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfsHITRLSFEQlqklvsdewQRNNTDMLspgEDDTG----R 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 91 TVMENIAlglevrsfygpDGLHAPKRPLPEApdalvdywlKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMD 170
Cdd:PRK10938 101 TTAEIIQ-----------DEVKDPARCEQLA---------QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILD 160
|
170 180 190
....*....|....*....|....*....|..
gi 1490467399 171 EPFSSLDAPTRESLEELTLKLQAErGLTVITV 202
Cdd:PRK10938 161 EPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
37-186 |
2.67e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 37 IIGPSGCGKTTLLYLLSGLIRPQGGEVRIG-GVKLerprpdsALILQ--DfGLLPWRTVMENIALGL--------EVRS- 104
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSGTIKIGeTVKL-------AYVDQsrD-ALDPNKTVWEEISGGLdiikvgnrEIPSr 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 -------FYGPDGlhapkrplpeapdalvdywLKRLGleavadhypsQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:PRK11819 427 ayvgrfnFKGGDQ-------------------QKKVG----------VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
....*....
gi 1490467399 178 APTRESLEE 186
Cdd:PRK11819 478 VETLRALEE 486
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-204 |
2.68e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIrPQGGEVRIGG--------VKLERPRpdsALILQDFGLLPWRTVMENIALglevr 103
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGqpleawsaAELARHR---AYLSQQQTPPFAMPVFQYLTL----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 104 sfYGPDGLHapkrplPEAPDALVDYWLKRLGLEAVADHYPSQISGG--QRQRTA-----IGRALVLGPDLLLMDEPFSSL 176
Cdd:PRK03695 93 --HQPDKTR------TEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAavvlqVWPDINPAGQLLLLDEPMNSL 164
|
170 180
....*....|....*....|....*...
gi 1490467399 177 DAPTRESLEELtLKLQAERGLTVITVTH 204
Cdd:PRK03695 165 DVAQQAALDRL-LSELCQQGIAVVMSSH 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
29-204 |
5.23e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.41 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVriggvklERPrPD--------SALILQDFgllpwrtvMENIALGl 100
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-------DEE-PSwdevlkrfRGTELQDY--------FKKLANG- 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSFYGP---DGLhaPK------RPLPEAPD--ALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLM 169
Cdd:COG1245 159 EIKVAHKPqyvDLI--PKvfkgtvRELLEKVDerGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190
....*....|....*....|....*....|....*
gi 1490467399 170 DEPFSSLDAPTRESLEELTLKLqAERGLTVITVTH 204
Cdd:COG1245 237 DEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEH 270
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-204 |
6.91e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRiggvklERPRPDSAL------ILQDFgllpwrtvMENIALGlEV 102
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE------EEPSWDEVLkrfrgtELQNY--------FKKLYNG-EI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 RSFYGPDGLHA-PK------RPLPEAPD--ALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPF 173
Cdd:PRK13409 161 KVVHKPQYVDLiPKvfkgkvRELLKKVDerGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 174 SSLDAPTRESLEELTLKLQAERglTVITVTH 204
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEGK--YVLVVEH 269
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-204 |
8.02e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 8.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRI-GGVKLERprpdsalILQDfgllPWR----TVME 94
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeQDLIVAR-------LQQD----PPRnvegTVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 95 NIALGLEVRSFYGPDgLHAPKRPLPEAPD-----------ALVDY---W---------LKRLGLEAvaDHYPSQISGGQR 151
Cdd:PRK11147 86 FVAEGIEEQAEYLKR-YHDISHLVETDPSeknlnelaklqEQLDHhnlWqlenrinevLAQLGLDP--DAALSSLSGGWL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 152 QRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAerglTVITVTH 204
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISH 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
30-208 |
1.60e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.49 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGL---------IRPQGGEVRIGGVKlerprpDS-----ALILQDFGLLPWRTVMEN 95
Cdd:NF040905 25 REGEIHALCGENGAGKSTLMKVLSGVyphgsyegeILFDGEVCRFKDIR------DSealgiVIIHQELALIPYLSIAEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 96 IALGLEVRSFygpdGLHAPKRPLPEApDALvdywLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSS 175
Cdd:NF040905 99 IFLGNERAKR----GVIDWNETNRRA-REL----LAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190
....*....|....*....|....*....|...
gi 1490467399 176 LDAPTRESLEELTLKLQAErGLTVITVTHSIEE 208
Cdd:NF040905 170 LNEEDSAALLDLLLELKAQ-GITSIIISHKLNE 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
29-208 |
3.35e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRP-DS-----ALILQ---DFGLLPWRTVMENIALG 99
Cdd:PRK09700 286 VCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAvkkgmAYITEsrrDNGFFPNFSIAQNMAIS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 --LEVRSFYGPDGLHAPKRPLPEAPDALVDYWLKRlgleAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLD 177
Cdd:PRK09700 366 rsLKDGGYKGAMGLFHEVDEQRTAENQRELLALKC----HSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGID 441
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 178 APTRESLEELTLKLqAERGLTVITVTHSIEE 208
Cdd:PRK09700 442 VGAKAEIYKVMRQL-ADDGKVILMVSSELPE 471
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-208 |
4.23e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAL------ILQDFGLLPWRTVMENIALGLev 102
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALengismVHQELNLVLQRSVMDNMWLGR-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsfYGPDGLHAPKRPLPEAPDALVDywlkRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRE 182
Cdd:PRK10982 99 ---YPTKGMFVDQDKMYRDTKAIFD----ELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180
....*....|....*....|....*.
gi 1490467399 183 SLEELTLKLQaERGLTVITVTHSIEE 208
Cdd:PRK10982 172 HLFTIIRKLK-ERGCGIVYISHKMEE 196
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
10-180 |
5.31e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.39 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 10 GIDFAWKPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQ---GGEVRIGGVKLER--PRPDSALILQDF 84
Cdd:PLN03140 169 GINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEfvPRKTSAYISQND 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 85 GLLPWRTVMENIAL-----GLEVRSfygpDGLHAPKRPLPEA---PDALV------------------DYWLKRLGLE-- 136
Cdd:PLN03140 249 VHVGVMTVKETLDFsarcqGVGTRY----DLLSELARREKDAgifPEAEVdlfmkatamegvksslitDYTLKILGLDic 324
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490467399 137 ---AVADHYPSQISGGQRQRTAIGRALVlGP-DLLLMDEPFSSLDAPT 180
Cdd:PLN03140 325 kdtIVGDEMIRGISGGQKKRVTTGEMIV-GPtKTLFMDEISTGLDSST 371
|
|
| cyc_pep_trnsptr |
TIGR01194 |
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ... |
29-204 |
9.04e-09 |
|
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]
Pssm-ID: 130262 [Multi-domain] Cd Length: 555 Bit Score: 55.35 E-value: 9.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvklerpRPDSALILQDFGLLpWRTVMENialglevrsFYGP 108
Cdd:TIGR01194 365 IAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDG------AAVSADSRDDYRDL-FSAIFAD---------FHLF 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 DGLHAPKRPLPEAPDALVDYwLKRLGLE---AVAD---HYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRE 182
Cdd:TIGR01194 429 DDLIGPDEGEHASLDNAQQY-LQRLEIAdkvKIEDggfSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKR 507
|
170 180
....*....|....*....|..
gi 1490467399 183 SLEELTLKLQAERGLTVITVTH 204
Cdd:TIGR01194 508 FFYEELLPDLKRQGKTIIIISH 529
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
17-220 |
9.31e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.60 E-value: 9.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 17 PHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQ-GGEVRIGGVKLERPRPDSA------LILQD---FGL 86
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAiragiaMVPEDrkrHGI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 87 LPWRTVMENIALGLeVRSFYGPDGLHApkrplpEAPDALVDYWLKRLGLEAVADHYP-SQISGGQRQRTAIGRALVLGPD 165
Cdd:TIGR02633 351 VPILGVGKNITLSV-LKSFCFKMRIDA------AAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPR 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 166 LLLMDEPFSSLDAPTRESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCLG 220
Cdd:TIGR02633 424 VLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVLGLSDRVLVIG 477
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
6-217 |
1.77e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAW--KPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRP-QGGEVRIGGVKLERPRpdsalilq 82
Cdd:PLN03232 615 ISIKNGYFSWdsKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGSVAYVPQ-------- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 83 dfglLPW---RTVMENIALG--LEVRSFYGPDGLHAPKRPLpeapDALVDYWLKRLGLEAVadhypsQISGGQRQRTAIG 157
Cdd:PLN03232 687 ----VSWifnATVRENILFGsdFESERYWRAIDVTALQHDL----DLLPGRDLTEIGERGV------NISGGQKQRVSMA 752
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDAPTRESLEELTLKlQAERGLTVITVTHSIEEAAFLGRKIL 217
Cdd:PLN03232 753 RAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIIL 811
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
30-202 |
2.10e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 30 KKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAL---IL-------QDfGLLPWRTVMENIALG 99
Cdd:PRK11288 277 RAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIragIMlcpedrkAE-GIIPVHSVADNINIS 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 100 leVRSFYGPDGLHAPKRPlpEAPDAlvDYWLKRLGLEAVADHYP-SQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:PRK11288 356 --ARRHHLRAGCLINNRW--EAENA--DRFIRSLNIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
170 180
....*....|....*....|....
gi 1490467399 179 PTRESLEELTLKLqAERGLTVITV 202
Cdd:PRK11288 430 GAKHEIYNVIYEL-AAQGVAVLFV 452
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
28-204 |
2.46e-08 |
|
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: 52.53 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGL--IRPQGGEVRIGGvklerprpdsalilQDFGLLPwrtVMENIALGLEVrsf 105
Cdd:cd03217 22 TIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKG--------------EDITDLP---PEERARLGIFL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 106 ygpdglhAPKRPlPEAPDALVDYWLKRL--GLeavadhypsqiSGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRES 183
Cdd:cd03217 82 -------AFQYP-PEIPGVKNADFLRYVneGF-----------SGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180
....*....|....*....|.
gi 1490467399 184 LEELTLKLqAERGLTVITVTH 204
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITH 162
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-172 |
6.66e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.72 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 8 VKGIDFawkphlplflnfwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDS------ALIL 81
Cdd:COG3845 274 LKDVSL--------------EVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErrrlgvAYIP 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 82 QD---FGLLPWRTVMENIALGLEVRSFYGPDGLHAPKRPLPEAPDALVDYWLKRLGLEAVAdhypSQISGGQRQRTAIGR 158
Cdd:COG3845 340 EDrlgRGLVPDMSVAENLILGRYRRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTPA----RSLSGGNQQKVILAR 415
|
170
....*....|....
gi 1490467399 159 ALVLGPDLLLMDEP 172
Cdd:COG3845 416 ELSRDPKLLIAAQP 429
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
54-216 |
9.35e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 9.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 54 GLIRPQGGEVRIGGVKLERPRPDSalilqdfGLLPWR---------TVMENIALGLEVR-----SFYGPDGLHAPKRPLP 119
Cdd:NF000106 43 GVLGP*GAA**RGALPAHV*GPDA-------GRRPWRf*twcanrrALRRTIG*HRPVR*grreSFSGRENLYMIGR*LD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 120 ---EAPDALVDYWLKRLGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEElTLKLQAERG 196
Cdd:NF000106 116 lsrKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWD-EVRSMVRDG 194
|
170 180
....*....|....*....|
gi 1490467399 197 LTVITVTHSIEEAAFLGRKI 216
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHEL 214
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
28-206 |
1.66e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. 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: 213255 [Multi-domain] Cd Length: 257 Bit Score: 51.06 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVK-----LERPRPDSALILQD---------FGLLPWRTVM 93
Cdd:cd03288 43 YIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDisklpLHTLRSRLSIILQDpilfsgsirFNLDPECKCT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 94 EN-IALGLEVRSfygpdgLHAPKRPLPEapdalvdywlkrlGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEP 172
Cdd:cd03288 123 DDrLWEALEIAQ------LKNMVKSLPG-------------GLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190
....*....|....*....|....*....|....
gi 1490467399 173 FSSLDAPTRESLEELTLKLQAERglTVITVTHSI 206
Cdd:cd03288 184 TASIDMATENILQKVVMTAFADR--TVVTIAHRV 215
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
23-204 |
2.98e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.90 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 23 LNFwwHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGevriggvKLERPRPdsalilQDFGLLPWRTVMENIALGLEV 102
Cdd:TIGR00954 471 LSF--EVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG-------RLTKPAK------GKLFYVPQRPYMTLGTLRDQI 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsFYgPDGLHAPKR------PLPEAPDAL-VDYWLKR-LGLEAVADhYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:TIGR00954 536 --IY-PDSSEDMKRrglsdkDLEQILDNVqLTHILEReGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
|
170 180 190
....*....|....*....|....*....|..
gi 1490467399 175 --SLDaptresLEELTLKLQAERGLTVITVTH 204
Cdd:TIGR00954 612 avSVD------VEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-205 |
4.32e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 37 IIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLER-PRPDSALILQDFGLLPWRTVMENIALGLEvrsFYGPdglhapk 115
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiAKPYCTYIGHNLGLKLEMTVFENLKFWSE---IYNS------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 116 rplPEAPDALVDYWlkrlGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLkLQAER 195
Cdd:PRK13541 101 ---AETLYAAIHYF----KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIV-MKANS 172
|
170
....*....|
gi 1490467399 196 GLTVITVTHS 205
Cdd:PRK13541 173 GGIVLLSSHL 182
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-184 |
5.64e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 21 LFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGevriggvklerprpdsalilqdfgllpwrTVMENIALGL 100
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG-----------------------------TVFRSAKVRM 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSFYGPDGLHAPKRPL-------PEAPDALVDYWLKRLGLE---AVADHYpsQISGGQRQRTAIGRALVLGPDLLLMD 170
Cdd:PLN03073 575 AVFSQHHVDGLDLSSNPLlymmrcfPGVPEQKLRAHLGSFGVTgnlALQPMY--TLSGGQKSRVAFAKITFKKPHILLLD 652
|
170
....*....|....
gi 1490467399 171 EPFSSLDAPTRESL 184
Cdd:PLN03073 653 EPSNHLDLDAVEAL 666
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
145-207 |
1.39e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.09 E-value: 1.39e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 145 QISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAerglTVITVTHSIE 207
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHARE 402
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
6-210 |
3.50e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 47.85 E-value: 3.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAWKPHLPLFLN-FWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVR-----IGGVKLERPRPDSAL 79
Cdd:PTZ00243 1309 LVFEGVQMRYREGLPLVLRgVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRvngreIGAYGLRELRRQFSM 1388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 80 ILQDFGLLPwRTVMENIalglevrsfygpdglhapkRPLPEAPDALVDYWLKRLGL-EAVADHYP----------SQISG 148
Cdd:PTZ00243 1389 IPQDPVLFD-GTVRQNV-------------------DPFLEASSAEVWAALELVGLrERVASESEgidsrvleggSNYSV 1448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490467399 149 GQRQRTAIGRALV-LGPDLLLMDEPFSSLDaPTRESLEELTLkLQAERGLTVITVTHSIEEAA 210
Cdd:PTZ00243 1449 GQRQLMCMARALLkKGSGFILMDEATANID-PALDRQIQATV-MSAFSAYTVITIAHRLHTVA 1509
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
36-178 |
4.12e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.53 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 36 AIIGPSGCGKTTLLYLLSGliRPQGG----EVRIGGV--KLERPRPDSALILQDFGLLPWRTVMENialgLEVRSFygpd 109
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGGyiegDIRISGFpkKQETFARISGYCEQNDIHSPQVTVRES----LIYSAF---- 979
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 110 gLHAPKRPLPEAPDALVDYWLKRLGLEAVADH---YP--SQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDA 178
Cdd:PLN03140 980 -LRLPKEVSKEEKMMFVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-221 |
5.12e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.19 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 24 NFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGvklerprpDSALILQDFGLLPWRTVMENIAL-GLEV 102
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG--------SAALIAISSGLNGQLTGIENIELkGLMM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 rsfygpdGLhaPKRPLPEAPDALVDYwlkrlgleavAD-----HYPSQI-SGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:PRK13545 114 -------GL--TKEKIKEIIPEIIEF----------ADigkfiYQPVKTySSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1490467399 177 DAP-TRESLEELT-LKlqaERGLTVITVTHSIEEAAFLGRKILCL--GH 221
Cdd:PRK13545 175 DQTfTKKCLDKMNeFK---EQGKTIFFISHSLSQVKSFCTKALWLhyGQ 220
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-180 |
6.38e-06 |
|
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: 45.72 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 16 KPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQG---GEVRIGGVKL----ERPRPDSALILQDFGLLP 88
Cdd:cd03233 17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYkefaEKYPGEIIYVSEEDVHFP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 89 WRTVMENIALGLEVRsfygpdglhapkrplpeapdalvdywlkrlgleavADHYPSQISGGQRQRTAIGRALVLGPDLLL 168
Cdd:cd03233 97 TLTVRETLDFALRCK-----------------------------------GNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170
....*....|..
gi 1490467399 169 MDEPFSSLDAPT 180
Cdd:cd03233 142 WDNSTRGLDSST 153
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
6-178 |
6.98e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 6.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 6 VEVKGIDFAW--KPHLPLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRP-QGGEVRIGGVKLERPRpdsalilq 82
Cdd:PLN03130 615 ISIKNGYFSWdsKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAYVPQ-------- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 83 dfglLPW---RTVMENIALGLEVRS--FYGPDGLHAPKRPLpeapDALVDYWLKRLGLEAVadhypsQISGGQRQRTAIG 157
Cdd:PLN03130 687 ----VSWifnATVRDNILFGSPFDPerYERAIDVTALQHDL----DLLPGGDLTEIGERGV------NISGGQKQRVSMA 752
|
170 180
....*....|....*....|.
gi 1490467399 158 RALVLGPDLLLMDEPFSSLDA 178
Cdd:PLN03130 753 RAVYSNSDVYIFDDPLSALDA 773
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-204 |
8.74e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.42 E-value: 8.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 20 PLFLNFWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIG-GVKLERPRPDS----------ALILQDFGLlp 88
Cdd:PRK15064 15 PLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQfafeeftvldTVIMGHTEL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 89 WRTVMENIAL---------------GLEVRsFYGPDGLHAPKRplpeAPDALvdywlkrLGLE-AVADHYP--SQISGGQ 150
Cdd:PRK15064 93 WEVKQERDRIyalpemseedgmkvaDLEVK-FAEMDGYTAEAR----AGELL-------LGVGiPEEQHYGlmSEVAPGW 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1490467399 151 RQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEElTLKlqaERGLTVITVTH 204
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLED-VLN---ERNSTMIIISH 210
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
29-208 |
8.99e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 8.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAL------ILQDF---GLLPWRTVMENIAL- 98
Cdd:PRK10762 275 LRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLangivyISEDRkrdGLVLGMSVKENMSLt 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 99 GLEVRSFYGPDGLHAPKRplpeapdalvdywlkrlglEAVADHY-------PSQ------ISGGQRQRTAIGRALVLGPD 165
Cdd:PRK10762 355 ALRYFSRAGGSLKHADEQ-------------------QAVSDFIrlfniktPSMeqaiglLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1490467399 166 LLLMDEPFSSLDAPTRESLEELTLKLQAErGLTVITVTHSIEE 208
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPE 457
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
29-236 |
9.10e-06 |
|
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: 44.87 E-value: 9.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGevriggvKLERPRpdsalilqdfgllpwrtvmenialgleVRSFYGP 108
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-------NDEWDG---------------------------ITPVYKP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 109 DGLhapkrplpeapdalvdywlkrlgleavadhypsQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELT 188
Cdd:cd03222 68 QYI---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAI 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490467399 189 LKLQAERGLTVITVTHSIEEAAFLGRKIlclghpphrepVVVEGPPPK 236
Cdd:cd03222 115 RRLSEEGKKTALVVEHDLAVLDYLSDRI-----------HVFEGEPGV 151
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-200 |
9.38e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 9.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 15 WKPHLPLFLN-FWWHLKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERprpdsalilqdFGLLPWRTVM 93
Cdd:PLN03232 1244 YRPGLPPVLHgLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK-----------FGLTDLRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 94 ENIALGLEVrsFYGPDGLHAPkrPLPEAPDAlvDYW--LKRLGLEAVADHYP-----------SQISGGQRQRTAIGRAL 160
Cdd:PLN03232 1313 SIIPQSPVL--FSGTVRFNID--PFSEHNDA--DLWeaLERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARAL 1386
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1490467399 161 VLGPDLLLMDEPFSSLDAPT--------RESLEELTLKLQAERGLTVI 200
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTdsliqrtiREEFKSCTMLVIAHRLNTII 1434
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
29-220 |
1.21e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.08 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIrpQG---GEVRIGG--VKLERPRpDS-----ALILQD---FGLLPWRTVMEN 95
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLFGAY--PGrweGEIFIDGkpVKIRNPQ-QAiaqgiAMVPEDrkrDGIVPVMGVGKN 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 96 IALGLeVRSFYGPDGLHApkrplpEAPDALVDYWLKRLGLEAVADHYP-SQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:PRK13549 362 ITLAA-LDRFTGGSRIDD------AAELKTILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1490467399 175 SLDAPTRESLEELTLKLqAERGLTVITVTHSIEEAAFLGRKILCLG 220
Cdd:PRK13549 435 GIDVGAKYEIYKLINQL-VQQGVAIIVISSELPEVLGLSDRVLVMH 479
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-207 |
3.19e-05 |
|
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: 44.90 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQGgEVRIGGVKLErprpdsALILQD----FGLLPWRTVMenialglevrsFYG 107
Cdd:TIGR01271 1245 GQRVGLLGRTGSGKSTLLSALLRLLSTEG-EIQIDGVSWN------SVTLQTwrkaFGVIPQKVFI-----------FSG 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 108 PdgLHAPKRPLPEAPDALVDYWLKRLGLEAVADHYPSQI-----------SGGQRQRTAIGRALVLGPDLLLMDEPFSSL 176
Cdd:TIGR01271 1307 T--FRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190
....*....|....*....|....*....|.
gi 1490467399 177 DAPTRESLEElTLKlQAERGLTVITVTHSIE 207
Cdd:TIGR01271 1385 DPVTLQIIRK-TLK-QSFSNCTVILSEHRVE 1413
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
29-180 |
4.43e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 4.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLI----RPQGGEVRIGGVKLE----RPRPDSALILQDFGLLPWRTVMENIALGL 100
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGITPEeikkHYRGDVVYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 101 EVRSFYG-PDGLHAPKRPlpeapDALVDYWLKRLGLE-----AVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:TIGR00956 164 RCKTPQNrPDGVSREEYA-----KHIADVYMATYGLShtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
....*.
gi 1490467399 175 SLDAPT 180
Cdd:TIGR00956 239 GLDSAT 244
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
145-204 |
6.93e-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: 41.96 E-value: 6.93e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490467399 145 QISGGQRQRTAIgrALVLG------PDLLLMDEPFSSLDAPTRESLEELtLKLQAERGLTVITVTH 204
Cdd:cd03227 77 QLSGGEKELSAL--ALILAlaslkpRPLYILDEIDRGLDPRDGQALAEA-ILEHLVKGAQVIVITH 139
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-177 |
1.05e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 32 GESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGG------VKLERPRPD-SALILQDFGLLPWRTVMENIALGLEVRS 104
Cdd:PRK10636 27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawVNQETPALPqPALEYVIDGDREYRQLEAQLHDANERND 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 105 FYGPDGLHAPKrplpeapDAlVDYW---------LKRLGLEAVADHYP-SQISGGQRQRTAIGRALVLGPDLLLMDEPFS 174
Cdd:PRK10636 107 GHAIATIHGKL-------DA-IDAWtirsraaslLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDEPTN 178
|
...
gi 1490467399 175 SLD 177
Cdd:PRK10636 179 HLD 181
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
147-204 |
1.58e-04 |
|
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: 41.44 E-value: 1.58e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490467399 147 SGGQRQ------RTAIGRALVLGPDLLLMDEPFSSLDAPTRE-SLEELTLKLQAERGLTVITVTH 204
Cdd:cd03240 117 SGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLAEIIEERKSQKNFQLIVITH 181
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
31-206 |
2.37e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 31 KGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEV----RIGGVklerprPDSALILQdfgllpwRTVMENIALGLEVRSFY 106
Cdd:PTZ00243 685 RGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSIAYV------PQQAWIMN-------ATVRGNILFFDEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 107 GPDG-----LHAPKRPLPEapdalvdywlkrlGLEAVADHYPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTR 181
Cdd:PTZ00243 752 LADAvrvsqLEADLAQLGG-------------GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVG 818
|
170 180
....*....|....*....|....*
gi 1490467399 182 ESLEELTLkLQAERGLTVITVTHSI 206
Cdd:PTZ00243 819 ERVVEECF-LGALAGKTRVLATHQV 842
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
29-201 |
2.67e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 29 LKKGESWAIIGPSGCGKTTLLYLLSGLIRPQGGEVRIGGVKLERPRPDSAlILQDFGLLPWRTVMENIALGLEV------ 102
Cdd:PRK10982 271 LHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEA-INHGFALVTEERRSTGIYAYLDIgfnsli 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 103 ---RSFYGPDGLHAPKRPLPEAPdalvdyWLkrlgLEAVADHYPSQ------ISGGQRQRTAIGRALVLGPDLLLMDEPF 173
Cdd:PRK10982 350 sniRNYKNKVGLLDNSRMKSDTQ------WV----IDSMRVKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180
....*....|....*....|....*....
gi 1490467399 174 SSLDAPTRESLEELTLKL-QAERGLTVIT 201
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELaKKDKGIIIIS 448
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
129-216 |
4.63e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 129 WLKRLGLE-----AVADH------YPSQISGGQRQRTAIGRALVLGPDLLLMDEPFSSLDAPTRESLEELTLKLQAERGL 197
Cdd:PRK15093 131 WRKRRAIEllhrvGIKDHkdamrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNT 210
|
90
....*....|....*....
gi 1490467399 198 TVITVTHSIEEAAFLGRKI 216
Cdd:PRK15093 211 TILLISHDLQMLSQWADKI 229
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
28-232 |
9.44e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 38.84 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 28 HLKKGESWAIIGPSGCGKTTLLylLSGLirPQGGEVRIGGVkLERPRPDSALILQDFGLLpwrtvmenIALGLEvrsfYG 107
Cdd:cd03238 17 SIPLNVLVVVTGVSGSGKSTLV--NEGL--YASGKARLISF-LPKFSRNKLIFIDQLQFL--------IDVGLG----YL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 108 PDGlhapkRPLpeapdalvdywlkrlgleavadhypSQISGGQRQRTAIGRALV--LGPDLLLMDEPFSSLDAPTRESLE 185
Cdd:cd03238 80 TLG-----QKL-------------------------STLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1490467399 186 ElTLKLQAERGLTVITVTHS---IEEAAFlgrkILCLGHPP--HREPVVVEG 232
Cdd:cd03238 130 E-VIKGLIDLGNTVILIEHNldvLSSADW----IIDFGPGSgkSGGKVVFSG 176
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
144-216 |
4.06e-03 |
|
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: 37.63 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490467399 144 SQISGGQRQRTAIGRALVLGP----------DLLLMDEPFSSLDAPTRESLEELtLKLQAERGLTVITVTHSIEEAAFLG 213
Cdd:cd03279 122 STLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGFGTLDPEALEAVATA-LELIRTENRMVGVISHVEELKERIP 200
|
...
gi 1490467399 214 RKI 216
Cdd:cd03279 201 QRL 203
|
|
| VirB4 |
COG3451 |
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and ... |
20-65 |
8.76e-03 |
|
Type IV secretory pathway, VirB4 component [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 442674 [Multi-domain] Cd Length: 546 Bit Score: 37.23 E-value: 8.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1490467399 20 PLFLNFWWHLKKGeSWAIIGPSGCGKTTLL-YLLSGLIRpQGGEVRI 65
Cdd:COG3451 193 PVFFDFHDGLDNG-NTLILGPSGSGKSFLLkLLLLQLLR-YGARIVI 237
|
|
| |
