|
Name |
Accession |
Description |
Interval |
E-value |
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-224 |
1.41e-84 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 252.32 E-value: 1.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 1 MS-SGPRLEIDVEGKKFDFL--PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG-VVAAEAP 76
Cdd:COG1116 1 MSaAAPALELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 77 PAGFVFQDPRLLPWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLL 150
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNValglelRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534501033 151 LLDEPFVSLD---RTlvvEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSGRPAKIVADYRFASAagqRPR 224
Cdd:COG1116 161 LMDEPFGALDaltRE---RLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSARPGRIVEEIDVDLP---RPR 231
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
20-214 |
6.60e-79 |
|
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: 236.60 E-value: 6.60e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-GFVFQDPRLLPWLTALDNI- 97
Cdd:cd03293 16 AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDrGYVFQQDALLPWLTVLDNVa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 -----RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLL 172
Cdd:cd03293 96 lglelQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 173 TLIETNRPTVLLVTHLPEDAATVADRAVVLSGRPAKIVADYR 214
Cdd:cd03293 176 DIWRETGKTVLLVTHDIDEAVFLADRVVVLSARPGRIVAEVE 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-203 |
5.73e-62 |
|
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: 193.12 E-value: 5.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 7 LEIDVEGKKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVF 82
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPErrniGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 QDPRLLPWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:cd03259 79 QDYALFPHLTVAENIafglklRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2534501033 157 VSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS 203
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMN 205
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-205 |
2.85e-59 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 190.69 E-value: 2.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 3 SGPRLEIDVEGKKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---- 78
Cdd:COG3842 2 AMPALELENVSKRYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEkrnv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 GFVFQDPRLLPWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVafglrmRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 153 DEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS-GR 205
Cdd:COG3842 160 DEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNdGR 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
20-203 |
4.69e-56 |
|
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: 178.45 E-value: 4.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----------GFVFQDPRLLP 89
Cdd:cd03255 16 KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafrrrhiGFVFQSFNLLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 WLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL 163
Cdd:cd03255 96 DLTALENVelplllAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSET 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534501033 164 VVEMEQVLLTLIETNRPTVLLVTHLPEDAATvADRAVVLS 203
Cdd:cd03255 176 GKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELR 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
8-205 |
5.05e-55 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 179.57 E-value: 5.05e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 8 EIDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVF 82
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPrerrvGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 QDPRLLPWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:COG1118 82 QHYALFPHMTVAENIafglrvRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 157 VSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS-GR 205
Cdd:COG1118 162 GALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNqGR 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
20-241 |
2.85e-54 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 175.05 E-value: 2.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVvAAEAPPA--GFVFQDPRLLPWLTALDNI 97
Cdd:COG4525 19 PQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV-PVTGPGAdrGVVFQKDALLPWLNVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 ------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVL 171
Cdd:COG4525 98 afglrlRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 172 LTLIETNRPTVLLVTHLPEDAATVADRAVVLSGRPAKIVADYR--FAS--AAGQRPRA---------EREHIANQIAGAA 238
Cdd:COG4525 178 LDVWQRTGKGVFLITHSVEEALFLATRLVVMSPGPGRIVERLEldFSRrfLAGEDARAiksdpafiaLREELLDIIFAQE 257
|
...
gi 2534501033 239 AER 241
Cdd:COG4525 258 EAE 260
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
20-214 |
5.78e-54 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 173.31 E-value: 5.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----------GFVFQDPRLLP 89
Cdd:COG1136 20 EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERelarlrrrhiGFVFQFFNLLP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 WLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL 163
Cdd:COG1136 100 ELTALENValplllAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 164 VVEMEQVLLTLIETNRPTVLLVTHLPEdAATVADRAVVLS-GRpakIVADYR 214
Cdd:COG1136 180 GEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRdGR---IVSDER 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
9-212 |
3.03e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.38 E-value: 3.03e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEG--KKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFV 81
Cdd:COG1131 1 IEVRGltKRYG--DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEvrrriGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 82 FQDPRLLPWLTALDNIR------AVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:COG1131 79 PQEPALYPDLTVRENLRffarlyGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534501033 156 FVSLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLS-GRpakIVAD 212
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAIIDkGR---IVAD 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-211 |
7.12e-49 |
|
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: 160.36 E-value: 7.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------G 79
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrlrrrmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 80 FVFQDPRLLPWLTALDNIrAV--RPETTESEAE----AM--LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLL 151
Cdd:cd03261 81 MLFQSGALFDSLTVFENV-AFplREHTRLSEEEireiVLekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 152 LDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSGRpaKIVA 211
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDG--KIVA 217
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
21-215 |
7.00e-48 |
|
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: 157.88 E-value: 7.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPR---LLPwl 91
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRelrrkvGLVFQNPDdqlFAP-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVV 165
Cdd:COG1122 92 TVEEDVafgpenLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2534501033 166 EMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLS-------GRPAKIVADYRF 215
Cdd:COG1122 172 ELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDdgrivadGTPREVFSDYEL 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
9-209 |
1.41e-47 |
|
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: 157.01 E-value: 1.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQD 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHkrpvNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 85 PRLLPWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVS 158
Cdd:cd03300 81 YALFPHLTVFENIafglrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534501033 159 LDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS-------GRPAKI 209
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNkgkiqqiGTPEEI 218
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-202 |
2.42e-47 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 156.45 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 27 FRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQDPRLLPWLTALDNIR-AVR 101
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAerpvSMLFQENNLFPHLTVAQNIGlGLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 102 P-----ETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFsVNPR-LLLLDEPFVSLDRTLVVEMEQVLLTLI 175
Cdd:COG3840 98 PglkltAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCL-VRKRpILLLDEPFSALDPALRQEMLDLVDELC 176
|
170 180
....*....|....*....|....*..
gi 2534501033 176 ETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:COG3840 177 RERGLTVLMVTHDPEDAARIADRVLLV 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
9-202 |
1.53e-46 |
|
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: 152.55 E-value: 1.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEG--KKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFV 81
Cdd:cd03230 1 IEVRNlsKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEvkrriGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 82 FQDPRLLPWLTALDNIRavrpetteseaeamlmrvglkgferyypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDR 161
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDP 128
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2534501033 162 TLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03230 129 ESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAIL 168
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
9-212 |
1.84e-46 |
|
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: 154.37 E-value: 1.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------G 79
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyelrrriG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 80 FVFQDPRLLPWLTALDNIrAV----RPETTESEAEAM----LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLL 151
Cdd:COG1127 86 MLFQGGALFDSLTVFENV-AFplreHTDLSEAEIRELvlekLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 152 LDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTH-LPEdAATVADRAVVLSGRpaKIVAD 212
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHdLDS-AFAIADRVAVLADG--KIIAE 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
9-209 |
1.90e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 154.38 E-value: 1.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEG--KKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-------- 78
Cdd:COG1126 2 IEIENlhKSFG--DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinklrrkv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 GFVFQDPRLLPWLTALDNI-------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLL 151
Cdd:COG1126 80 GMVFQQFNLFPHLTVLENVtlapikvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 152 LDEPFVSLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVL-------SGRPAKI 209
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLAKEGM-TMVVVTHEMGFAREVADRVVFMdggriveEGPPEEF 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
24-204 |
4.42e-45 |
|
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: 149.99 E-value: 4.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA--------GFVFQDPRLLPWLTALD 95
Cdd:cd03262 16 LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinelrqkvGMVFQQFNLFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NI-------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:cd03262 96 NItlapikvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534501033 169 QVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:cd03262 176 DVMKDLAEEGM-TMVVVTHEMGFAREVADRVIFMDD 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-203 |
8.23e-45 |
|
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: 150.18 E-value: 8.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 7 LEIDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP----AGFVF 82
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVqernVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 QDPRLLPWLTALDNI--------RAVRPETTESEAEAM--LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:cd03296 81 QHYALFRHMTVFDNVafglrvkpRSERPPEAEIRAKVHelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 153 DEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS 203
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMN 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-207 |
1.17e-44 |
|
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: 149.54 E-value: 1.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG-VVAAEAPPAGFVFQDPRLLPWLTALDNI----R 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkQITEPGPDRMVVFQNYSLLPWLTVRENIalavD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 99 AVRPETTESEAEAM----LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTL 174
Cdd:TIGR01184 81 RVLPDLSKSERRAIveehIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI 160
|
170 180 190
....*....|....*....|....*....|...
gi 2534501033 175 IETNRPTVLLVTHLPEDAATVADRAVVLSGRPA 207
Cdd:TIGR01184 161 WEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPA 193
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-203 |
1.93e-44 |
|
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: 148.38 E-value: 1.93e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRL-LPWLTA 93
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKelrrkvGLVFQNPDDqFFGPTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEM 167
Cdd:cd03225 94 EEEVafglenLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRREL 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534501033 168 EQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLS 203
Cdd:cd03225 174 LELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLE 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
9-202 |
5.21e-44 |
|
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: 146.18 E-value: 5.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV--------VAAEAPPAGF 80
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEdltdledeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 81 VFQDPRLLPWLTALDNIRavrpetteseaeamlmrvglkgferyYPheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:cd03229 81 VFQDFALFPHLTVLENIA--------------------------LG--LSGGQQQRVALARALAMDPDVLLLDEPTSALD 132
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 161 RTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03229 133 PITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVL 174
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
8-204 |
8.40e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 150.61 E-value: 8.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 8 EIDVEG--KKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFV 81
Cdd:COG3839 3 SLELENvsKSYG--GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKdrniAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 82 FQDPRLLPWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:COG3839 81 FQSYALYPHMTVYENIafplklRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2534501033 156 FVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:COG3839 161 LSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMND 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
20-202 |
1.08e-43 |
|
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: 146.88 E-value: 1.08e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------GFVFQDPR--LL 88
Cdd:cd03257 17 SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkirrkeiQMVFQDPMssLN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLTALDNI----RAVRPETTESEAEA----MLMRVGL-KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSL 159
Cdd:cd03257 97 PRMTIGEQIaeplRIHGKLSKKEARKEavllLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2534501033 160 DRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03257 177 DVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVM 219
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
21-187 |
2.43e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.97 E-value: 2.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------GFVFQDPRLLPWL 91
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipylrrriGVVFQDFRLLPDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDN------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVV 165
Cdd:COG2884 95 TVYENvalplrVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSW 174
|
170 180
....*....|....*....|....
gi 2534501033 166 EmeqVLLTLIETNRP--TVLLVTH 187
Cdd:COG2884 175 E---IMELLEEINRRgtTVLIATH 195
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
17-225 |
3.19e-43 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 146.77 E-value: 3.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 17 DFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVvAAEAPPA--GFVFQDPRLLPWLTAL 94
Cdd:PRK11248 10 DYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK-PVEGPGAerGVVFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:PRK11248 89 DNVafglqlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 169 QVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSGRPAKIVA----DYRFASAAGQRPRA 225
Cdd:PRK11248 169 TLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVVErlplNFARRFVAGESSRS 229
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-198 |
4.22e-43 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 146.01 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 18 FLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVvAAEAP---------PAGFVFQDPRLL 88
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGL-KVNDPkvderlirqEAGMVFQQFYLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLTALDN-------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDR 161
Cdd:PRK09493 90 PHLTALENvmfgplrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2534501033 162 TLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADR 198
Cdd:PRK09493 170 ELRHEVLKVMQDLAEEGM-TMVIVTHEIGFAEKVASR 205
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-209 |
6.53e-43 |
|
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: 144.36 E-value: 6.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 6 RLEIDVEGKkfdflptplLDGFRLEIE---PSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEA------P 76
Cdd:cd03297 1 MLCVDIEKR---------LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinlP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 77 P----AGFVFQDPRLLPWLTALDNI----RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPR 148
Cdd:cd03297 72 PqqrkIGLVFQQYALFPHLNVRENLafglKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 149 LLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS-GRPAKI 209
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEdGRLQYI 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
9-207 |
9.94e-43 |
|
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: 145.00 E-value: 9.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQ 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREarrqiGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 84 DPRLLPWLTALDNIRA------VRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:COG4555 82 ERGLYDRLTVRENIRYfaelygLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 158 SLD---RTLVVEMeqvLLTLIETNRpTVLLVTHLPEDAATVADRAVVLS-GRPA 207
Cdd:COG4555 162 GLDvmaRRLLREI---LRALKKEGK-TVLFSSHIMQEVEALCDRVVILHkGKVV 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-212 |
2.66e-42 |
|
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: 143.02 E-value: 2.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 27 FRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQDPRLLPWLTALDNI---RA 99
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAdrpvSMLFQENNLFAHLTVEQNVglgLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 100 VRPETTESEAEAM---LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIE 176
Cdd:cd03298 97 PGLKLTAEDRQAIevaLARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534501033 177 TNRPTVLLVTHLPEDAATVADRAVVLSGrpAKIVAD 212
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDN--GRIAAQ 210
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
24-205 |
4.54e-42 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 142.96 E-value: 4.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV----------DGVVAAEAPPAGFVFQDPRLLPWLTA 93
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfaldeDARARLRARHVGFVFQSFQLLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNI-----RAVRPETTEsEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:COG4181 108 LENVmlpleLAGRRDARA-RARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQII 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 2534501033 169 QVLLTLIETNRPTVLLVTHLPEDAATvADRAVVL-SGR 205
Cdd:COG4181 187 DLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLrAGR 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-211 |
1.08e-41 |
|
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: 143.17 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----------GFVFQDPRLLPWLTALDN-- 96
Cdd:cd03294 45 LDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrkkiSMVFQSFALLPHRTVLENva 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 ----IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLL 172
Cdd:cd03294 125 fgleVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELL 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2534501033 173 TLIETNRPTVLLVTHLPEDAATVADR-------AVVLSGRPAKIVA 211
Cdd:cd03294 205 RLQAELQKTIVFITHDLDEALRLGDRiaimkdgRLVQVGTPEEILT 250
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
21-205 |
3.41e-41 |
|
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: 139.92 E-value: 3.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQDPRLLPWLTALD 95
Cdd:COG4133 15 RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDyrrrlAYLGHADGLKPELTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIRAVR----PETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRtlvvEMEQVL 171
Cdd:COG4133 95 NLRFWAalygLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA----AGVALL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 2534501033 172 LTLIET---NRPTVLLVTHLPEDAAtvADRAVVLSGR 205
Cdd:COG4133 171 AELIAAhlaRGGAVLLTTHQPLELA--AARVLDLGDF 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-212 |
6.16e-40 |
|
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: 139.94 E-value: 6.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 39 LVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV----VAAEAPPAGFVFQDPRLLPWLTALDNI------RAVRPETTESE 108
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEdvtnVPPHLRHINMVFQSYALFPHMTVEENVafglkmRKVPRAEIKPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 109 AEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHL 188
Cdd:TIGR01187 81 VLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHD 160
|
170 180
....*....|....*....|....
gi 2534501033 189 PEDAATVADRAVVLSGrpAKIVAD 212
Cdd:TIGR01187 161 QEEAMTMSDRIAIMRK--GKIAQI 182
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
14-202 |
6.72e-40 |
|
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: 136.62 E-value: 6.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 14 KKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQDPRLLP 89
Cdd:cd03301 8 KRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKdrdiAMVFQNYALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 WLTALDNI------RAVRPETTE---SEAEAMLmrvGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:cd03301 86 HMTVYDNIafglklRKVPKDEIDervREVAELL---QIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 161 RTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03301 163 AKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVM 204
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-202 |
1.17e-39 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 137.24 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGF------VFQDPR--LLPWLTA 93
Cdd:COG1124 19 PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFrrrvqmVFQDPYasLHPRHTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNI----RAVRPETTESEAEAMLMRVGL-KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:COG1124 99 DRILaeplRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEIL 178
|
170 180 190
....*....|....*....|....*....|....
gi 2534501033 169 QVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:COG1124 179 NLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVM 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-157 |
2.37e-39 |
|
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: 133.16 E-value: 2.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWLTALDNI 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKslrkeiGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 R------AVRPETTESEAEAMLMRVGLKGFE----RYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:pfam00005 81 RlglllkGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
21-202 |
2.43e-39 |
|
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: 136.28 E-value: 2.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWLTAL 94
Cdd:cd03295 14 KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVelrrkiGYVIQQIGLFPHMTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIRAV------RPETTESEAEAMLMRVGL--KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVE 166
Cdd:cd03295 94 ENIALVpkllkwPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQ 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534501033 167 MEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03295 174 LQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIM 209
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-202 |
2.34e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.63 E-value: 2.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVF 82
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPewrrqvAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 QDPRLLPwLTALDNIRAV----RPETTESEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:COG4619 81 QEPALWG-GTVRDNLPFPfqlrERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 158 SLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-212 |
3.43e-38 |
|
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: 138.88 E-value: 3.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------GFVFQDPR--LL 88
Cdd:COG1123 277 GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrelrrrvQMVFQDPYssLN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLT-------ALDNIRAVRPETTESEAEAMLMRVGL-KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:COG1123 357 PRMTvgdiiaePLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALD 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 161 RTLVVEMEQVLLTLIETNRPTVLLVTHlpeD---AATVADRAVVLS-GRpakIVAD 212
Cdd:COG1123 437 VSVQAQILNLLRDLQRELGLTYLFISH---DlavVRYIADRVAVMYdGR---IVED 486
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-203 |
3.54e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 135.98 E-value: 3.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 7 LEIDVEGKKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV----VAAEAPPAGFVF 82
Cdd:PRK10851 3 IEIANIKKSFG--RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTdvsrLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 QDPRLLPWLTALDNI--------RAVRPETTESEAEAM--LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:PRK10851 81 QHYALFRHMTVFDNIafgltvlpRRERPNAAAIKAKVTqlLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 153 DEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS 203
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
5-225 |
3.92e-38 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 136.00 E-value: 3.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 5 PRLEIDVEGKKFDFLptplLDgFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVV----------AAE 74
Cdd:COG4148 1 MMLEVDFRLRRGGFT----LD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlqdsargiflPPH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 75 APPAGFVFQDPRLLPWLTALDNI-----RAVRPETTESEAE--AMLmrvGLKGFERYYPHELSGGMQRRVALARAFSVNP 147
Cdd:COG4148 76 RRRIGYVFQEARLFPHLSVRGNLlygrkRAPRAERRISFDEvvELL---GIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 148 RLLLLDEPFVSLDRTLVVEMEQVLLTLI-ETNRPtVLLVTHLPEDAATVADRAVVL-------SGRPAKIVADYRFASAA 219
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRdELDIP-ILYVSHSLDEVARLADHVVLLeqgrvvaSGPLAEVLSRPDLLPLA 231
|
....*.
gi 2534501033 220 GQRPRA 225
Cdd:COG4148 232 GGEEAG 237
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-202 |
5.15e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 136.23 E-value: 5.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 1 MSSGPRLEIDVEGKKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV----VAAEAP 76
Cdd:PRK09452 9 SSLSPLVELRGISKSFD--GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 77 PAGFVFQDPRLLPWLTALDNI-------RAVRPETTESEAEAMLMrVGLKGFERYYPHELSGGMQRRVALARAFSVNPRL 149
Cdd:PRK09452 87 HVNTVFQSYALFPHMTVFENVafglrmqKTPAAEITPRVMEALRM-VQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 150 LLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVM 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-242 |
1.95e-37 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 136.96 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 5 PRLEIDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV---DTLFSGRVLVDGVVAAEAPPA--- 78
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEAlrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 ---GFVFQDPR--LLPwLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNP 147
Cdd:COG1123 83 rriGMVFQDPMtqLNP-VTVGDQIaealenLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 148 RLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL-------SGRPAKIVADYRFASAAg 220
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMddgriveDGPPEEILAAPQALAAV- 240
|
250 260
....*....|....*....|..
gi 2534501033 221 qrPRAEREHIANQIAGAAAERL 242
Cdd:COG1123 241 --PRLGAARGRAAPAAAAAEPL 260
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
9-224 |
3.38e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 131.03 E-value: 3.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV--------------DGVVAAE 74
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqqKGLIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 75 APPAGFVFQDPRLLPWLTALDNI-------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNP 147
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 148 RLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLSGrpAKIV----ADYRFASAAGQRP 223
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQ--GRIVeqgpAKALFADPQQPRT 240
|
.
gi 2534501033 224 R 224
Cdd:PRK11264 241 R 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
21-193 |
3.85e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 129.52 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGvdTL-----FSGRVLVDGVVAAEAPPA----GFVFQDPRLLPWL 91
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAG--TLspafsASGEVLLNGRRLTALPAEqrriGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDNIR-AVRPETTESE----AEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVE 166
Cdd:COG4136 92 SVGENLAfALPPTIGRAQrrarVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQ 171
|
170 180
....*....|....*....|....*..
gi 2534501033 167 MEQVLLTLIETNRPTVLLVTHLPEDAA 193
Cdd:COG4136 172 FREFVFEQIRQRGIPALLVTHDEEDAP 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
11-202 |
7.02e-37 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 127.36 E-value: 7.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 11 VEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGvvaaeappagfvfQDPRLLPW 90
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-------------KDIAKLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALDNIRAVrpetteseaeamlmrvglkgferyypHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQV 170
Cdd:cd00267 69 EELRRRIGYV--------------------------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLEL 122
|
170 180 190
....*....|....*....|....*....|..
gi 2534501033 171 LLTLIETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd00267 123 LRELAEEGR-TVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
24-212 |
9.49e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 129.61 E-value: 9.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------GFVFQDPRLLPWLTAL 94
Cdd:cd03256 17 LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrqiGMIFQQFNLIERLSVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNI-----------RAVRPETTESE---AEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:cd03256 97 ENVlsgrlgrrstwRSLFGLFPKEEkqrALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 161 RTLVvemEQVLLTLIETNRP---TVLLVTHLPEDAATVADRAVVLsgRPAKIVAD 212
Cdd:cd03256 177 PASS---RQVMDLLKRINREegiTVIVSLHQVDLAREYADRIVGL--KDGRIVFD 226
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
12-193 |
2.67e-36 |
|
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: 127.85 E-value: 2.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 12 EGKkfdfLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----------GFV 81
Cdd:TIGR02211 13 EGK----LDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNeraklrnkklGFI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 82 FQDPRLLPWLTALDN------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:TIGR02211 89 YQFHHLLPDFTALENvampllIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEP 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 2534501033 156 FVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAA 193
Cdd:TIGR02211 169 TGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAK 206
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-210 |
3.37e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 129.83 E-value: 3.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWLTAL 94
Cdd:COG1125 15 TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVelrrriGYVIQQIGLFPHMTVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIRAVrP-------ETTESEAEAMLMRVGL--KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD---RT 162
Cdd:COG1125 95 ENIATV-PrllgwdkERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDpitRE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534501033 163 lvvEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLsgRPAKIV 210
Cdd:COG1125 174 ---QLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVM--REGRIV 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-205 |
5.29e-36 |
|
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: 127.45 E-value: 5.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQDPRLLPWLTALDNI-- 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEkrdiSYVPQNYALFPHMTVYKNIay 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 --RAVRPETTESEAEAMLM--RVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLT 173
Cdd:cd03299 95 glKKRKVDKKEIERKVLEIaeMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKK 174
|
170 180 190
....*....|....*....|....*....|...
gi 2534501033 174 LIETNRPTVLLVTHLPEDAATVADR-AVVLSGR 205
Cdd:cd03299 175 IRKEFGVTVLHVTHDFEEAWALADKvAIMLNGK 207
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
24-200 |
9.45e-36 |
|
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: 126.29 E-value: 9.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------GFVFQDPRLLPWLTAL 94
Cdd:TIGR02982 21 LFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKqlvqlrrriGYIFQAHNLLGFLTAR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIR-------AVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL---V 164
Cdd:TIGR02982 101 QNVQmalelqpNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKLVLADEPTAALDSKSgrdV 180
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534501033 165 VEMEQvllTLIETNRPTVLLVTHLPEdAATVADRAV 200
Cdd:TIGR02982 181 VELMQ---KLAKEQGCTILMVTHDNR-ILDVADRIL 212
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-209 |
1.77e-35 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 129.57 E-value: 1.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 5 PRLEIDVEGKKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP----AGF 80
Cdd:PRK11607 18 PLLEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPyqrpINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 81 VFQDPRLLPWLTALDNI-------RAVRPETTESEAEaMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLD 153
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIafglkqdKLPKAEIASRVNE-MLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 154 EPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS-------GRPAKI 209
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNrgkfvqiGEPEEI 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
24-205 |
2.41e-35 |
|
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: 125.37 E-value: 2.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLF-----SGRVLVDG--VVAAEAPP------AGFVFQDPRLLPw 90
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGkdIYDLDVDVlelrrrVGMVFQKPNPFP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALDNI------RAVRP-ETTESEAEAMLMRVGLKGFE--RYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDR 161
Cdd:cd03260 95 GSIYDNVayglrlHGIKLkEELDERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 162 TLVVEMEQVLLTLieTNRPTVLLVTHLPEDAATVADR-AVVLSGR 205
Cdd:cd03260 175 ISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRtAFLLNGR 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-212 |
2.66e-35 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 132.65 E-value: 2.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPwLTAL 94
Cdd:COG2274 488 PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPAslrrqiGVVLQDVFLFS-GTIR 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtl 163
Cdd:COG2274 567 ENITLGDPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALD--- 643
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 164 vVEMEQVLLTLIETNRP--TVLLVTHlpeDAATV--ADRAVVLSGrpAKIVAD 212
Cdd:COG2274 644 -AETEAIILENLRRLLKgrTVIIIAH---RLSTIrlADRIIVLDK--GRIVED 690
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-202 |
4.20e-35 |
|
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: 131.03 E-value: 4.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWlTAL 94
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAswrrqiAWVPQNPYLFAG-TIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIRAVRPETTESEAEAMLMRVGLKGFERYYPHE-----------LSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtl 163
Cdd:COG4988 429 ENLRLGRPDASDEELEAALEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLD--- 505
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2534501033 164 vVEMEQVLLTLIETNRP--TVLLVTHLPEDAAtVADRAVVL 202
Cdd:COG4988 506 -AETEAEILQALRRLAKgrTVILITHRLALLA-QADRILVL 544
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-212 |
6.71e-35 |
|
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: 124.47 E-value: 6.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP-----AGFV--FQDPRLLPWLTALDN 96
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPheiarLGIGrtFQIPRLFPELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IR------------AVRPETTESE----AEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:cd03219 96 VMvaaqartgsgllLARARREEREarerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 161 RTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVL-------SGRPAKIVAD 212
Cdd:cd03219 176 PEETEELAELIRELRERGI-TVLLVEHDMDVVMSLADRVTVLdqgrviaEGTPDEVRNN 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
24-198 |
1.51e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 124.02 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLvdgvvAAEAPPAG------FVFQDPRLLPWLTALDNI 97
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEaredtrLMFQDARLLPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIET 177
Cdd:PRK11247 103 GLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQ 182
|
170 180
....*....|....*....|.
gi 2534501033 178 NRPTVLLVTHLPEDAATVADR 198
Cdd:PRK11247 183 HGFTVLLVTHDVSEAVAMADR 203
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
21-210 |
4.94e-34 |
|
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: 122.84 E-value: 4.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWLTAL 94
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRelarriAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNI--------RAVRPETTESE--AEAMLMRVGLKGF-ERYYpHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL 163
Cdd:COG1120 94 ELValgryphlGLFGRPSAEDReaVEEALERTGLEHLaDRPV-DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAH 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 164 VVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL-------SGRPAKIV 210
Cdd:COG1120 173 QLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLkdgrivaQGPPEEVL 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
21-204 |
6.49e-34 |
|
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: 121.92 E-value: 6.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------GFVFQDPRLLPWL 91
Cdd:cd03258 18 VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkarrriGMIFQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDNI----------RAVRPEttesEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDR 161
Cdd:cd03258 98 TVFENValpleiagvpKAEIEE----RVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2534501033 162 TlvvEMEQVLLTLIETNR---PTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:cd03258 174 E---TTQSILALLRDINRelgLTIVLITHEMEVVKRICDRVAVMEK 216
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
24-212 |
1.19e-33 |
|
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: 121.68 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP-----AGFV--FQDPRLLPWLTALDN 96
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPhriarLGIArtFQNPRLFPELTVLEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IR-------------------AVRPETTESEAEAM--LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:COG0411 100 VLvaaharlgrgllaallrlpRARREEREARERAEelLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDEP 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 156 FVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL-------SGRPAKIVAD 212
Cdd:COG0411 180 AAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLdfgrviaEGTPAEVRAD 243
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
20-202 |
1.20e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 127.19 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPwLTA 93
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDdlrrriAVVPQRPHLFD-TTL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRt 162
Cdd:COG4987 426 RENLRLARPDATDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDA- 504
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 163 lvvEMEQVLLTLIETNRP--TVLLVTHLPEDAATvADRAVVL 202
Cdd:COG4987 505 ---ATEQALLADLLEALAgrTVLLITHRLAGLER-MDRILVL 542
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-212 |
1.24e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 120.74 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 27 FRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-VAAEAP---PAGFVFQDPRLLPWLTALDNI----- 97
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQsHTGLAPyqrPVSMLFQENNLFAHLTVRQNIglglh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 -----RAVRPETTESEAEamlmRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLL 172
Cdd:TIGR01277 97 pglklNAEQQEKVVDAAQ----QVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534501033 173 TLIETNRPTVLLVTHLPEDAATVADRAVVLSGRPAKIVAD 212
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSD 212
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
20-202 |
4.46e-33 |
|
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: 117.87 E-value: 4.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPwLTA 93
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLEslrkniAYVPQDPFLFS-GTI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIravrpetteseaeamlmrvglkgferyypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvVEMEQVLLT 173
Cdd:cd03228 93 RENI-------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALD----PETEALILE 137
|
170 180 190
....*....|....*....|....*....|...
gi 2534501033 174 LIETNRP--TVLLVTHlpeDAATV--ADRAVVL 202
Cdd:cd03228 138 ALRALAKgkTVIVIAH---RLSTIrdADRIIVL 167
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-205 |
9.89e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.92 E-value: 9.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 27 FRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQDPRLLPWLTALDNIR-AVR 101
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSrrpvSMLFQENNLFSHLTVAQNIGlGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 102 PETTESEA-----EAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIE 176
Cdd:PRK10771 98 PGLKLNAAqreklHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQ 177
|
170 180 190
....*....|....*....|....*....|
gi 2534501033 177 TNRPTVLLVTHLPEDAATVADRA-VVLSGR 205
Cdd:PRK10771 178 ERQLTLLMVSHSLEDAARIAPRSlVVADGR 207
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
23-202 |
1.56e-32 |
|
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: 121.25 E-value: 1.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV--DTLFSGRVLVDGVVAAEAPP----AGFVFQDPRLLPWLTALDN 96
Cdd:TIGR03258 20 VLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFvkAAGLTGRIAIADRDLTHAPPhkrgLALLFQNYALFPHLKVEDN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 I-------RAVRPETTESEAEAmLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQ 169
Cdd:TIGR03258 100 VafglraqKMPKADIAERVADA-LKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSALDANIRANMRE 178
|
170 180 190
....*....|....*....|....*....|....
gi 2534501033 170 VLLTLIET-NRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:TIGR03258 179 EIAALHEElPELTILCVTHDQDDALTLADKAGIM 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-202 |
3.99e-32 |
|
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: 122.78 E-value: 3.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWlTAL 94
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADswrdqiAWVPQHPFLFAG-TIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIRAVRPETTESEAEAMLMRVGLKGFERYYP-----------HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL 163
Cdd:TIGR02857 414 ENIRLARPDASDAEIREALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534501033 164 VVEMEQVLLTLIETNrpTVLLVTHLPEDAAtVADRAVVL 202
Cdd:TIGR02857 494 EAEVLEALRALAQGR--TVLLVTHRLALAA-LADRIVVL 529
|
|
| ABC_choXWV_ATP |
TIGR03415 |
choline ABC transporter, ATP-binding protein; Members of this protein family are the ... |
29-211 |
4.14e-32 |
|
choline ABC transporter, ATP-binding protein; Members of this protein family are the ATP-binding subunit of a three-protein transporter. This family belongs, more broadly, to the family of proline and glycine-betaine transporters, but members have been identified by direct characterization and by bioinformatic means as choline transporters. Many species have several closely-related members of this family, probably with variable abilities to act additionally on related quaternary amines. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 188317 [Multi-domain] Cd Length: 382 Bit Score: 120.65 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV---DGVV-AAEAPPA----------GFVFQDPRLLPWLTAL 94
Cdd:TIGR03415 45 LDIEEGEICVLMGLSGSGKSTLLRAVNGLNPVSRGSVLVkdgDGSVdVANCDAAtlrrlrthrvSMVFQQFALLPWRTVE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:TIGR03415 125 ENVafglemQGMPKAERRKRVDEQLELVGLAQWADRKPGELSGGMQQRVGLARAFATEAPILLMDEPFSALDPLIRTQLQ 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 169 QVLLTLIETNRPTVLLVTHLPEDAATVADR-AVVLSGR------PAKIVA 211
Cdd:TIGR03415 205 DELLELQSKLKKTIVFVSHDLDEALKIGNRiAIMEGGRiiqhgtPEEIVL 254
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-205 |
6.08e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.11 E-value: 6.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-GFV---FQDPRLLPwLTALD- 95
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRiGYVpqrAEVDWDFP-ITVRDv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 -------NIRAVRPETTESEAEAM--LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvVE 166
Cdd:COG1121 98 vlmgrygRRGLFRRPSRADREAVDeaLERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD----AA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2534501033 167 MEQVLLTLI----ETNRpTVLLVTHLPEDAATVADRAVVLSGR 205
Cdd:COG1121 174 TEEALYELLrelrREGK-TILVVTHDLGAVREYFDRVLLLNRG 215
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
14-203 |
7.56e-32 |
|
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: 116.07 E-value: 7.56e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 14 KKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-VAAEAPPA----GFVFQDPRLL 88
Cdd:cd03263 8 KTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsIRTDRKAArqslGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLTALDN------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:cd03263 88 DELTVREHlrfyarLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2534501033 163 LVVEMEQVLLTLIEtNRpTVLLVTHLPEDAATVADRAVVLS 203
Cdd:cd03263 168 SRRAIWDLILEVRK-GR-SIILTTHSMDEAEALCDRIAIMS 206
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
29-202 |
5.64e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 117.14 E-value: 5.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEA------PP----AGFVFQDPRLLPWLTALDNIR 98
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSrkgiflPPekrrIGYVFQEARLFPHLSVRGNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 99 ----AVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTL 174
Cdd:TIGR02142 98 ygmkRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERL 177
|
170 180
....*....|....*....|....*...
gi 2534501033 175 IETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:TIGR02142 178 HAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-202 |
6.94e-31 |
|
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: 113.66 E-value: 6.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP---------PAGFVFQDPRLLPWL 91
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraipylrrKIGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDN------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVV 165
Cdd:cd03292 94 NVYENvafaleVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 2534501033 166 EMEQvLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03292 174 EIMN-LLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
22-206 |
6.98e-31 |
|
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: 113.40 E-value: 6.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP-AGFVFQDpRLLPW---LTALD-- 95
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKrIGYVPQR-RSIDRdfpISVRDvv 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 ------NIRAVRPETTE--SEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEM 167
Cdd:cd03235 92 lmglygHKGLFRRLSKAdkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDI 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534501033 168 EQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLSGRP 206
Cdd:cd03235 172 YELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLNRTV 209
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
23-205 |
7.99e-31 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 113.72 E-value: 7.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV----------DGVVAAEAPPAGFVFQDPRLLPWLT 92
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeEARAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVE 166
Cdd:PRK10584 105 ALENVelpallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534501033 167 MEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSGR 205
Cdd:PRK10584 185 IADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
24-204 |
1.38e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.56 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------GFVFQDPRLLPWLTAL 94
Cdd:COG1135 21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraarrkiGMIFQHFNLLSSRTVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIRA------VRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD--RTlvve 166
Cdd:COG1135 101 ENVALpleiagVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDpeTT---- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2534501033 167 mEQVLLTLIETNRP---TVLLVTHLPEDAATVADRAVVLSG 204
Cdd:COG1135 177 -RSILDLLKDINRElglTIVLITHEMDVVRRICDRVAVLEN 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-204 |
2.98e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 117.57 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPwLTAL 94
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLEslrrqiGVVPQDTFLFS-GTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGmQR-RVALARAFSVNPRLLLLDEPFVSLDrt 162
Cdd:COG1132 432 ENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGG-QRqRIAIARALLKDPPILILDEATSALD-- 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2534501033 163 lvVEMEQVLLTLIETNRP--TVLLVTH-LpedaATV--ADRAVVLSG 204
Cdd:COG1132 509 --TETEALIQEALERLMKgrTTIVIAHrL----STIrnADRILVLDD 549
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-212 |
4.67e-30 |
|
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: 110.22 E-value: 4.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAgfvfqdprllpwltALDNIRAV 100
Cdd:cd03214 12 RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK--------------ELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 101 RPEtteseaeaMLMRVGLKGF-ERYYpHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNR 179
Cdd:cd03214 78 VPQ--------ALELLGLAHLaDRPF-NELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERG 148
|
170 180 190
....*....|....*....|....*....|...
gi 2534501033 180 PTVLLVTHLPEDAATVADRAVVLSGRpaKIVAD 212
Cdd:cd03214 149 KTVVMVLHDLNLAARYADRVILLKDG--RIVAQ 179
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-202 |
5.96e-30 |
|
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: 113.61 E-value: 5.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV---DTLFSGRVLVDGVVAAEAPPA----------GFVFQDPrllpw 90
Cdd:COG0444 21 VDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSEKelrkirgreiQMIFQDP----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALD-----------NIRA---VRPETTESEAEAMLMRVGLKGFERY---YPHELSGGMQRRVALARAFSVNPRLLLLD 153
Cdd:COG0444 96 MTSLNpvmtvgdqiaePLRIhggLSKAEARERAIELLERVGLPDPERRldrYPHELSGGMRQRVMIARALALEPKLLIAD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 154 EPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHlpeD---AATVADRAVVL 202
Cdd:COG0444 176 EPTTALDVTIQAQILNLLKDLQRELGLAILFITH---DlgvVAEIADRVAVM 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-212 |
8.64e-30 |
|
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: 110.76 E-value: 8.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLpWLTA 93
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAdlrrniGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:cd03245 95 RDNITLGAPLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 163 LVVEMEQVLLTLIETNrpTVLLVTHLPEdAATVADRAVVL-SGRpakIVAD 212
Cdd:cd03245 175 SEERLKERLRQLLGDK--TLIIITHRPS-LLDLVDRIIVMdSGR---IVAD 219
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
29-204 |
3.66e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 112.43 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQDPRLLPWLTALDNI------- 97
Cdd:PRK11000 24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAergvGMVFQSYALYPHLSVAENMsfglkla 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 ---RAVRPETTESEAEaMLMRVGLkgFERyYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTL 174
Cdd:PRK11000 104 gakKEEINQRVNQVAE-VLQLAHL--LDR-KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRL 179
|
170 180 190
....*....|....*....|....*....|
gi 2534501033 175 IETNRPTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:PRK11000 180 HKRLGRTMIYVTHDQVEAMTLADKIVVLDA 209
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
22-202 |
4.70e-29 |
|
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: 108.46 E-value: 4.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQDPRLLPWLTALDNI 97
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAlrriGALIEAPGFYPNLTARENL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 R--AVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLI 175
Cdd:cd03268 94 RllARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLR 173
|
170 180
....*....|....*....|....*..
gi 2534501033 176 ETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03268 174 DQGI-TVLISSHLLSEIQKVADRIGII 199
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
24-204 |
7.71e-29 |
|
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: 108.05 E-value: 7.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSsVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQDPRLLPWLTALDN-- 96
Cdd:cd03264 16 LDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKlrrriGYLPQEFGVYPNFTVREFld 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 ----IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD-------RTLVV 165
Cdd:cd03264 95 yiawLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDpeerirfRNLLS 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534501033 166 EmeqvlltlIETNRpTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:cd03264 175 E--------LGEDR-IVILSTHIVEDVESLCNQVAVLNK 204
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-187 |
2.65e-28 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 107.21 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 12 EGKkfdfLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG------VVAAEAP----PAGFV 81
Cdd:PRK11629 17 EGS----VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklSSAAKAElrnqKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 82 FQDPRLLPWLTALDN------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:PRK11629 93 YQFHHLLPDFTALENvampllIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|..
gi 2534501033 156 FVSLDRTLVVEMEQVLLTLIETNRPTVLLVTH 187
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTH 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-212 |
2.85e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 106.75 E-value: 2.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-------GFVFQDPRLLPWLTA 93
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHeraragiGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIRAVRPETTESEAEAMLMRV-----GLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:cd03224 93 EENLLLGAYARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 169 QVLLTLIETNRpTVLLVTHLPEDAATVADRA-------VVLSGRPAKIVAD 212
Cdd:cd03224 173 EAIRELRDEGV-TILLVEQNARFALEIADRAyvlergrVVLEGTAAELLAD 222
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
22-203 |
4.24e-28 |
|
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: 106.36 E-value: 4.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV---DGVV-AAEAPPA----------GFVFQDPRL 87
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWVdLAQASPReilalrrrtiGYVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 88 LPWLTALDNI------RAVRPETTESEAEAMLMRVGLKgfERY---YPHELSGGMQRRVALARAFSVNPRLLLLDEPFVS 158
Cdd:COG4778 105 IPRVSALDVVaeplleRGVDREEARARARELLARLNLP--ERLwdlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTAS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 159 LD---RTLVVEmeqvlltLIETNRP---TVLLVTHLPEDAATVADRAVVLS 203
Cdd:COG4778 183 LDaanRAVVVE-------LIEEAKArgtAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-208 |
4.78e-28 |
|
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: 107.54 E-value: 4.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPL----LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA---------GFVFQDP-R 86
Cdd:TIGR04521 14 TPFekkaLDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKklkdlrkkvGLVFQFPeH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 87 LLPWLTALDNIrA-------VRPETTESEAEAMLMRVGLKgfERYY---PHELSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:TIGR04521 94 QLFEETVYKDI-AfgpknlgLSEEEAEERVKEALELVGLD--EEYLersPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 157 VSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS-GRPAK 208
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHkGKIVL 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-202 |
1.15e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.27 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG--VV--AAEAPPAGFVFQDPRLLPWLTALDNI-- 97
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGedVThrSIQQRDICMVFQSYALFPHMSLGENVgy 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 -----RAVRPETTESEAEAMLMrVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLL 172
Cdd:PRK11432 102 glkmlGVPKEERKQRVKEALEL-VDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIR 180
|
170 180 190
....*....|....*....|....*....|
gi 2534501033 173 TLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK11432 181 ELQQQFNITSLYVTHDQSEAFAVSDTVIVM 210
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-204 |
2.69e-27 |
|
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: 103.88 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP---AGFVFQDP-RLLPWLTALDNIR 98
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERrksIGYVMQDVdYQLFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 99 AVRPETTES--EAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIE 176
Cdd:cd03226 95 LGLKELDAGneQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA 174
|
170 180
....*....|....*....|....*...
gi 2534501033 177 TNRpTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:cd03226 175 QGK-AVIVITHDYEFLAKVCDRVLLLAN 201
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
29-202 |
3.25e-27 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.81 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----------GFVFQDPRLLPWLTALDN-- 96
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevrrkkiAMVFQSFALMPHMTVLDNta 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 ----IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLL 172
Cdd:PRK10070 129 fgmeLAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|
gi 2534501033 173 TLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIM 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-202 |
6.35e-27 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 101.91 E-value: 6.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWlTALD 95
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNelgdhvGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIravrpetteseaeamlmrvglkgferyypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvVEMEQVLLTLI 175
Cdd:cd03246 95 NI-------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD----VEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|
gi 2534501033 176 ETNR---PTVLLVTHLPEDAATvADRAVVL 202
Cdd:cd03246 140 AALKaagATRIVIAHRPETLAS-ADRILVL 168
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
9-212 |
2.75e-26 |
|
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: 99.81 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEG--KKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAeappagfvFQDPR 86
Cdd:cd03216 1 LELRGitKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS--------FASPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 87 llpwlTALDN-IRAVrpetteseaeamlmrvglkgferyypHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVV 165
Cdd:cd03216 71 -----DARRAgIAMV--------------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2534501033 166 EMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLsgRPAKIVAD 212
Cdd:cd03216 120 RLFKVIRRLRAQGV-AVIFISHRLDEVFEIADRVTVL--RDGRVVGT 163
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
9-212 |
3.65e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 102.51 E-value: 3.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPT--PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP-------PAG 79
Cdd:TIGR04520 1 IEVENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweirkKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 80 FVFQDPrllpwltalDN--IRAV---------------RPETTESEAEAmLMRVGLKGFERYYPHELSGGMQRRVALARA 142
Cdd:TIGR04520 81 MVFQNP---------DNqfVGATveddvafglenlgvpREEMRKRVDEA-LKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 143 FSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATvADRAVVLSGrpAKIVAD 212
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNK--GKIVAE 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-202 |
7.84e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 99.62 E-value: 7.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVlvdgVVAAEAPPAgFVFQ---DPRLLPwLTALD--- 95
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----RRAGGARVA-YVPQrseVPDSLP-LTVRDlva 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 -----NIRAVRPETTESEA--EAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:NF040873 80 mgrwaRRGLWRRLTRDDRAavDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERII 159
|
170 180 190
....*....|....*....|....*....|....
gi 2534501033 169 QVLLTLIETNRpTVLLVTHLPEDAATvADRAVVL 202
Cdd:NF040873 160 ALLAEEHARGA-TVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
9-211 |
2.28e-25 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 100.22 E-value: 2.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGvvaaEAPPA---------- 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG----ENIPAmsrsrlytvr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 ---GFVFQDPRLLPWLTALDNIR-AVRPETTESEA---EAMLMR---VGLKGFERYYPHELSGGMQRRVALARAFSVNPR 148
Cdd:PRK11831 84 krmSMLFQSGALFTDMNVFDNVAyPLREHTQLPAPllhSTVMMKleaVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534501033 149 LLLLDEPFVSLDRtlvVEMeQVLLTLI-ETNRP---TVLLVTHLPEDAATVADRAVVLSGRpaKIVA 211
Cdd:PRK11831 164 LIMFDEPFVGQDP---ITM-GVLVKLIsELNSAlgvTCVVVSHDVPEVLSIADHAYIVADK--KIVA 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
9-202 |
2.37e-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: 98.89 E-value: 2.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGF-------- 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 81 VFQDPRLLPWLTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 161 RTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03269 161 PVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLL 201
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
21-204 |
2.79e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 101.84 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----GFVFQDPRLLPWLTALDN 96
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAdrdiAMVFQNYALYPHMSVREN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 ------IRAV-RPETTESEAEAMLMrVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQ 169
Cdd:PRK11650 97 mayglkIRGMpKAEIEERVAEAARI-LELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRL 175
|
170 180 190
....*....|....*....|....*....|....*
gi 2534501033 170 VLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:PRK11650 176 EIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNG 210
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-160 |
3.30e-25 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 100.96 E-value: 3.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAG---------FVFQDPR--LLPWLT 92
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrplrrrmqMVFQDPYasLNPRMT 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534501033 93 -------ALDNIRAVRPETTESEAEAMLMRVGLK-GFERYYPHELSGGmQR-RVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:COG4608 114 vgdiiaePLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGG-QRqRIGIARALALNPKLIVCDEPVSALD 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
18-216 |
4.61e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 102.40 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 18 FLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-------GFVFQDPRLLPW 90
Cdd:COG1129 14 FGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdaqaagiAIIHQELNLVPN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALDNI---------RAVRPETTESEAEAMLMRVGLK-------GferyyphELSGGMQRRVALARAFSVNPRLLLLDE 154
Cdd:COG1129 94 LSVAENIflgreprrgGLIDWRAMRRRARELLARLGLDidpdtpvG-------DLSVAQQQLVEIARALSRDARVLILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 155 PFVSLDRTLVvemeQVLLTLIETNRP---TVLLVTH-LPEdAATVADRAVVLsgRPAKIVADYRFA 216
Cdd:COG1129 167 PTASLTEREV----ERLFRIIRRLKAqgvAIIYISHrLDE-VFEIADRVTVL--RDGRLVGTGPVA 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
9-205 |
5.05e-25 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 98.21 E-value: 5.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQ 83
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREvrrriGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 84 DPRLLPWLTALDN------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:cd03265 81 DLSVDDELTGWENlyiharLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2534501033 158 SLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADR-AVVLSGR 205
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRvAIIDHGR 209
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
8-202 |
1.43e-24 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 97.30 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 8 EIDVEGKKFDFLPT-PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GF 80
Cdd:cd03254 2 EIEFENVNFSYDEKkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKslrsmiGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 81 VFQDPRLLPWlTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYP-----------HELSGGMQRRVALARAFSVNPRL 149
Cdd:cd03254 82 VLQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534501033 150 LLLDEPFVSLDrtlvVEMEQVL---LTLIETNRpTVLLVTHLPedaATV--ADRAVVL 202
Cdd:cd03254 161 LILDEATSNID----TETEKLIqeaLEKLMKGR-TSIIIAHRL---STIknADKILVL 210
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-187 |
1.71e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.29 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAaeappAGFVFQDPRLLPWLTALDNIRAVR 101
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLR-----IGYLPQEPPLDDDLTVLDTVLDGD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 102 PE--------------------------------------TTESEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARA 142
Cdd:COG0488 87 AElraleaeleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPvSELSGGWRRRVALARA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 143 FSVNPRLLLLDEPFVSLDrtlvVEM----EQVLLtlietNRP-TVLLVTH 187
Cdd:COG0488 167 LLSEPDLLLLDEPTNHLD----LESiewlEEFLK-----NYPgTVLVVSH 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-213 |
1.92e-24 |
|
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: 97.46 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVD--------TLFsGRVL--VD--------GVVAAEappagfvF 82
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLpptygndvRLF-GERRggEDvwelrkriGLVSPA-------L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 QDpRLLPWLTALDNI-----------RAVRPETTEsEAEAMLMRVGLKGF-ERYYpHELSGGMQRRVALARAFSVNPRLL 150
Cdd:COG1119 88 QL-RFPRDETVLDVVlsgffdsiglyREPTDEQRE-RARELLELLGLAHLaDRPF-GTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 151 LLDEPFVSLD---RTLVVEMeqvLLTLIETNRPTVLLVTHLPEDAATVADRAVVLsgRPAKIVADY 213
Cdd:COG1119 165 ILDEPTAGLDlgaRELLLAL---LDKLAAEGAPTLVLVTHHVEEIPPGITHVLLL--KDGRVVAAG 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
28-202 |
2.11e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.01 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 28 RLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG-------VVAAEAPPA-----GFVFQDPRLLPWLTALD 95
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqKPSEKAIRLlrqkvGMVFQQYNLWPHLTVME 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 N-IRA------VRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:COG4161 102 NlIEApckvlgLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVV 181
|
170 180 190
....*....|....*....|....*....|....
gi 2534501033 169 QVLLTLIETNrPTVLLVTHLPEDAATVADRAVVL 202
Cdd:COG4161 182 EIIRELSQTG-ITQVIVTHEVEFARKVASQVVYM 214
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
9-209 |
2.12e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.20 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLP-TPL----LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEA-------- 75
Cdd:PRK13637 3 IKIENLTHIYMEgTPFekkaLDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvklsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 76 PPAGFVFQDP--RLLPWLTALD------NIRAVRPETTESEAEAMLMrVGLKgFERY---YPHELSGGMQRRVALARAFS 144
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDiafgpiNLGLSEEEIENRVKRAMNI-VGLD-YEDYkdkSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 145 VNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVV-------LSGRPAKI 209
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVmnkgkceLQGTPREV 232
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
29-202 |
2.70e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.01 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG----VVAAEAPPA--------GFVFQDPRLLPWLTALDN 96
Cdd:PRK11124 23 LDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdFSKTPSDKAirelrrnvGMVFQQYNLWPHLTVQQN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 -------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQ 169
Cdd:PRK11124 103 lieapcrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVS 182
|
170 180 190
....*....|....*....|....*....|...
gi 2534501033 170 VLLTLIETNrPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK11124 183 IIRELAETG-ITQVIVTHEVEVARKTASRVVYM 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-195 |
2.71e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 96.03 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAgfVFQDprLL---------PWLT 92
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE--YHQD--LLylghqpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNIR---AVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQ 169
Cdd:PRK13538 91 ALENLRfyqRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170 180
....*....|....*....|....*...
gi 2534501033 170 VLLTLIEtNRPTVLLVTH--LPEDAATV 195
Cdd:PRK13538 171 LLAQHAE-QGGMVILTTHqdLPVASDKV 197
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-187 |
3.66e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.14 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV-DGVVaaeappAGFVFQDPRL 87
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVK------IGYFDQHQEE 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 88 L-PWLTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvV 165
Cdd:COG0488 390 LdPDKTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD----I 465
|
170 180
....*....|....*....|..
gi 2534501033 166 EMEQVLLTLIETNRPTVLLVTH 187
Cdd:COG0488 466 ETLEALEEALDDFPGTVLLVSH 487
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
9-205 |
3.91e-24 |
|
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: 93.67 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVaaeappagfvfqdprll 88
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 pwltaldniravrpetteseaeamlmRVGlkgferYYPHeLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEME 168
Cdd:cd03221 64 --------------------------KIG------YFEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALE 110
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534501033 169 QVLLTLietnRPTVLLVTHlpeDAA---TVADRAVVLSGR 205
Cdd:cd03221 111 EALKEY----PGTVILVSH---DRYfldQVATKIIELEDG 143
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
24-205 |
4.17e-24 |
|
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: 95.90 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQDPRLLPWLTALDNIR 98
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEarrrlGFVSDSTGLYDRLTARENLE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 99 ------AVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLL 172
Cdd:cd03266 101 yfaglyGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIR 180
|
170 180 190
....*....|....*....|....*....|....
gi 2534501033 173 TLIETNRpTVLLVTHLPEDAATVADRAVVL-SGR 205
Cdd:cd03266 181 QLRALGK-CILFSTHIMQEVERLCDRVVVLhRGR 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-212 |
4.96e-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: 96.07 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP-------AGFV 81
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 82 FQDPRLLPWLTALDNIRAVRPETTESEA------EAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKereeklEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 156 FVSLDRTLVVEMEQVLLTLIETNrPTVLLVTHLPEDAATVADRA-------VVLSGRPAKIVAD 212
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRG-IGVLITDHNVRETLSITDRAyiiyegkVLAEGTPEEIAAN 223
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
24-212 |
5.14e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 100.18 E-value: 5.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----------GFVFQDPRLLPWLTA 93
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADalaqlrrehfGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDN--IRAVRPETTESE----AEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEM 167
Cdd:PRK10535 104 AQNveVPAVYAGLERKQrllrAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 168 EQVLLTLIETNRpTVLLVTHLPEDAATvADRavVLSGRPAKIVAD 212
Cdd:PRK10535 184 MAILHQLRDRGH-TVIIVTHDPQVAAQ-AER--VIEIRDGEIVRN 224
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
29-205 |
1.72e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.10 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLR-------MIGGVDTlfSGRVLVDG--VVAAEAPPA------GFVFQDPRLLPwLTA 93
Cdd:COG1117 32 LDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGARV--EGEILLDGedIYDPDVDVVelrrrvGMVFQKPNPFP-KSI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNI------RAVRPETTESEA-EAMLMRVGL----------KGFEryypheLSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:COG1117 109 YDNVayglrlHGIKSKSELDEIvEESLRKAALwdevkdrlkkSALG------LSGGQQQRLCIARALAVEPEVLLMDEPT 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 157 VSLD--RTLVVEMeqvlltLIET--NRPTVLLVTHLPEDAATVADR-AVVLSGR 205
Cdd:COG1117 183 SALDpiSTAKIEE------LILElkKDYTIVIVTHNMQQAARVSDYtAFFYLGE 230
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-187 |
1.88e-23 |
|
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: 98.20 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP------AGFVFQDPRLLPwLTALD 95
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdevrrrVSVCAQDAHLFD-TTVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLV 164
Cdd:TIGR02868 428 NLRLARPDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETA 507
|
170 180
....*....|....*....|...
gi 2534501033 165 VEMEQVLLTLieTNRPTVLLVTH 187
Cdd:TIGR02868 508 DELLEDLLAA--LSGRTVVLITH 528
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-204 |
2.03e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.98 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLF-----SGRVLVDGVVAAEAP------P 77
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDvielrrR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 78 AGFVFQDPRLLPWLTALDNI----RAVRPETTESEAEAMLmRVGLKGFERYY---------PHELSGGMQRRVALARAFS 144
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENValglKLNRLVKSKKELQERV-RWALEKAQLWDevkdrldapAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 145 VNPRLLLLDEPFVSLDRTLVVEMEQVLLTLieTNRPTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYK 220
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
22-212 |
2.20e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.84 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAgfvfqdprllpwltALDNIRAVR 101
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPA--------------ELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 102 PETT--------------------------ESEAEAMLMRVGLKGFE-RYYPhELSGGMQRRVALARAF------SVNPR 148
Cdd:PRK13548 82 PQHSslsfpftveevvamgraphglsraedDALVAAALAQVDLAHLAgRDYP-QLSGGEQQRVQLARVLaqlwepDGPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 149 LLLLDEPFVSLD-----RTLvvemeQVLLTLIETNRPTVLLVTHlpeD---AATVADRAVVLSGrpAKIVAD 212
Cdd:PRK13548 161 WLLLDEPTSALDlahqhHVL-----RLARQLAHERGLAVIVVLH---DlnlAARYADRIVLLHQ--GRLVAD 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-204 |
5.05e-23 |
|
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: 93.37 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPwLTALD 95
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRwlrsqiGLVSQEPVLFD-GTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIRAVRPETTESEAEA------------MLM-----RVGLKGFEryypheLSGGMQRRVALARAFSVNPRLLLLDEPFVS 158
Cdd:cd03249 96 NIRYGKPDATDEEVEEaakkanihdfimSLPdgydtLVGERGSQ------LSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 159 LDRtlvvEMEQVL---LTLIETNRpTVLLVTH-LpedaATV--ADRAVVLSG 204
Cdd:cd03249 170 LDA----ESEKLVqeaLDRAMKGR-TTIVIAHrL----STIrnADLIAVLQN 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
24-204 |
6.17e-23 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.25 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-VAAEAPPA--------GFVFQDPRLLPWLTAL 94
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQdLTALSEKElrkarrqiGMIFQHFNLLSSRTVF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRtlvvEME 168
Cdd:PRK11153 101 DNValplelAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDP----ATT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534501033 169 QVLLTLI-ETNRP---TVLLVTHLPEDAATVADRAVVLSG 204
Cdd:PRK11153 177 RSILELLkDINRElglTIVLITHEMDVVKRICDRVAVIDA 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
24-212 |
8.84e-23 |
|
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: 92.74 E-value: 8.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-------GFVFQDPRLLPWLTALDN 96
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriarlgiGYVPEGRRIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IR-AVRPETTESEAEAMLMRVglkgFErYYPH----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVV 165
Cdd:COG0410 99 LLlGAYARRDRAEVRADLERV----YE-LFPRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 166 EMEQVLLTLIETNRpTVLLVTHLPEDAATVADRA-------VVLSGRPAKIVAD 212
Cdd:COG0410 174 EIFEIIRRLNREGV-TILLVEQNARFALEIADRAyvlergrIVLEGTAAELLAD 226
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-222 |
1.38e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.88 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEA------PPAGFVFQDPR-LLPWLTA 93
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEnekwvrSKVGLVFQDPDdQVFSSTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD-RTLVVE 166
Cdd:PRK13647 98 WDDVafgpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDpRGQETL 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 167 MEqvLLTLIETNRPTVLLVTHLPEDAATVADRAVVL-SGR-----PAKIVADYRFASAAGQR 222
Cdd:PRK13647 178 ME--ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLkEGRvlaegDKSLLTDEDIVEQAGLR 237
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-212 |
1.77e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.49 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRL-LPWlTAL 94
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWelarrrAVLPQHSSLaFPF-TVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIR----AVRPETTESE--AEAMLMRVGLKGF-ERYYPhELSGGMQRRVALARAF-----SVN--PRLLLLDEPFVSLD 160
Cdd:COG4559 94 EVVAlgraPHGSSAAQDRqiVREALALVGLAHLaGRSYQ-TLSGGEQQRVQLARVLaqlwePVDggPRWLFLDEPTSALD 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 161 -----RTLvvemeQVLLTLieTNRP-TVLLVTHlpeD---AATVADRAVVLSGRpaKIVAD 212
Cdd:COG4559 173 lahqhAVL-----RLARQL--ARRGgGVVAVLH---DlnlAAQYADRILLLHQG--RLVAQ 221
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-189 |
1.84e-22 |
|
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: 91.02 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAG-----FVFQDPRLLPWLTALDNI 97
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIargllYLGHAPGIKTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIET 177
Cdd:cd03231 95 RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCAR 174
|
170
....*....|..
gi 2534501033 178 NrPTVLLVTHLP 189
Cdd:cd03231 175 G-GMVVLTTHQD 185
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-243 |
4.40e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.10 E-value: 4.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAA------EAPPA----GFVFQDPR-LLPWLTALDNI 97
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstskqkEIKPVrkkvGVVFQFPEsQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 R------AVRPETTESEAEAMLMRVGL-KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQV 170
Cdd:PRK13643 107 AfgpqnfGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 171 LLTLIETNRpTVLLVTHLPEDAATVADRAVVLS-------GRPAKIVADYRFASAAG-QRPRAerEHIANQIAGAAA--- 239
Cdd:PRK13643 187 FESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEkghiiscGTPSDVFQEVDFLKAHElGVPKA--THFADQLQKTGAvtf 263
|
....
gi 2534501033 240 ERLP 243
Cdd:PRK13643 264 EKLP 267
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-217 |
7.62e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.76 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGvdtlF---SGRVLVDGVVAAEAPPA------GFVFQDPrLLPWL 91
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG----FlpyQGSLKINGIELRELDPEswrkhlSWVGQNP-QLPHG 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDNIRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:PRK11174 438 TLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2534501033 161 RtlvVEMEQVLLTLIE-TNRPTVLLVTHLPEDAATVaDRAVVLsgRPAKIVADYRFAS 217
Cdd:PRK11174 518 A---HSEQLVMQALNAaSRRQTTLMVTHQLEDLAQW-DQIWVM--QDGQIVQQGDYAE 569
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-215 |
8.22e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 8.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP----------AGFVFQDPR-LLPW 90
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdikqirkkVGLVFQFPEsQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALDNIR------AVRPETTESEAEAMLMRVGLKG--FERYyPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:PRK13649 101 ETVLKDVAfgpqnfGVSQEEAEALAREKLALVGISEslFEKN-PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 163 LVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRA-------VVLSGRPAKIVADYRF 215
Cdd:PRK13649 180 GRKELMTLFKKLHQSGM-TIVLVTHLMDDVANYADFVyvlekgkLVLSGKPKDIFQDVDF 238
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
24-160 |
1.13e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 91.56 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAG---------FVFQDP--RLLPWLT 92
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqkllrqkiqIVFQNPygSLNPRKK 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534501033 93 A--------LDNIRAVRPETTEsEAEAMLMRVGLKGfERY--YPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:PRK11308 111 VgqileeplLINTSLSAAERRE-KALAMMAKVGLRP-EHYdrYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-189 |
1.14e-21 |
|
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: 88.95 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQDPRLLPWLTALD 95
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpheniLYLGHLPGLKPELSALE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIRAVRP--ETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLT 173
Cdd:TIGR01189 93 NLHFWAAihGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172
|
170
....*....|....*.
gi 2534501033 174 LIETNrPTVLLVTHLP 189
Cdd:TIGR01189 173 HLARG-GIVLLTTHQD 187
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-204 |
1.67e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.43 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 3 SGPRLEIDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-VAAEAPPA--- 78
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVpVPARARLArar 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 -GFVFQDPRLLPWLTALDNI----RAVRPETTESEA--EAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLL 151
Cdd:PRK13536 116 iGVVPQFDNLDLEFTVRENLlvfgRYFGMSTREIEAviPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 152 LDEPFVSLD---RTLVVEMEQVLLTLIEtnrpTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:PRK13536 196 LDEPTTGLDphaRHLIWERLRSLLARGK----TILLTTHFMEEAERLCDRLCVLEA 247
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-209 |
2.74e-21 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 90.14 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 14 KKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQDPRLL 88
Cdd:TIGR01188 1 KVYG--DFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKvrrsiGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLTALDNIR------AVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:TIGR01188 79 EDLTGRENLEmmgrlyGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534501033 163 LVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADR-AVVLSGRPAKI 209
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGV-TILLTTHYMEEADKLCDRiAIIDHGRIIAE 205
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
21-212 |
3.42e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 89.38 E-value: 3.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP-------PAGFVFQDP--RLLPWL 91
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdirnKAGMVFQNPdnQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALD------NIrAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTlvv 165
Cdd:PRK13633 103 VEEDvafgpeNL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS--- 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 166 EMEQVLLTLIETNRP---TVLLVTHLPEDAATvADRAVVLSGrpAKIVAD 212
Cdd:PRK13633 179 GRREVVNTIKELNKKygiTIILITHYMEEAVE-ADRIIVMDS--GKVVME 225
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-207 |
3.98e-21 |
|
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: 87.22 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGG--VDTLFSGRVLVDGV-VAAEAPPA--GFVFQDPRLLPWLTald 95
Cdd:cd03213 22 KQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRpLDKRSFRKiiGYVPQDDILHPTLT--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 niraVRpetteseaEAMLMRVGLKGferyypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLI 175
Cdd:cd03213 99 ----VR--------ETLMFAAKLRG--------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLA 158
|
170 180 190
....*....|....*....|....*....|....
gi 2534501033 176 ETNRpTVLLVTHLP-EDAATVADRAVVLS-GRPA 207
Cdd:cd03213 159 DTGR-TIICSIHQPsSEIFELFDKLLLLSqGRVI 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
24-210 |
4.65e-21 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 91.28 E-value: 4.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTL----LRMIGgvdtlFSGRVLVDGVVAAEAPPAGF---------VFQDP--RLL 88
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSRRALrplrrrmqvVFQDPfgSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLTALDNI----RAVRPETTESE----AEAMLMRVGLKGFERY-YPHELSGGmQR-RVALARAFSVNPRLLLLDEPFVS 158
Cdd:COG4172 377 PRMTVGQIIaeglRVHGPGLSAAErrarVAEALEEVGLDPAARHrYPHEFSGG-QRqRIAIARALILEPKLLVLDEPTSA 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 159 LDRTLVVEMEQVLLTLIETNRPTVLLVTHlpeDAATV---ADRAVVLsgRPAKIV 210
Cdd:COG4172 456 LDVSVQAQILDLLRDLQREHGLAYLFISH---DLAVVralAHRVMVM--KDGKVV 505
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-202 |
4.95e-21 |
|
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: 87.59 E-value: 4.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAE-APPAGFvfqdprlLPWLTALDNIRAV-- 100
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLlGLGGGF-------NPELTGRENIYLNgr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 101 -----RPETTESEAEaMLMRVGLKGFeRYYP-HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTL 174
Cdd:cd03220 111 llglsRKEIDEKIDE-IIEFSELGDF-IDLPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL 188
|
170 180
....*....|....*....|....*...
gi 2534501033 175 IETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:cd03220 189 LKQGK-TVILVSHDPSSIKRLCDRALVL 215
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
24-214 |
5.24e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.21 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVaaeAPP----AGFvfqDPRllpwLTALDNIRA 99
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV---SALlelgAGF---HPE----LTGRENIYL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 100 V-------RPETTESEAE----AmlmrvGLKGFE----RYYphelSGGMQRRVALARAFSVNPRLLLLDE-------PFV 157
Cdd:COG1134 112 NgrllglsRKEIDEKFDEivefA-----ELGDFIdqpvKTY----SSGMRARLAFAVATAVDPDILLVDEvlavgdaAFQ 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 158 --SLDRtlvveMEQvlltLIETNRpTVLLVTHLPEDAATVADRAVVLS-------GRPAKIVADYR 214
Cdd:COG1134 183 kkCLAR-----IRE----LRESGR-TVIFVSHSMGAVRRLCDRAIWLEkgrlvmdGDPEEVIAAYE 238
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-209 |
6.22e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 88.53 E-value: 6.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPT--PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP------PAGF 80
Cdd:PRK13635 6 IRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETvwdvrrQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 81 VFQDP-RLLPWLT-------ALDNIRAVRPETTESEAEAmLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:PRK13635 86 VFQNPdNQFVGATvqddvafGLENIGVPREEMVERVDQA-LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 153 DEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATvADRAVVLS-------GRPAKI 209
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNkgeileeGTPEEI 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
9-223 |
8.11e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.90 E-value: 8.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGvVAAEAPPAGFVFQDPRLL 88
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG-DDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLTALD---NIRAV--------------RPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLL 151
Cdd:PRK09536 83 PQDTSLSfefDVRQVvemgrtphrsrfdtWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 152 LDEPFVSLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLS-------GRPAKIVADYRFASAAGQRP 223
Cdd:PRK09536 163 LDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLAdgrvraaGPPADVLTADTLRAAFDART 240
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
21-212 |
8.34e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 88.21 E-value: 8.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG--------VVAAEAPPAGFVFQDPRLLPWLT 92
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRKTVGIVFQNPDDQLFAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNIRAVRP-------ETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRtlvV 165
Cdd:PRK13639 95 TVEEDVAFGPlnlglskEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP---M 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 166 EMEQVLLTLIETNRP--TVLLVTHLPEDAATVADRAVVLS-------GRPAKIVAD 212
Cdd:PRK13639 172 GASQIMKLLYDLNKEgiTIIISTHDVDLVPVYADKVYVMSdgkiikeGTPKEVFSD 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-204 |
1.26e-20 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 87.55 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAG---------FVFQD------PR 86
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrrdvqLVFQDspsavnPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 87 L-LPWLTA--LDNIRAVRPETTESEAEAMLMRVGLKG-FERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:TIGR02769 105 MtVRQIIGepLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 163 LVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:TIGR02769 185 LQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDK 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-212 |
1.32e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.01 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGG---VDtlfSGRVLVDGVVAAEAPP---A----GFVFQDPRLLPWLTA 93
Cdd:COG1137 19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGlvkPD---SGRIFLDGEDITHLPMhkrArlgiGYLPQEASIFRKLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIRAVRpETT-------ESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVE 166
Cdd:COG1137 96 EDNILAVL-ELRklskkerEERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVAD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 167 MEQVLLTLieTNRPTVLLVT-HLPEDAATVADRA-------VVLSGRPAKIVAD 212
Cdd:COG1137 175 IQKIIRHL--KERGIGVLITdHNVRETLGICDRAyiisegkVLAEGTPEEILNN 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-197 |
1.34e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 87.20 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV-----DTLFSGRVLVDG--VVAAEAPP------AGFVFQDPRLLP 89
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrnIYSPDVDPievrreVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 WLTALDNI-------RAVRPETTESE-AEAMLMRVGL----KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:PRK14267 99 HLTIYDNVaigvklnGLVKSKKELDErVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534501033 158 SLDRTLVVEMEQVLLTLieTNRPTVLLVTHLPEDAATVAD 197
Cdd:PRK14267 179 NIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSD 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-202 |
1.71e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.46 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 18 FLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDT-----LFSGRVLVDGV-------VAAEAPPAGFVFQDP 85
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRsifnyrdVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 86 RLLPwLTALDNIRA-------VRPETTESEAEAMLMRVGL----KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDE 154
Cdd:PRK14271 111 NPFP-MSIMDNVLAgvrahklVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534501033 155 PFVSLDRTLVVEMEQVLLTLieTNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALF 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
24-198 |
2.12e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.08 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG-----VVAAEAP----PAGFVFQDPRLLPWLTAL 94
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrLKNREVPflrrQIGMIFQDHHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DN------IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLvveME 168
Cdd:PRK10908 98 DNvaipliIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL---SE 174
|
170 180 190
....*....|....*....|....*....|..
gi 2534501033 169 QVLLTLIETNR--PTVLLVTHlpeDAATVADR 198
Cdd:PRK10908 175 GILRLFEEFNRvgVTVLMATH---DIGLISRR 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
31-212 |
2.67e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 87.00 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 31 IEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV-DGVVAAEAPP---------AGFVFQDPR-LLPWLTALDNIR- 98
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgERVITAGKKNkklkplrkkVGIVFQFPEhQLFEETVEKDICf 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 99 -----AVRPETTESEAEAMLMRVGL--KGFERYyPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVL 171
Cdd:PRK13634 110 gpmnfGVSEEDAKQKAREMIELVGLpeELLARS-PFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMF 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534501033 172 LTLIETNRPTVLLVTHLPEDAATVADRAVVL-------SGRPAKIVAD 212
Cdd:PRK13634 189 YKLHKEKGLTTVLVTHSMEDAARYADQIVVMhkgtvflQGTPREIFAD 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-204 |
3.07e-20 |
|
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: 89.04 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWlTAL 94
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREelgrhiGYLPQDVELFDG-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIrAVRPETTESEAEAMLMRVGLkgferyypHE-------------------LSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:COG4618 424 ENI-ARFGDADPEKVVAAAKLAGV--------HEmilrlpdgydtrigeggarLSGGQRQRIGLARALYGDPRLVVLDEP 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 156 FVSLDrtlvVEMEQVLLTLIETNRP---TVLLVTHLPEdAATVADRAVVLSG 204
Cdd:COG4618 495 NSNLD----DEGEAALAAAIRALKArgaTVVVITHRPS-LLAAVDKLLVLRD 541
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-202 |
4.69e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 4.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP------------PAGFVFQDPRLLPW 90
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqidaiklrkEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALDNI------------RAVRPETTESeaeamLMRVGL--KGFERYYP--HELSGGMQRRVALARAFSVNPRLLLLDE 154
Cdd:PRK14246 105 LSIYDNIayplkshgikekREIKKIVEEC-----LRKVGLwkEVYDRLNSpaSQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534501033 155 PFVSLDRTLVVEMEQVLLTLieTNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFL 225
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-212 |
5.72e-20 |
|
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: 85.23 E-value: 5.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPwLTALDN 96
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAwlrrqvGVVLQENVLFN-RSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvV 165
Cdd:cd03252 96 IALADPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDEATSALD----Y 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 166 EMEQVL---LTLIETNRpTVLLVTHlpeDAATV--ADRAVVLSGrpAKIVAD 212
Cdd:cd03252 172 ESEHAImrnMHDICAGR-TVIIIAH---RLSTVknADRIIVMEK--GRIVEQ 217
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-202 |
6.60e-20 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.82 E-value: 6.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 1 MSSGPRLEidVEGKKFDF----LPTPLLDGFRLEIEPSSVVALVGPSGVGKS----TLLRMIGGVDTLFSGRVLVDGVVA 72
Cdd:COG4172 1 MMSMPLLS--VEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 73 AEAPPA----------GFVFQDPrllpwLTALD---NI-----------RAVRPETTESEAEAMLMRVGLKGFER---YY 125
Cdd:COG4172 79 LGLSERelrrirgnriAMIFQEP-----MTSLNplhTIgkqiaevlrlhRGLSGAAARARALELLERVGIPDPERrldAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 126 PHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHlpeDAATV---ADRAVVL 202
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITH---DLGVVrrfADRVAVM 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-187 |
7.20e-20 |
|
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: 7.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQDPRLLPwLTALD 95
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAlssliSVLNQRPYLFD-TTLRN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIravrpetteseaeamlmrvGLKgferyypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRtlvvEMEQVLLTLI 175
Cdd:cd03247 94 NL-------------------GRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDP----ITERQLLSLI 141
|
170
....*....|....
gi 2534501033 176 --ETNRPTVLLVTH 187
Cdd:cd03247 142 feVLKDKTLIWITH 155
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
9-187 |
7.75e-20 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 84.97 E-value: 7.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPT-PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMiggvdtLF------SGRVLVDGVVAAEAPPA--- 78
Cdd:cd03253 1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRL------LFrfydvsSGSILIDGQDIREVTLDslr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 ---GFVFQDPRLLPwLTALDNIRAVRPETTESEAEA-----------MLM------RVGLKGFeryyphELSGGMQRRVA 138
Cdd:cd03253 75 raiGVVPQDTVLFN-DTIGYNIRYGRPDATDEEVIEaakaaqihdkiMRFpdgydtIVGERGL------KLSGGEKQRVA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 139 LARAFSVNPRLLLLDEPFVSLDrtlvVEMEQVLLTLIE---TNRpTVLLVTH 187
Cdd:cd03253 148 IARAILKNPPILLLDEATSALD----THTEREIQAALRdvsKGR-TTIVIAH 194
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-214 |
8.47e-20 |
|
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: 8.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP---AGF---VFQDPRL--LPWLTAL 94
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEykrAKYigrVFQDPMMgtAPSMTIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNI---------RAVRPETTESEAE------AML---------MRVGLkgferyypheLSGGmQRR-VALARAFSVNPRL 149
Cdd:COG1101 101 ENLalayrrgkrRGLRRGLTKKRRElfrellATLglglenrldTKVGL----------LSGG-QRQaLSLLMATLTKPKL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 150 LLLDEPFVSLD-RTlvveMEQVL-LT--LIETNRPTVLLVTHLPEDAATVADRAVVL-SGRpakIVADYR 214
Cdd:COG1101 170 LLLDEHTAALDpKT----AALVLeLTekIVEENNLTTLMVTHNMEQALDYGNRLIMMhEGR---IILDVS 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
21-207 |
1.11e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.56 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVdgvvaaeapPAG----FVFQDPRLLpwltaLDN 96
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIAR---------PAGarvlFLPQRPYLP-----LGT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IRAV--RPETTES----EAEAMLMRVGLKGF------ERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlv 164
Cdd:COG4178 442 LREAllYPATAEAfsdaELREALEAVGLGHLaerldeEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD---- 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 165 VEMEQVLLTLIETNRP--TVLLVTHLPEDAAtVADRAVVLSGRPA 207
Cdd:COG4178 518 EENEAALYQLLREELPgtTVISVGHRSTLAA-FHDRVLELTGDGS 561
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
20-202 |
1.43e-19 |
|
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: 84.20 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWlTA 93
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAslrrqiGLVSQDVFLFND-TV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrt 162
Cdd:cd03251 93 AENIAYGRPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSALD-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 163 lvVEMEQVLLTLIE---TNRpTVLLVTHlpeDAATV--ADRAVVL 202
Cdd:cd03251 171 --TESERLVQAALErlmKNR-TTFVIAH---RLSTIenADRIVVL 209
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
9-215 |
1.70e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.66 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLP--TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEA------PPAGF 80
Cdd:PRK13632 8 IKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnlkeirKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 81 VFQDP-RLLPWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLD 153
Cdd:PRK13632 88 IFQNPdNQFIGATVEDDIafglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 154 EPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHlPEDAATVADRAVVLS-------GRPAKIVADYRF 215
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISITH-DMDEAILADKVIVFSegkliaqGKPKEILNNKEI 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-202 |
1.83e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.70 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 28 RLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSG------RVLVDGVVAAEAPPA----GFVFQDPRLLPWLTALDNI 97
Cdd:PRK11144 18 NLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEKGICLPPEkrriGYVFQDARLFPHYKVRGNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 RAVRPETTESEAEAMlmrVGLKGFE---RYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTL 174
Cdd:PRK11144 98 RYGMAKSMVAQFDKI---VALLGIEpllDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180
....*....|....*....|....*...
gi 2534501033 175 IETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK11144 175 AREINIPILYVSHSLDEILRLADRVVVL 202
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-214 |
2.68e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.39 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA--GFVFQDPRLLPWLTALDNI---- 97
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRriGYLPEERGLYPKMKVGEQLvyla 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 --RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLI 175
Cdd:COG4152 97 rlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2534501033 176 ETNRpTVLLVTHLPEDAATVADR-------AVVLSGRPAKIVADYR 214
Cdd:COG4152 177 AKGT-TVIFSSHQMELVEELCDRiviinkgRKVLSGSVDEIRRQFG 221
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-204 |
2.74e-19 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 83.09 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVD---TLFSGRVLVDGVvaaEAPPA------GFVFQDPRLLPWLTA 93
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVeggGTTSGQILFNGQ---PRKPDqfqkcvAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIR-----AVRPETTESEAEAM-----LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL 163
Cdd:cd03234 99 RETLTytailRLPRKSSDAIRKKRvedvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 164 VVEMEQVLLTLIETNRpTVLLVTHLP-EDAATVADRAVVLSG 204
Cdd:cd03234 179 ALNLVSTLSQLARRNR-IVILTIHQPrSDLFRLFDRILLLSS 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
29-197 |
2.96e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 84.06 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLF-----SGRVLVDG--VVAAEAPPA------GFVFQDPRLLPwLTALD 95
Cdd:PRK14243 31 LDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGknLYAPDVDPVevrrriGMVFQKPNPFP-KSIYD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NI------------------RAVRPETTESEAEAMLMRVGLkgferyyphELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:PRK14243 110 NIaygaringykgdmdelveRSLRQAALWDEVKDKLKQSGL---------SLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534501033 158 SLDRTLVVEMEQVLLTLIEtnRPTVLLVTHLPEDAATVAD 197
Cdd:PRK14243 181 ALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARVSD 218
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
24-198 |
3.47e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.29 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLfSGRVLVDGVVAAE-----APPA---------GFVFQDPRLLP 89
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDL-NPEVTITGSIVYNghniySPRTdtvdlrkeiGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 wLTALDN------IRAVRPETTESEA-EAMLMRVGLKGFERYYPHE----LSGGMQRRVALARAFSVNPRLLLLDEPFVS 158
Cdd:PRK14239 100 -MSIYENvvyglrLKGIKDKQVLDEAvEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534501033 159 LDRTLVVEMEQVLLTLieTNRPTVLLVTHLPEDAATVADR 198
Cdd:PRK14239 179 LDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDR 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
9-202 |
4.42e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.52 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDT----------LFSGRVLVDGVVAAEAPPA 78
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshieLLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 ----GFVFQDPRLLPWLTALDNI------------RAVRPETTESEAEAM--LMRVGLKGFERYYPHELSGGMQRRVALA 140
Cdd:PRK09984 85 rantGYIFQQFNLVNRLSVLENVligalgstpfwrTCFSWFTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 141 RAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
29-212 |
7.97e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 7.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP-------PAGFVFQDPRLLPWLTALDNIRAV- 100
Cdd:PRK10895 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhararrGIGYLPQEASIFRRLSVYDNLMAVl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 101 ------RPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTL 174
Cdd:PRK10895 104 qirddlSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 175 IETNRpTVLLVTHLPEDAATVADRAVVLS-------GRPAKIVAD 212
Cdd:PRK10895 184 RDSGL-GVLITDHNVRETLAVCERAYIVSqghliahGTPTEILQD 227
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-202 |
2.27e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 81.55 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG-----VVAAEAPPAGF--------------VFQ 83
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlVRDKDGQLKVAdknqlrllrtrltmVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 84 DPRLLPWLTALDNIR-------AVRPETTESEAEAMLMRVGLKGFER-YYPHELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:PRK10619 100 HFNLWSHMTVLENVMeapiqvlGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEP 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2534501033 156 FVSLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK10619 180 TSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFL 225
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-189 |
2.39e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 80.30 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVvAAEAPPAGFVF-----QDPrLLPWLTALDN 96
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-DIDDPDVAEAChylghRNA-MKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 I---RAVRpETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVvemeQVLLT 173
Cdd:PRK13539 94 LefwAAFL-GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV----ALFAE 168
|
170
....*....|....*....
gi 2534501033 174 LIETNRP---TVLLVTHLP 189
Cdd:PRK13539 169 LIRAHLAqggIVIAATHIP 187
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
25-206 |
3.73e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.80 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 25 DGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP-----AGFV--FQDPRLLPWLTALDNI 97
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGhqiarMGVVrtFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 -----RAVR----------PETTESEAEAM------LMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:PRK11300 102 lvaqhQQLKtglfsgllktPAFRRAESEALdraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 157 VSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS-GRP 206
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNqGTP 232
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
31-187 |
3.93e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 80.65 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 31 IEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVvaaeapPAGF------------VFQDPRllpwlTALD--- 95
Cdd:COG4167 36 LEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH------KLEYgdykyrckhirmIFQDPN-----TSLNprl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIRAV-----RPETTESEAE------AMLMRVGLKG-FERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL 163
Cdd:COG4167 105 NIGQIleeplRLNTDLTAEEreerifATLRLVGLLPeHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAALDMSV 184
|
170 180
....*....|....*....|....
gi 2534501033 164 VVEMEQVLLTLIETNRPTVLLVTH 187
Cdd:COG4167 185 RSQIINLMLELQEKLGISYIYVSQ 208
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
24-202 |
3.96e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.00 E-value: 3.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEA------PPAGFVFQDPRLLPWLTALDNI 97
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnirevrKFVGLVFQNPDDQIFSPTVEQD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 RAVRP-------ETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQV 170
Cdd:PRK13652 100 IAFGPinlgldeETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDF 179
|
170 180 190
....*....|....*....|....*....|..
gi 2534501033 171 LLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK13652 180 LNDLPETYGMTVIFSTHQLDLVPEMADYIYVM 211
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
9-210 |
4.63e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.51 E-value: 4.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVF 82
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelakrlAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 QDPRLLPWLTaldniraVR--------PE-----TTESEA--EAMLMRVGLKGFERYYPHELSGGmQR-RVALARAFSVN 146
Cdd:COG4604 82 QENHINSRLT-------VRelvafgrfPYskgrlTAEDREiiDEAIAYLDLEDLADRYLDELSGG-QRqRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 147 PRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHlpeD---AATVADR-------AVVLSGRPAKIV 210
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLH---DinfASCYADHivamkdgRVVAQGTPEEII 224
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-187 |
4.76e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.57 E-value: 4.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIggvdTLF----SGRVLVDGVVAAEAPPAG------FVFQDPRLLP 89
Cdd:PRK11160 352 PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL----TRAwdpqQGEILLNGQPIADYSEAAlrqaisVVSQRVHLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 wLTALDNIRAVRPETTESEAEAMLMRVGL-------KGFE-------RyyphELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:PRK11160 428 -ATLRDNLLLAAPNASDEALIEVLQQVGLeklleddKGLNawlgeggR----QLSGGEQRRLGIARALLHDAPLLLLDEP 502
|
170 180 190
....*....|....*....|....*....|....*
gi 2534501033 156 FVSLDRtlvvEMEQVLLTLIE---TNRpTVLLVTH 187
Cdd:PRK11160 503 TEGLDA----ETERQILELLAehaQNK-TVLMITH 532
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
23-203 |
4.85e-18 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 79.72 E-value: 4.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKST----LLRMIGGVDTLFSGRVLVDGVVAAEAP----PAGFVFQDPR--LLPWLT 92
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSirgrHIATIMQNPRtaFNPLFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ----ALDNIRAVrpETTESEAEAM----LMRVGLKGFERY---YPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDR 161
Cdd:TIGR02770 81 mgnhAIETLRSL--GKLSKQARALileaLEAVGLPDPEEVlkkYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 162 TLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLS 203
Cdd:TIGR02770 159 VNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMD 200
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-202 |
5.34e-18 |
|
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: 79.05 E-value: 5.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAaeappagFVFQdprlLPWL---TALDN 96
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIA-------YVSQ----EPWIqngTIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IRAVRP-------ETTESEA-----EAM----LMRVGLKGFEryypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:cd03250 86 ILFGKPfdeeryeKVIKACAlepdlEILpdgdLTEIGEKGIN------LSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 161 ----RTLvveMEQVLLTLIETNRpTVLLVTH----LPEdaatvADRAVVL 202
Cdd:cd03250 160 ahvgRHI---FENCILGLLLNNK-TRILVTHqlqlLPH-----ADQIVVL 200
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
11-212 |
6.13e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.64 E-value: 6.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 11 VEGKKFDFL--P-TPL----LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-VAAEA------- 75
Cdd:PRK13641 3 IKFENVDYIysPgTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhITPETgnknlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 76 --PPAGFVFQDPRL-LPWLTALDNIR------AVRPETTESEAEAMLMRVGLK-GFERYYPHELSGGMQRRVALARAFSV 145
Cdd:PRK13641 83 lrKKVSLVFQFPEAqLFENTVLKDVEfgpknfGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 146 NPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLS-GR------PAKIVAD 212
Cdd:PRK13641 163 EPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEhGKlikhasPKEIFSD 235
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-208 |
7.15e-18 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 79.37 E-value: 7.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP------AGFVFQDPRL------- 87
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPeiyrqqVSYCAQTPTLfgdtvyd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 88 ---LPWLtaldnIRAVRPEttESEAEAMLMRVGL------KGFEryyphELSGGMQRRVALARAFSVNPRLLLLDEPFVS 158
Cdd:PRK10247 100 nliFPWQ-----IRNQQPD--PAIFLDDLERFALpdtiltKNIA-----ELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 159 LDRTLVVEMEQVLLTLIETNRPTVLLVTHlPEDAATVADRAVVLSGRPAK 208
Cdd:PRK10247 168 LDESNKHNVNEIIHRYVREQNIAVLWVTH-DKDEINHADKVITLQPHAGE 216
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-209 |
8.61e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 8.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLfSGRVLVDGVVAAEAP------------ 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGRVEFFNQniyerrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 77 --PAGFVFQDPRLLPwLTALDNIR------AVRPET-----TESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAF 143
Cdd:PRK14258 87 rrQVSMVHPKPNLFP-MSVYDNVAygvkivGWRPKLeiddiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 144 SVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSGRPAKI 209
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-187 |
3.23e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.13 E-value: 3.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKST----LLRMIGGvdtlfSGRVLVDGvvaaeAPPAGF--------------VFQDP 85
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDG-----QPLHNLnrrqllpvrhriqvVFQDP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 86 R--LLPWLTALDNI----RAVRPETTESEAE----AMLMRVGLKGFERY-YPHELSGGMQRRVALARAFSVNPRLLLLDE 154
Cdd:PRK15134 372 NssLNPRLNVLQIIeeglRVHQPTLSAAQREqqviAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190
....*....|....*....|....*....|...
gi 2534501033 155 PFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTH 187
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-187 |
3.70e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-------------VAAeappagfVFQDPRLL 88
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVplvqydhhylhrqVAL-------VGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWlTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:TIGR00958 568 SG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190
....*....|....*....|....*....|
gi 2534501033 158 SLDrtlvVEMEQVLLTLIETNRPTVLLVTH 187
Cdd:TIGR00958 647 ALD----AECEQLLQESRSRASRTVLLIAH 672
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
24-221 |
4.29e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 4.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAG---------FVFQDPrllpwLTAL 94
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQrkafrrdiqMVFQDS-----ISAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 D---NIRAVRPE-----TTESEAE------AMLMRVGLK-GFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSL 159
Cdd:PRK10419 103 NprkTVREIIREplrhlLSLDKAErlarasEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 160 DRTLVVEMEQVLLTLIETNRPTVLLVTHlpeDAATV---ADRAVVLSGrpAKIVAD------YRFASAAGQ 221
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITH---DLRLVerfCQRVMVMDN--GQIVETqpvgdkLTFSSPAGR 248
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-208 |
4.68e-17 |
|
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: 77.45 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEP-----SSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGFVFQDPRLLPWLTALDNIR 98
Cdd:cd03237 10 LGEFTLEVEGgsiseSEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 99 AVRPETtESEAEAMLMRVGLkgFERYYPhELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETN 178
Cdd:cd03237 90 YTHPYF-KTEIAKPLQIEQI--LDREVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180 190
....*....|....*....|....*....|
gi 2534501033 179 RPTVLLVTHLPEDAATVADRAVVLSGRPAK 208
Cdd:cd03237 166 EKTAFVVEHDIIMIDYLADRLIVFEGEPSV 195
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
25-202 |
4.76e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 78.59 E-value: 4.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 25 DGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGF---------VFQDP--RLLPWLTA 93
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravrsdiqmIFQDPlaSLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNI----RAVRPETTESEAE----AMLMRVGL-KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlV 164
Cdd:PRK15079 118 GEIIaeplRTYHPKLSRQEVKdrvkAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD---V 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2534501033 165 VEMEQVLLTLIETNRPTVLLVTHLPEDAATV---ADRAVVL 202
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVkhiSDRVLVM 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-220 |
4.85e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 78.30 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV---DTLFSGRVLVDGVVAAEAP------PAGFVFQDP-RLLP 89
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTvwdireKVGIVFQNPdNQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 WLTALDNI------RAV-RPETTESEAEAmLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:PRK13640 99 GATVGDDVafglenRAVpRPEMIKIVRDV-LADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 163 LVVEMEQVLLTLIETNRPTVLLVTHlPEDAATVADRAVVL-------SGRPAKIVADYRFASAAG 220
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITH-DIDEANMADQVLVLddgkllaQGSPVEIFSKVEMLKEIG 241
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-205 |
4.90e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 78.31 E-value: 4.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 1 MSSGPrleIDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRV-LVDGVVAAEAPPA- 78
Cdd:PRK13537 3 MSVAP---IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPVPSRARHAr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 ---GFVFQDPRLLPWLTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYPH------ELSGGMQRRVALARAFSVNPRL 149
Cdd:PRK13537 80 qrvGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKadakvgELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 150 LLLDEPFVSLD---RTLVVEMEQVLLtlieTNRPTVLLVTHLPEDAATVADR-AVVLSGR 205
Cdd:PRK13537 160 LVLDEPTTGLDpqaRHLMWERLRSLL----ARGKTILLTTHFMEEAERLCDRlCVIEEGR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
24-212 |
1.02e-16 |
|
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: 78.69 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV----DGVVAAEAPPA---------GFVFQDPRLLPW 90
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDgrgrakryiGILHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALDNIR-----------AVRPET--------TESEAEAMLMRvglkgferyYPHELSGGMQRRVALARAFSVNPRLLL 151
Cdd:TIGR03269 380 RTVLDNLTeaiglelpdelARMKAVitlkmvgfDEEKAEEILDK---------YPDELSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 152 LDEPFVSLDR-TLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRA-------VVLSGRPAKIVAD 212
Cdd:TIGR03269 451 LDEPTGTMDPiTKVDVTHSILKAREEMEQ-TFIIVSHDMDFVLDVCDRAalmrdgkIVKIGDPEEIVEE 518
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
21-212 |
1.66e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.81 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV--------VAAEAPPAGFVFQDP--RLLPW 90
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkgLMKLRESVGMVFQDPdnQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALD------NIRAVRPETTEsEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLV 164
Cdd:PRK13636 99 SVYQDvsfgavNLKLPEDEVRK-RVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 165 VEMEQVLLTLIETNRPTVLLVTH------LPEDAATVADRA-VVLSGRPAKIVAD 212
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHdidivpLYCDNVFVMKEGrVILQGNPKEVFAE 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
24-202 |
1.86e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.76 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-------GFVFQDPRLLPWLTALDN 96
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdaialgiGMVHQHFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 I-----RAVRPETTESEAEAMLMRVGlkgfERY--------YPHELSGGMQRRVALARAFSVNPRLLLLDEPfvsldrTL 163
Cdd:COG3845 101 IvlglePTKGGRLDRKAARARIRELS----ERYgldvdpdaKVEDLSVGEQQRVEILKALYRGARILILDEP------TA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 164 VvemeqvlLTLIETNR------------PTVLLVTH-LPEdAATVADRAVVL 202
Cdd:COG3845 171 V-------LTPQEADElfeilrrlaaegKSIIFITHkLRE-VMAIADRVTVL 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-204 |
4.10e-16 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 74.43 E-value: 4.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG-------------VVAAeappagfVFQDPRL 87
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGkpisqyehkylhsKVSL-------VGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 88 LPwLTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYPHE-----------LSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:cd03248 100 FA-RSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQRVAIARALIRNPQVLILDEAT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 157 VSLDRTLVVEMEQVLLTLIEtnRPTVLLVTHlpeDAATV--ADRAVVLSG 204
Cdd:cd03248 179 SALDAESEQQVQQALYDWPE--RRTVLVIAH---RLSTVerADQILVLDG 223
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-173 |
5.40e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 76.53 E-value: 5.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV--DGVVA--AEAPP---AGFVF----------- 82
Cdd:PRK11147 16 APLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqDLIVArlQQDPPrnvEGTVYdfvaegieeqa 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 --------------QDP--RLLPWLTA----LDNIRAVRPETTESEaeaMLMRVGLKGFERYypHELSGGMQRRVALARA 142
Cdd:PRK11147 96 eylkryhdishlveTDPseKNLNELAKlqeqLDHHNLWQLENRINE---VLAQLGLDPDAAL--SSLSGGWLRKAALGRA 170
|
170 180 190
....*....|....*....|....*....|.
gi 2534501033 143 FSVNPRLLLLDEPFVSLDRTLVVEMEQVLLT 173
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEGFLKT 201
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-205 |
6.67e-16 |
|
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: 74.29 E-value: 6.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVFQDPRLLPW-LTALD 95
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKflrriGVVFGQKTQLWWdLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIRAVR----------PETTESEAEAMLMRVGLKGFERyyphELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlVV 165
Cdd:cd03267 115 SFYLLAaiydlpparfKKRLDELSELLDLEELLDTPVR----QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD---VV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2534501033 166 EMEQVLLTLIETNR---PTVLLVTHLPEDAATVADRAVVLS-GR 205
Cdd:cd03267 188 AQENIRNFLKEYNRergTTVLLTSHYMKDIEALARRVLVIDkGR 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-205 |
9.92e-16 |
|
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: 72.46 E-value: 9.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-------GFVFQDPR---LLPWLTA 93
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdairagiAYVPEDRKregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIRAvrpetteseaeamlmrvglkgferyyPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLT 173
Cdd:cd03215 96 AENIAL--------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
170 180 190
....*....|....*....|....*....|...
gi 2534501033 174 LIETNRPTVLLVTHLPEdAATVADRAVVLS-GR 205
Cdd:cd03215 150 LADAGKAVLLISSELDE-LLGLCDRILVMYeGR 181
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-215 |
1.11e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 74.89 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA----------------------GFV 81
Cdd:PRK13631 42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNhelitnpyskkiknfkelrrrvSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 82 FQDPRLLPWLTALD-NIR------AVRPETTESEAEAMLMRVGLK-GFERYYPHELSGGMQRRVALARAFSVNPRLLLLD 153
Cdd:PRK13631 122 FQFPEYQLFKDTIEkDIMfgpvalGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFD 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 154 EPFVSLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVL-------SGRPAKIVADYRF 215
Cdd:PRK13631 202 EPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMdkgkilkTGTPYEIFTDQHI 269
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-205 |
1.32e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 75.63 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMiggvdtLF------SGRVLVDGVVAAEAPPA------GFVFQDprllp 89
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARL------LFrfydvtSGRILIDGQDIRDVTQAslraaiGIVPQD----- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 wlTAL------DNIRAVRPETTESEAEA-----------------MLMRVGLKGFEryypheLSGGMQRRVALARAFSVN 146
Cdd:COG5265 441 --TVLfndtiaYNIAYGRPDASEEEVEAaaraaqihdfieslpdgYDTRVGERGLK------LSGGEKQRVAIARTLLKN 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 147 PRLLLLDEPFVSLD-RTlvvEME-QVLLTLIETNRpTVLLVTH-LpedaATV--ADRAVVLS-GR 205
Cdd:COG5265 513 PPILIFDEATSALDsRT---ERAiQAALREVARGR-TTLVIAHrL----STIvdADEILVLEaGR 569
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
21-206 |
1.53e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.96 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGFVF---QDPRLLPWLTALDNI 97
Cdd:PRK13543 24 EPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAylgHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 RAV------RPETTESEAEAMlmrVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVL 171
Cdd:PRK13543 104 HFLcglhgrRAKQMPGSALAI---VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
|
170 180 190
....*....|....*....|....*....|....*
gi 2534501033 172 LTLIETNRPTvLLVTHLPEDAATVADRAVVLSGRP 206
Cdd:PRK13543 181 SAHLRGGGAA-LVTTHGAYAAPPVRTRMLTLEAAA 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-208 |
1.63e-15 |
|
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: 72.56 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 7 LEIDVEGKKfdflptpLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVD--TLFSGRVLVDGVVAAEAPP-----AG 79
Cdd:cd03217 6 LHVSVGGKE-------ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPeerarLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 80 -FV-FQDPRLLPWLTALDNIRAVRpetteseaeamlmrvglKGFeryyphelSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:cd03217 79 iFLaFQYPPEIPGVKNADFLRYVN-----------------EGF--------SGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 158 SLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATV-ADRA-VVLSGRPAK 208
Cdd:cd03217 134 GLDIDALRLVAEVINKLREEGK-SVLIITHYQRLLDYIkPDRVhVLYDGRIVK 185
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
30-209 |
1.85e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.39 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 30 EIEPSSVVALVGPSGVGKS-TLLRMIGGVDtlFSGRVLVDG------------------VVAAEAppaGFVFQDP--RLL 88
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSvSSLAIMGLID--YPGRVMAEKlefngqdlqrisekerrnLVGAEV---AMIFQDPmtSLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLT-------ALDNIRAVRPETTESEAEAMLMRVGLKGFER---YYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVS 158
Cdd:PRK11022 104 PCYTvgfqimeAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASrldVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 159 LDRTLVVEMEQVLLTLIETNRPTVLLVTHlpeDAATVADRA----------VVLSGRPAKI 209
Cdd:PRK11022 184 LDVTIQAQIIELLLELQQKENMALVLITH---DLALVAEAAhkiivmyagqVVETGKAHDI 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-205 |
2.11e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 20 PTPLLDGFRLEIEPSSVVALVGPSGVGKStlLRMIGGVDTL------FSGRVLVDGVVAAEAPPAG----FVFQDPR--L 87
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILpagvrqTAGRVLLDGKPVAPCALRGrkiaTIMQNPRsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 88 LPWLT----ALDNIRAVRPETTESEAEAMLMRVGLKGFERY---YPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:PRK10418 93 NPLHTmhthARETCLALGKPADDATLTAALEAVGLENAARVlklYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534501033 161 rtLVVEME--QVLLTLIETNRPTVLLVTHLPEDAATVADR-AVVLSGR 205
Cdd:PRK10418 173 --VVAQARilDLLESIVQKRALGMLLVTHDMGVVARLADDvAVMSHGR 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
13-190 |
2.25e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 72.30 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 13 GKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGvdtlfsgrvlvdgvVAAEAPPAGFVfqDPRLLPWLT 92
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG--------------ALKGTPVAGCV--DVPDNQFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNIRAVRPETTESEAEAMLMRVGLKG--FERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQV 170
Cdd:COG2401 99 EASLIDAIGRKGDFKDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARN 178
|
170 180
....*....|....*....|
gi 2534501033 171 LLTLIETNRPTVLLVTHLPE 190
Cdd:COG2401 179 LQKLARRAGITLVVATHHYD 198
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-220 |
2.74e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.12 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 16 FDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV------DTLFSGRVL---VDGVVAAEAPPAGfVFQDPR 86
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLlrpqkgAVLWQGKPLdysKRGLLALRQQVAT-VFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 87 LLPWLTALD--------NIRAVRPETTESEAEAMLMrVGLKGFeRYYPHE-LSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:PRK13638 88 QQIFYTDIDsdiafslrNLGVPEAEITRRVDEALTL-VDAQHF-RHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 158 SLDRTLVVEMEQVLLTLIETNRPTVL------LVTHLpEDAATVADRAVVLS-GRPAKIVADYRFASAAG 220
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIIsshdidLIYEI-SDAVYVLRQGQILThGAPGEVFACTEAMEQAG 234
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-190 |
3.10e-15 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.03 E-value: 3.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVlvdgvvaaEAPPAG---FVFQDPRLlpwltaldni 97
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEdllFLPQRPYL---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 ravrPETTESEAEAmlmrvglkgferyYP--HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvVEMEQVLLTLI 175
Cdd:cd03223 76 ----PLGTLREQLI-------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD----EESEDRLYQLL 134
|
170
....*....|....*
gi 2534501033 176 ETNRPTVLLVTHLPE 190
Cdd:cd03223 135 KELGITVISVGHRPS 149
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
23-189 |
4.51e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGG--VDTLFSGRVLVDGVVAAEA--PPAGFVFQDPRLLPWLTALDNI- 97
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQilKRTGFVTQDDILYPHLTVRETLv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 --------RAVRPETTESEAEAMLMRVGLKGFERY-----YPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLV 164
Cdd:PLN03211 163 fcsllrlpKSLTKQEKILVAESVISELGLTKCENTiignsFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180
....*....|....*....|....*
gi 2534501033 165 VEMEQVLLTLIETNRpTVLLVTHLP 189
Cdd:PLN03211 243 YRLVLTLGSLAQKGK-TIVTSMHQP 266
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
24-212 |
8.40e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.05 E-value: 8.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-VAAE-----APPAGFVFQDP-RLLPWLTALDN 96
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElLTAEnvwnlRRKIGMVFQNPdNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 I------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQV 170
Cdd:PRK13642 103 VafgmenQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 171 LLTLIETNRPTVLLVTHLPEDAATvADRAVVLsgRPAKIVAD 212
Cdd:PRK13642 183 IHEIKEKYQLTVLSITHDLDEAAS-SDRILVM--KAGEIIKE 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-215 |
1.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 19 LPTPL--LDGFRLEIEPSSVVALVGPSGVGKST--------LLRMIGGVDTLFSGRVLVDGVVAAEAPPAGFVFQDPRLl 88
Cdd:PRK13651 16 LPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTfiehlnalLLPDTGTIEWIFKDEKNKKKTKEKEKVLEKLVIQKTRF- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 pwlTALDNIRAVR---------------PETTE------------SEAEA------MLMRVGLKgfERYY---PHELSGG 132
Cdd:PRK13651 95 ---KKIKKIKEIRrrvgvvfqfaeyqlfEQTIEkdiifgpvsmgvSKEEAkkraakYIELVGLD--ESYLqrsPFELSGG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 133 MQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVLS-------GR 205
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKdgkiikdGD 248
|
250
....*....|
gi 2534501033 206 PAKIVADYRF 215
Cdd:PRK13651 249 TYDILSDNKF 258
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
9-202 |
1.91e-14 |
|
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: 72.06 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPT--PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GF 80
Cdd:TIGR02203 331 VEFRNVTFRYPGRdrPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAslrrqvAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 81 VFQDPRLLPwLTALDNIRAVRPETT-ESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPR 148
Cdd:TIGR02203 411 VSQDVVLFN-DTIANNIAYGRTEQAdRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAP 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 149 LLLLDEPFVSLDRTLVVEMEQVLLTLIEtNRpTVLLVTHlpeDAATV--ADRAVVL 202
Cdd:TIGR02203 490 ILILDEATSALDNESERLVQAALERLMQ-GR-TTLVIAH---RLSTIekADRIVVM 540
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
24-210 |
3.19e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 70.70 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVD----TLFSGRVLVDGVVAAEAPPA----------GFVFQDPR--L 87
Cdd:COG4170 23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwHVTADRFRWNGIDLLKLSPRerrkiigreiAMIFQEPSscL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 88 LPWLTALDNIRAVRPETT------------ESEAEAMLMRVGLKGFERY---YPHELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:COG4170 103 DPSAKIGDQLIEAIPSWTfkgkwwqrfkwrKKRAIELLHRVGIKDHKDImnsYPHELTEGECQKVMIAMAIANQPRLLIA 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 153 DEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL-------SGRPAKIV 210
Cdd:COG4170 183 DEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLycgqtveSGPTEQIL 247
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
9-202 |
7.19e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 69.38 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLP---TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP------PAG 79
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENvwdirhKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 80 FVFQDP-RLLPWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVafglenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 153 DEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHlPEDAATVADRAVVL 202
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDYQMTVISITH-DLDEVALSDRVLVM 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-208 |
8.53e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 8.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSS-----VVALVGPSGVGKSTLLRMIGGVdtlfsgrvlvdgvvaaEAPPAGFVFQDPRLL---------P 89
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGV----------------LKPDEGEVDPELKISykpqyikpdY 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 90 WLTALDNIRAVRPETTESEAEAMLMR-VGL-KGFERYYPhELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvVEm 167
Cdd:PRK13409 414 DGTVEDLLRSITDDLGSSYYKSEIIKpLQLeRLLDKNVK-DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----VE- 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2534501033 168 EQVLLT-----LIETNRPTVLLVTHlpeDAA---TVADRAVVLSGRPAK 208
Cdd:PRK13409 488 QRLAVAkairrIAEEREATALVVDH---DIYmidYISDRLMVFEGEPGK 533
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-205 |
1.16e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 25 DGFRLEIEPSSVVALVGPSGVGKS----TLLRMI--------GGvDTLFSGRVLVDgvvAAEAPPAG-------FVFQDP 85
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsppvvypSG-DIRFHGESLLH---ASEQTLRGvrgnkiaMIFQEP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 86 rlLPWLTALDNI-----------RAVRPETTESEAEAMLMRVGLKGFERY---YPHELSGGMQRRVALARAFSVNPRLLL 151
Cdd:PRK15134 102 --MVSLNPLHTLekqlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 152 LDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADR-AVVLSGR 205
Cdd:PRK15134 180 ADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRvAVMQNGR 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-188 |
1.16e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.66 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 31 IEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVD------GVVAAEAPPAGFVFQDP-----------RLLPWLTA 93
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdhplhfGDYSYRSQRIRMIFQDPstslnprqrisQILDFPLR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNirAVRPETTESEAEAMLMRVGLK-GFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLL 172
Cdd:PRK15112 116 LNT--DLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLML 193
|
170
....*....|....*..
gi 2534501033 173 TLIETNRPTVLLVT-HL 188
Cdd:PRK15112 194 ELQEKQGISYIYVTqHL 210
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-202 |
1.24e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.60 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV------VAAEAPPAGFVFQDPRLLPwLTALD 95
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTdirtvtRASLRRNIAVVFQDAGLFN-RSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NIRAVRPETTESE-------AEAM-LMRVGLKGF-----ERyyPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:PRK13657 428 NIRVGRPDATDEEmraaaerAQAHdFIERKPDGYdtvvgER--GRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 163 LVVEMEQVLLTLIEtNRPTVLLVTHLpedaATV--ADRAVVL 202
Cdd:PRK13657 506 TEAKVKAALDELMK-GRTTFIIAHRL----STVrnADRILVF 542
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-189 |
1.68e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLL-----RMIGGVDtlFSGRVLVDGVVAaEAPP----AGFVFQDPRLLPWLTA 93
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVK--GSGSVLLNGMPI-DAKEmraiSAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNI---------RAVRPETTESEAEAMLMRVGL--------------KGferyypheLSGGMQRRVALARAFSVNPRLL 150
Cdd:TIGR00955 117 REHLmfqahlrmpRRVTKKEKRERVDEVLQALGLrkcantrigvpgrvKG--------LSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534501033 151 LLDEPFVSLDRTLVVEMEQVLLTLiETNRPTVLLVTHLP 189
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQP 226
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
22-187 |
2.76e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 68.81 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGrvlvdgvvaaEAPPA-----GFVFQDPRLLPWLTALDN 96
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------EARPQpgikvGYLPQEPQLDPTKTVREN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IRAVRPE--------------------------TTESEAEAMLMRVGLKGFE----------RYYPHE-----LSGGMQR 135
Cdd:TIGR03719 89 VEEGVAEikdaldrfneisakyaepdadfdklaAEQAELQEIIDAADAWDLDsqleiamdalRCPPWDadvtkLSGGERR 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 136 RVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLltliETNRPTVLLVTH 187
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTH 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
24-176 |
4.23e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.79 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVdTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWLT----- 92
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAelarhrAYLSQQQSPPFAMPvfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNIRAVRPETTESEAEAMLMRVGLkgfERYYP---HELSGGMQRRVALARAF-----SVNP--RLLLLDEPFVSLDrt 162
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLAEALGL---EDKLSrplTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLD-- 165
|
170
....*....|....
gi 2534501033 163 lvVEMEQVLLTLIE 176
Cdd:COG4138 166 --VAQQAALDRLLR 177
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-208 |
6.59e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 67.50 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEP-----SSVVALVGPSGVGKSTLLRMIGGVdtlfsgrvlvdgvvaaEAPPAGFVFQDPRLL--PW------ 90
Cdd:COG1245 351 YGGFSLEVEGgeireGEVLGIVGPNGIGKTTFAKILAGV----------------LKPDEGEVDEDLKISykPQyispdy 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 -LTALDNIRAVRPETTES---EAEaMLMRVGLKG-FERYYPhELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvV 165
Cdd:COG1245 415 dGTVEEFLRSANTDDFGSsyyKTE-IIKPLGLEKlLDKNVK-DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD----V 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 166 EmEQVLLT-----LIETNRPTVLLVTHlpeDAAT---VADRAVVLSGRPAK 208
Cdd:COG1245 489 E-QRLAVAkairrFAENRGKTAMVVDH---DIYLidyISDRLMVFEGEPGV 535
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
14-205 |
6.67e-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: 67.73 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 14 KKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-----VAAEAPPAGFVFQDPRLL 88
Cdd:TIGR01257 936 KIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnLDAVRQSLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 PWLTALDNI------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:TIGR01257 1016 HHLTVAEHIlfyaqlKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2534501033 163 LVVEMEQVLLTLiETNRpTVLLVTHLPEDAATVADR-AVVLSGR 205
Cdd:TIGR01257 1096 SRRSIWDLLLKY-RSGR-TIIMSTHHMDEADLLGDRiAIISQGR 1137
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-204 |
1.04e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGF---VFQDPRLL----------- 88
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFarkVAYLPQQLpaaegmtvrel 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 89 ------PWLTALDNIRAVRPETTEsEAEAMlmrVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:PRK10575 106 vaigryPWHGALGRFGAADREKVE-EAISL---VGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 163 LVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:PRK10575 182 HQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRG 223
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-174 |
1.18e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 33 PSSVVALVGPSGVGKST----LLRMI--GGVDTLFSGR---VLVDGVVAAEAPPAGFVFQDP--RLLPWLTALDNI---- 97
Cdd:PRK10261 349 PGETLSLVGESGSGKSTtgraLLRLVesQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyaSLDPRQTVGDSImepl 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 ---RAVRPETTESEAEAMLMRVGLKGFERY-YPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLT 173
Cdd:PRK10261 429 rvhGLLPGKAAAARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
.
gi 2534501033 174 L 174
Cdd:PRK10261 509 L 509
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-176 |
1.24e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.49 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV--------DTLFSGRVLV-DGVVAAEAPPAGFVFQDPRLLPWLTAL 94
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVyphgtyegEIIFEGEELQaSNIRDTERAGIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNI---RAVRP------ETTESEAEAMLMRVGLkGFERYYP-HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLdrtlv 164
Cdd:PRK13549 101 ENIflgNEITPggimdyDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEIAKALNKQARLLILDEPTASL----- 174
|
170
....*....|...
gi 2534501033 165 VEME-QVLLTLIE 176
Cdd:PRK13549 175 TESEtAVLLDIIR 187
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
9-187 |
1.57e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.20 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVL-----VDGVVAAEAPPAGFVFQ 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILferqsIKKDLCTYQKQLCFVGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 84 DPRLLPWLTALDN-IRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:PRK13540 82 RSGINPYLTLRENcLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDEL 161
|
170 180
....*....|....*....|....*...
gi 2534501033 163 LVvemeQVLLTLIETNRP---TVLLVTH 187
Cdd:PRK13540 162 SL----LTIITKIQEHRAkggAVLLTSH 185
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
21-212 |
2.07e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.01 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP-------AGFVFQDPRLLPWLTA 93
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlqgirklVGIVFQNPETQFVGRT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 LDNIRAVRPET-------TESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVE 166
Cdd:PRK13644 95 VEEDLAFGPENlclppieIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 167 MEQVLLTLIETNRpTVLLVTHLPE-----DAATVADRA-VVLSGRPAKIVAD 212
Cdd:PRK13644 175 VLERIKKLHEKGK-TIVYITHNLEelhdaDRIIVMDRGkIVLEGEPENVLSD 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
29-205 |
2.40e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.56 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV---DGVVA--AEAPPA----------GFVFQDPR--LLPWL 91
Cdd:PRK11701 27 FDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRdlYALSEAerrrllrtewGFVHQHPRdgLRMQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDNIravrpetteseAEAmLMRVGlkgfERYY------------------------PHELSGGMQRRVALARAFSVNP 147
Cdd:PRK11701 107 SAGGNI-----------GER-LMAVG----ARHYgdiratagdwlerveidaariddlPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 148 RLLLLDEPFVSLD-----------RTLVVEMeqvlltlietnRPTVLLVTHLPEDAATVADRAVVL-SGR 205
Cdd:PRK11701 171 RLVFMDEPTGGLDvsvqarlldllRGLVREL-----------GLAVVIVTHDLAVARLLAHRLLVMkQGR 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
24-202 |
3.68e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.64 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV-DGVVAAEAPP----------AGFVFQDPRLLPWLT 92
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLKKikevkrlrkeIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNIRAVRP-ETTESEAEA------MLMRVGL-KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLV 164
Cdd:PRK13645 107 TIEKDIAFGPvNLGENKQEAykkvpeLLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186
|
170 180 190
....*....|....*....|....*....|....*...
gi 2534501033 165 VEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK13645 187 EDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVM 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-202 |
4.85e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 14 KKFDFLPTplLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV--------DTLFSGRVLV-DGVVAAEAPPAGFVFQD 84
Cdd:TIGR02633 9 KTFGGVKA--LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVyphgtwdgEIYWSGSPLKaSNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 85 PRLLPWLTALDNI-----------RAVRPETTEsEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:TIGR02633 87 LTLVPELSVAENIflgneitlpggRMAYNAMYL-RAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 153 DEPFVSLDRTLVvemeQVLLTLI---ETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:TIGR02633 166 DEPSSSLTEKET----EILLDIIrdlKAHGVACVYISHKLNEVKAVCDTICVI 214
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
30-187 |
6.34e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 30 EIEPSSVVALVGPSGVGKSTLLRMIGGVdTLFSGRVLVDGVVAAEAPPAGF------------------VFQDPRL-LPW 90
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELarhraylsqqqtppfampVFQYLTLhQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 91 LTALDNIRAVRPETTEseaeamlmRVGLKGFERYYPHELSGGMQRRVALARAF-----SVNP--RLLLLDEPFVSLDRTL 163
Cdd:PRK03695 97 KTRTEAVASALNEVAE--------ALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQ 168
|
170 180
....*....|....*....|....
gi 2534501033 164 VVEMEQVLLTLIETNRpTVLLVTH 187
Cdd:PRK03695 169 QAALDRLLSELCQQGI-AVVMSSH 191
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
24-202 |
7.11e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 63.65 E-value: 7.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPP----------AGFVFQDPRllpwlTA 93
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirpvrkrIGMVFQFPE-----SQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 94 L--DNIR----------AVRPETTESEAEAMLMRVGlkgFER----YYPHELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:PRK13646 98 LfeDTVEreiifgpknfKMNLDEVKNYAHRLLMDLG---FSRdvmsQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2534501033 158 SLD---RTLVVEMEQVLltLIETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK13646 175 GLDpqsKRQVMRLLKSL--QTDENK-TIILVSHDMNEVARYADEVIVM 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-155 |
7.48e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG-VVAAEAPPA------GFVFQDPRLLPWLTALDN 96
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkEVTFNGPKSsqeagiGIIHQELNLIPQLTIAEN 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 97 IRAVRPETTE----------SEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:PRK10762 100 IFLGREFVNRfgridwkkmyAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEP 168
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
24-202 |
8.81e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.57 E-value: 8.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA-----GFVF-QDPRLLPWLTALD-- 95
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEfarriGVVFgQRSQLWWDLPAIDsf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 -------NIRAVRPETTESEAEAMLmrvGLKGFERYYPHELSGGmQR-RVALARAFSVNPRLLLLDEPFVSLDrtlVVEM 167
Cdd:COG4586 118 rllkaiyRIPDAEYKKRLDELVELL---DLGELLDTPVRQLSLG-QRmRCELAAALLHRPKILFLDEPTIGLD---VVSK 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 2534501033 168 EQVLLTLIETNRP---TVLLVTHLPEDAATVADRAVVL 202
Cdd:COG4586 191 EAIREFLKEYNRErgtTILLTSHDMDDIEALCDRVIVI 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-160 |
1.13e-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: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 4 GPRLE---IDVEG--KKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVdgvvaAEAPPA 78
Cdd:TIGR03719 315 GPRLGdkvIEAENltKAFG--DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-----GETVKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 GFVFQ-----DPRLLPWLTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:TIGR03719 388 AYVDQsrdalDPNKTVWEEISGGLDIIKLGKREIPSRAYVGRFNFKGSDQQKKvGQLSGGERNRVHLAKTLKSGGNVLLL 467
|
....*...
gi 2534501033 153 DEPFVSLD 160
Cdd:TIGR03719 468 DEPTNDLD 475
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-213 |
1.16e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.67 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTL--FSGRVL-------------VDGVVAA 73
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyveRPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 74 EAPPAGFVFQDPRLLPW---------------------------LTALDNIRAVRPETTESEAEAMLMRVGL---KGFER 123
Cdd:TIGR03269 81 PCPVCGGTLEPEEVDFWnlsdklrrrirkriaimlqrtfalygdDTVLDNVLEALEEIGYEGKEAVGRAVDLiemVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 124 YYPH---ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAV 200
Cdd:TIGR03269 161 RITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|
gi 2534501033 201 VLS-------GRPAKIVADY 213
Cdd:TIGR03269 241 WLEngeikeeGTPDEVVAVF 260
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-187 |
1.56e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 39 LVGPSGVGKSTLLRMIGGVDTLFSGrvlvdgvvaaEAPPA-----GFVFQDPRLLPWLTALDNIRAVRPETTESEAE--- 110
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG----------EARPApgikvGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRfne 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 111 -AMLMRVGLKGFE--------------------------------RYYPHE-----LSGGMQRRVALARAFSVNPRLLLL 152
Cdd:PRK11819 108 iYAAYAEPDADFDalaaeqgelqeiidaadawdldsqleiamdalRCPPWDakvtkLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190
....*....|....*....|....*....|....*.
gi 2534501033 153 DEPFVSLDRTLVVEMEQVLltlieTNRP-TVLLVTH 187
Cdd:PRK11819 188 DEPTNHLDAESVAWLEQFL-----HDYPgTVVAVTH 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
39-205 |
1.71e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.82 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 39 LVGPSGVGKST-------LLR---MIGGvDTLFSGRVLVD------GVVAAEAppAGFVFQDPrllpwLTALDNIRAVRP 102
Cdd:PRK09473 47 IVGESGSGKSQtafalmgLLAangRIGG-SATFNGREILNlpekelNKLRAEQ--ISMIFQDP-----MTSLNPYMRVGE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 103 ETTE--------SEAEA------MLMRVGL---KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVV 165
Cdd:PRK09473 119 QLMEvlmlhkgmSKAEAfeesvrMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2534501033 166 EMEQVLLTLIETNRPTVLLVTHlpeDAATVA---DRAVVL-SGR 205
Cdd:PRK09473 199 QIMTLLNELKREFNTAIIMITH---DLGVVAgicDKVLVMyAGR 239
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-205 |
2.84e-11 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 60.97 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKST----LLRMIggvdTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPwl 91
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLV----ELSSGSILIDGVDISKIGLHdlrsriSIIPQDPVLFS-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 talDNIRA-VRPETTESEAE--AMLMRVGLKGFERYYP-----HELSGGM-----QRR-VALARAFSVNPRLLLLDEPFV 157
Cdd:cd03244 92 ---GTIRSnLDPFGEYSDEElwQALERVGLKEFVESLPggldtVVEEGGEnlsvgQRQlLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 158 SLDrtlvVEMEQVLLTLIETNRP--TVLLVTH-LPedaaTVA--DRAVVL-SGR 205
Cdd:cd03244 169 SVD----PETDALIQKTIREAFKdcTVLTIAHrLD----TIIdsDRILVLdKGR 214
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
108-202 |
3.78e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.57 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 108 EAEAMLMRvglkgferyYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTH 187
Cdd:PRK10261 157 EAQTILSR---------YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITH 227
|
90
....*....|....*
gi 2534501033 188 LPEDAATVADRAVVL 202
Cdd:PRK10261 228 DMGVVAEIADRVLVM 242
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
7-189 |
4.76e-11 |
|
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: 62.07 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 7 LEIDVEGKKFDFLP--TP----LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVdgvvaaeaPPAGF 80
Cdd:TIGR00954 445 VEYQDNGIKFENIPlvTPngdvLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTK--------PAKGK 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 81 VFQDPRlLPWLTaLDNIR--AVRPETTE---------SEAEAMLMRVGLK-------GFE--RYYPHELSGGMQRRVALA 140
Cdd:TIGR00954 517 LFYVPQ-RPYMT-LGTLRdqIIYPDSSEdmkrrglsdKDLEQILDNVQLThileregGWSavQDWMDVLSGGEKQRIAMA 594
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 141 RAFSVNPRLLLLDE--PFVSldrtlvVEMEQVLLTLIETNRPTVLLVTHLP 189
Cdd:TIGR00954 595 RLFYHKPQFAILDEctSAVS------VDVEGYMYRLCREFGITLFSVSHRK 639
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-179 |
6.02e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 6.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAG-------FVFQDPRLLPWLTAL 94
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKahqlgiyLVPQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNI--RAVRPETTESEAEAMLMRVG--LKgferyyPHELSGGM----QRRVALARAFSVNPRLLLLDEPFVSldrtlvve 166
Cdd:PRK15439 105 ENIlfGLPKRQASMQKMKQLLAALGcqLD------LDSSAGSLevadRQIVEILRGLMRDSRILILDEPTAS-------- 170
|
170
....*....|...
gi 2534501033 167 meqvlLTLIETNR 179
Cdd:PRK15439 171 -----LTPAETER 178
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-192 |
1.01e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.80 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGvD---------TLF-----SGRVLVD-----GVVAAEappagfVF 82
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DhpqgysndlTLFgrrrgSGETIWDikkhiGYVSSS------LH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 83 QDPRLLpwLTALDNI-----------RAVrPETTESEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLL 150
Cdd:PRK10938 347 LDYRVS--TSVRNVIlsgffdsigiyQAV-SDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLL 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 151 LLDEPFVSLD---RTLVVEMEQVLLTLIETNrptVLLVTHLPEDA 192
Cdd:PRK10938 424 ILDEPLQGLDplnRQLVRRFVDVLISEGETQ---LLFVSHHAEDA 465
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
22-203 |
1.05e-10 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 61.29 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------GFVFQDPRLLPWlTALD 95
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHtlrqfiNYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 N-IRAVRPETTESEAEAML----MRVGLKGFERYYPHEL-------SGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtl 163
Cdd:TIGR01193 567 NlLLGAKENVSQDEIWAACeiaeIKDDIENMPLGYQTELseegssiSGGQKQRIALARALLTDSKVLILDESTSNLD--- 643
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2534501033 164 VVEMEQVLLTLIETNRPTVLLVTHLPEdAATVADRAVVLS 203
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDKTIIFVAHRLS-VAKQSDKIIVLD 682
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-195 |
1.06e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.08 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 3 SGPRLEIDVEGKKFdflptP---LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVV-----AAE 74
Cdd:PRK11288 1 SSPYLSFDGIGKTF-----PgvkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 75 APPAG--FVFQDPRLLPWLTALDNI-------RA--VRPETTESEAEAMLMRVGlkgfERYYPH----ELSGGMQRRVAL 139
Cdd:PRK11288 76 ALAAGvaIIYQELHLVPEMTVAENLylgqlphKGgiVNRRLLNYEAREQLEHLG----VDIDPDtplkYLSIGQRQMVEI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 140 ARAFSVNPRLLLLDEPFVSLDrtlVVEMEQvLLTLIETNRP---TVLLVTHLPE------DAATV 195
Cdd:PRK11288 152 AKALARNARVIAFDEPTSSLS---AREIEQ-LFRVIRELRAegrVILYVSHRMEeifalcDAITV 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-202 |
1.27e-10 |
|
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: 61.18 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGrvlvDGVVAAEAPPAGF--VFQDPRLLPWLTALDNI- 97
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSG----DATVAGKSILTNIsdVHQNMGYCPQFDAIDDLl 2027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 ------------RAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVV 165
Cdd:TIGR01257 2028 tgrehlylyarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
|
170 180 190
....*....|....*....|....*....|....*..
gi 2534501033 166 EMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:TIGR01257 2108 MLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIM 2143
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-159 |
1.28e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 5 PRLEIDVEGKKFDflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA------ 78
Cdd:PRK09700 4 PYISMAGIGKSFG--PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlaaqlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 -GFVFQDPRLLPWLTALDNIRAVRPETTE-------------SEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFS 144
Cdd:PRK09700 82 iGIIYQELSVIDELTVLENLYIGRHLTKKvcgvniidwremrVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170
....*....|....*
gi 2534501033 145 VNPRLLLLDEPFVSL 159
Cdd:PRK09700 162 LDAKVIIMDEPTSSL 176
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
24-202 |
1.36e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 60.57 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGV--------DTLFSGRVL-VDGVVAAEAppAGFVF--QDPRLLPWLT 92
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVyphgsyegEILFDGEVCrFKDIRDSEA--LGIVIihQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNI-----RAVRP----ETTESEAEAMLMRVGLKgfERyyPHELSG----GMQRRVALARAFSVNPRLLLLDEPFVSL 159
Cdd:NF040905 95 IAENIflgneRAKRGvidwNETNRRARELLAKVGLD--ES--PDTLVTdigvGKQQLVEIAKALSKDVKLLILDEPTAAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2534501033 160 DRtlvvEMEQVLLTLIETNRP---TVLLVTHLPEDAATVADRAVVL 202
Cdd:NF040905 171 NE----EDSAALLDLLLELKAqgiTSIIISHKLNEIRRVADSITVL 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
21-204 |
1.85e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 59.26 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG-VVAAEAP----------------PAGFVFQ 83
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkPISMLSSrqlarrlallpqhhltPEGITVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 84 D-------PRLLPW--LTALDNIRAvrpetteseAEAMlMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDE 154
Cdd:PRK11231 95 ElvaygrsPWLSLWgrLSAEDNARV---------NQAM-EQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2534501033 155 PFVSLDRTLVVEMEQvLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:PRK11231 165 PTTYLDINHQVELMR-LMRELNTQGKTVVTVLHDLNQASRYCDHLVVLAN 213
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
7-211 |
2.51e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 58.54 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 7 LEID-----VEGKkfdflptPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVD--TLFSGRVLVDGVVAAEAPP-- 77
Cdd:COG0396 1 LEIKnlhvsVEGK-------EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPde 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 78 ---AG-FV-FQDP---------RLLpwLTALDNIR--AVRPETTESEAEAMLMRVGL-KGF-ERYYPHELSGGMQRRVAL 139
Cdd:COG0396 74 rarAGiFLaFQYPveipgvsvsNFL--RTALNARRgeELSAREFLKLLKEKMKELGLdEDFlDRYVNEGFSGGEKKRNEI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534501033 140 ARAFSVNPRLLLLDEPFVSLD----RTLVvemeQVLLTLIETNRpTVLLVTHLPE--DaATVADRAVVLSGrpAKIVA 211
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLDidalRIVA----EGVNKLRSPDR-GILIITHYQRilD-YIKPDFVHVLVD--GRIVK 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
38-202 |
2.51e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.99 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 38 ALVGPSGVGKSTLLRMIGGVDTLFSGRVLV-DGVVAAE-----APPAGFVFQDPR------LLPWLTA--LDNiRAVRPE 103
Cdd:PRK13648 39 SIVGHNGSGKSTIAKLMIGIEKVKSGEIFYnNQAITDDnfeklRKHIGIVFQNPDnqfvgsIVKYDVAfgLEN-HAVPYD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 104 TTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRtlvvEMEQVLLTLI----ETNR 179
Cdd:PRK13648 118 EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP----DARQNLLDLVrkvkSEHN 193
|
170 180
....*....|....*....|....
gi 2534501033 180 PTVLLVTH-LPEdaATVADRAVVL 202
Cdd:PRK13648 194 ITIISITHdLSE--AMEADHVIVM 215
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
27-208 |
3.61e-10 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 57.20 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 27 FRLEIEP-----SSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAeappagfvfqdprllpwltaldniraVR 101
Cdd:cd03222 13 FFLLVELgvvkeGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV--------------------------YK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 102 PETTEseaeamlmrvglkgferyypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPT 181
Cdd:cd03222 67 PQYID----------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKT 124
|
170 180
....*....|....*....|....*..
gi 2534501033 182 VLLVTHLPEDAATVADRAVVLSGRPAK 208
Cdd:cd03222 125 ALVVEHDLAVLDYLSDRIHVFEGEPGV 151
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
35-204 |
3.89e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 58.36 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 35 SVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGFVFQDPRL------LPWLTA----------LDNIR 98
Cdd:PRK15056 34 SIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSeevdwsFPVLVEdvvmmgryghMGWLR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 99 AVRPETTESEAEAmLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvVEMEQVLLTLIETN 178
Cdd:PRK15056 114 RAKKRDRQIVTAA-LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD----VKTEARIISLLREL 188
|
170 180
....*....|....*....|....*....
gi 2534501033 179 RP---TVLLVTHLPEDAATVADRAVVLSG 204
Cdd:PRK15056 189 RDegkTMLVSTHNLGSVTEFCDYTVMVKG 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-187 |
5.21e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.82 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAeappaGFVFQDPRLLPWLT-ALDNIRAVR 101
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRI-----GYVPQKLYLDTTLPlTVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 102 PETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvVEMEQVLLTLIETNRPT 181
Cdd:PRK09544 94 PGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD----VNGQVALYDLIDQLRRE 169
|
170
....*....|
gi 2534501033 182 ----VLLVTH 187
Cdd:PRK09544 170 ldcaVLMVSH 179
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
24-202 |
6.03e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 57.58 E-value: 6.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGFVFQDPRLLPwltaldNIRAVRPE 103
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVP------EGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 104 TTESEAEAM-------------LMRVgLKGFERYYPHE------LSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLV 164
Cdd:PRK11614 95 MTVEENLAMggffaerdqfqerIKWV-YELFPRLHERRiqragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 2534501033 165 VEMEQVLLTLIETNRpTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK11614 174 QQIFDTIEQLREQGM-TIFLVEQNANQALKLADRGYVL 210
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-204 |
6.44e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.80 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 1 MSSGPRLEIDVEGKKFDF---LPtPLLDGFRLEIEPSSVVALVGPSGVGKSTLLR-MIGGVDTLfSGRVLVDGVVAAeAP 76
Cdd:TIGR00957 629 IKPGEGNSITVHNATFTWardLP-PTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVHMKGSVAY-VP 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 77 PAGFVFQDprllpwlTALDNI---RAVRPETTES--EAEAML-----------MRVGLKGFEryypheLSGGMQRRVALA 140
Cdd:TIGR00957 706 QQAWIQND-------SLRENIlfgKALNEKYYQQvlEACALLpdleilpsgdrTEIGEKGVN------LSGGQKQRVSLA 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 141 RAFSVNPRLLLLDEPFVSLDRTLVVEM-EQVLLTLIETNRPTVLLVTH----LPEdaatvADRAVVLSG 204
Cdd:TIGR00957 773 RAVYSNADIYLFDDPLSAVDAHVGKHIfEHVIGPEGVLKNKTRILVTHgisyLPQ-----VDVIIVMSG 836
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
8-189 |
9.11e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 56.48 E-value: 9.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 8 EIDVEGKKfdflpTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDT--LFSGRVLVDG--VVAAEAPPAGFVFQ 83
Cdd:cd03232 12 TVPVKGGK-----RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGrpLDKNFQRSTGYVEQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 84 DPRLLPWLTaldniraVRpetteseaEAMLMRVGLKGferyypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL 163
Cdd:cd03232 87 QDVHSPNLT-------VR--------EALRFSALLRG--------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|....*.
gi 2534501033 164 VVEMEQVLLTLIETNRpTVLLVTHLP 189
Cdd:cd03232 144 AYNIVRFLKKLADSGQ-AILCTIHQP 168
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
33-191 |
9.67e-10 |
|
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: 55.46 E-value: 9.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 33 PSSVVALVGPSGVGKSTLLRMIggvdtlfsgrvlvdgvvAAEAPPAGFvfqdprllpwltaldNIRAVRPETTESEAEAM 112
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARAL-----------------ARELGPPGG---------------GVIYIDGEDILEEVLDQ 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 113 LMRVGLKGferyYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT-----LVVEMEQVLLTLIETNRPTVLLVTH 187
Cdd:smart00382 49 LLLIIVGG----KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLLLLKSEKNLTVILTTN 124
|
....
gi 2534501033 188 LPED 191
Cdd:smart00382 125 DEKD 128
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
22-187 |
1.63e-09 |
|
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: 56.19 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP----------PAGFVFQDPRLLPwL 91
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSfeatrsrnrySVAYAAQKPWLLN-A 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDNIRAVRPeTTESEAEAMLMRVGLKGFERYYPH-----------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:cd03290 94 TVEENITFGSP-FNKQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180
....*....|....*....|....*...
gi 2534501033 161 RTLVVE-MEQVLLTLIETNRPTVLLVTH 187
Cdd:cd03290 173 IHLSDHlMQEGILKFLQDDKRTLVLVTH 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
36-241 |
2.06e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.95 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 36 VVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVA-----AEAPPAGFVF--QDPR---LLPWLTALDNI-------- 97
Cdd:COG1129 280 ILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrirspRDAIRAGIAYvpEDRKgegLVLDLSIRENItlasldrl 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 ---RAVRPETTESEAEAMLMRVGLKgferyYPH------ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlV---V 165
Cdd:COG1129 360 srgGLLDRRRERALAEEYIKRLRIK-----TPSpeqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID---VgakA 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2534501033 166 EMEQVLLTLIETNRpTVLLVT-HLPEdAATVADRAVVLSGRpaKIVADYRfasaagqRPRAEREHIANQIAGAAAER 241
Cdd:COG1129 432 EIYRLIRELAAEGK-AVIVISsELPE-LLGLSDRILVMREG--RIVGELD-------REEATEEAIMAAATGGAAAA 497
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
30-202 |
2.41e-09 |
|
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: 55.99 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 30 EIEPSSVVALVGPSGVGKSTLLRMI--------GGVDTLFSGRVLVDGVVAAEAPPA-------GFVFQDPR--LLPWLT 92
Cdd:TIGR02323 25 DLYPGEVLGIVGESGSGKSTLLGCLagrlapdhGTATYIMRSGAELELYQLSEAERRrlmrtewGFVHQNPRdgLRMRVS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNIrAVRPETT--------ESEAEAMLMRVGL-KGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTL 163
Cdd:TIGR02323 105 AGANI-GERLMAIgarhygniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSV 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 2534501033 164 VVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVL 202
Cdd:TIGR02323 184 QARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVM 222
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
9-160 |
3.21e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 9 IDVEGKKFDF---LPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLR-MIGGVDTLFSGRVLVDGVVAAeAPPAGFVFQd 84
Cdd:PLN03232 615 ISIKNGYFSWdskTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSVAY-VPQVSWIFN- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 85 prllpwLTALDNI------------RAVRPETTESEAEAM----LMRVGLKGFEryypheLSGGMQRRVALARAFSVNPR 148
Cdd:PLN03232 693 ------ATVRENIlfgsdfeserywRAIDVTALQHDLDLLpgrdLTEIGERGVN------ISGGQKQRVSMARAVYSNSD 760
|
170
....*....|..
gi 2534501033 149 LLLLDEPFVSLD 160
Cdd:PLN03232 761 IYIFDDPLSALD 772
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
8-202 |
4.48e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 54.73 E-value: 4.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 8 EIDVEGKKFDFLP--TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAP------PAG 79
Cdd:cd03369 6 EIEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPledlrsSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 80 FVFQDPRLLpwltaLDNIRA-VRPETTESEAEAM-LMRVGLKGferyypHELSGGMQRRVALARAFSVNPRLLLLDEPFV 157
Cdd:cd03369 86 IIPQDPTLF-----SGTIRSnLDPFDEYSDEEIYgALRVSEGG------LNLSQGQRQLLCLARALLKRPRVLVLDEATA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 158 SLDRTLVVEMEQVLLTliETNRPTVLLVTHlpeDAATVADRAVVL 202
Cdd:cd03369 155 SIDYATDALIQKTIRE--EFTNSTILTIAH---RLRTIIDYDKIL 194
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
21-204 |
5.42e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLF---SGRVLVDGVVAAEAPP-----AGFVFQDPRLLPWLT 92
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEkypgeIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 aldniraVRpETTESEAEamlmrvgLKGFEryYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLL 172
Cdd:cd03233 100 -------VR-ETLDFALR-------CKGNE--FVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIR 162
|
170 180 190
....*....|....*....|....*....|...
gi 2534501033 173 TLI-ETNRPTVLLVTHLPEDAATVADRAVVLSG 204
Cdd:cd03233 163 TMAdVLKTTTFVSLYQASDEIYDLFDKVLVLYE 195
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-160 |
1.14e-08 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 55.11 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 1 MSSGprlEIDVEGKKFDFLP-TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA- 78
Cdd:PRK10790 336 LQSG---RIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSv 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 -----GFVFQDPRLLPwLTALDNIRAVRpETTESEAEAMLMRVGLKGFERYYP-----------HELSGGMQRRVALARA 142
Cdd:PRK10790 413 lrqgvAMVQQDPVVLA-DTFLANVTLGR-DISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARV 490
|
170
....*....|....*...
gi 2534501033 143 FSVNPRLLLLDEPFVSLD 160
Cdd:PRK10790 491 LVQTPQILILDEATANID 508
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
112-202 |
1.29e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 112 MLMRVGLKGFE---RYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHL 188
Cdd:PRK15093 139 LLHRVGIKDHKdamRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHD 218
|
90
....*....|....
gi 2534501033 189 PEDAATVADRAVVL 202
Cdd:PRK15093 219 LQMLSQWADKINVL 232
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-214 |
1.43e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 6 RLEIDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRvlvdgVVAAEAPPAGFVFQDP 85
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-----VKWSENANIGYYAQDH 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 86 --------RLLPWL----TALDNIRAVRpetteseaeAMLMRVGLKGFE-RYYPHELSGGMQRRVALARAFSVNPRLLLL 152
Cdd:PRK15064 392 aydfendlTLFDWMsqwrQEGDDEQAVR---------GTLGRLLFSQDDiKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 153 DEPFVSLDrtlvveMEQV--LLTLIETNRPTVLLVTHLPEDAATVADRavVLSGRPAKIVaDYR 214
Cdd:PRK15064 463 DEPTNHMD------MESIesLNMALEKYEGTLIFVSHDREFVSSLATR--IIEITPDGVV-DFS 517
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
31-187 |
1.96e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.48 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 31 IEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVL----VDGVVAAEAPPAGFVFQDPRLLPWLTALdniravrPETTE 106
Cdd:PLN03073 532 IDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsakVRMAVFSQHHVDGLDLSSNPLLYMMRCF-------PGVPE 604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 107 SEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLietnRPTVLLV 185
Cdd:PLN03073 605 QKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLF----QGGVLMV 680
|
..
gi 2534501033 186 TH 187
Cdd:PLN03073 681 SH 682
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
23-212 |
2.48e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGG--VDTLFSGRVLVDGVVAAEAPPAGFVfqDPRLLPWLtaldniRAV 100
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAI--DAPRLARL------RAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 101 RPETTESE------------------------------AEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFS------ 144
Cdd:PRK13547 88 LPQAAQPAfafsareivllgrypharragalthrdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 145 ---VNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLSGrpAKIVAD 212
Cdd:PRK13547 168 daaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLAD--GAIVAH 236
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
33-202 |
3.12e-08 |
|
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: 51.59 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 33 PSSVVALVGPSGVGKSTLLRMIGgvdtlfsgrvlvdgVVAAEAPPAGFVFQDPrllpwltaldnirAVRPETTESEAEAM 112
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAIG--------------LALGGAQSATRRRSGV-------------KAGCIVAAVSAELI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 113 LMRVGLkgferyyphelSGGMQRRVALARAF---SVNPR-LLLLDEPFVSLDRtlvvEMEQVLLTLIETNR---PTVLLV 185
Cdd:cd03227 73 FTRLQL-----------SGGEKELSALALILalaSLKPRpLYILDEIDRGLDP----RDGQALAEAILEHLvkgAQVIVI 137
|
170
....*....|....*..
gi 2534501033 186 THLPEdaatVADRAVVL 202
Cdd:cd03227 138 THLPE----LAELADKL 150
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
33-189 |
3.68e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 3.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 33 PSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG--VVAAEAPPAGFVFQDPRLLPWLTALDNIRAVRPETTESEA- 109
Cdd:PRK13541 25 PSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcnINNIAKPYCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETl 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 110 EAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRtlvvEMEQVL--LTLIETNR-PTVLLVT 186
Cdd:PRK13541 105 YAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSK----ENRDLLnnLIVMKANSgGIVLLSS 180
|
...
gi 2534501033 187 HLP 189
Cdd:PRK13541 181 HLE 183
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-188 |
5.13e-08 |
|
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: 53.38 E-value: 5.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 16 FDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAaeappagFVFQDPRLLPWlTALD 95
Cdd:TIGR01271 434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRIS-------FSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NI---------------RAVRPETTES----EAEAMLMRVGLKgferyypheLSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:TIGR01271 506 NIifglsydeyrytsviKACQLEEDIAlfpeKDKTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPF 576
|
170 180 190
....*....|....*....|....*....|..
gi 2534501033 157 VSLDRTLVVEMEQVLLTLIETNRPTVLLVTHL 188
Cdd:TIGR01271 577 THLDVVTEKEIFESCLCKLMSNKTRILVTSKL 608
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-160 |
6.44e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 4 GPRLE---IDVEG--KKF-DFLptpLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV-DGVVAAeap 76
Cdd:PRK11819 317 GPRLGdkvIEAENlsKSFgDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLA--- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 77 pagFVFQ-----DPRLLPWLT---ALDNIRAvrpETTESEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNP 147
Cdd:PRK11819 391 ---YVDQsrdalDPNKTVWEEisgGLDIIKV---GNREIPSRAYVGRFNFKGGDQQKKvGVLSGGERNRLHLAKTLKQGG 464
|
170
....*....|...
gi 2534501033 148 RLLLLDEPFVSLD 160
Cdd:PRK11819 465 NVLLLDEPTNDLD 477
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-186 |
8.11e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 8.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLR-MIGGVDTLFSGRVLVDGVVAAeAPPAGFVFQdprllpwLTALDNI--- 97
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTVAY-VPQVSWIFN-------ATVRDNIlfg 702
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 98 ---------RAVRPETTESEAEAM----LMRVGLKGFEryypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLV 164
Cdd:PLN03130 703 spfdperyeRAIDVTALQHDLDLLpggdLTEIGERGVN------ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180
....*....|....*....|....
gi 2534501033 165 vemEQVLLTLI--ETNRPTVLLVT 186
Cdd:PLN03130 777 ---RQVFDKCIkdELRGKTRVLVT 797
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
29-212 |
9.03e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.53 E-value: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG----------------VVAAEAP-PAGFVFQD------- 84
Cdd:PRK10253 28 VEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGehiqhyaskevarrigLLAQNATtPGDITVQElvargry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 85 ---PRLLPWltaldniravRPETTESEAEAMlMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDR 161
Cdd:PRK10253 108 phqPLFTRW----------RKEDEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 162 TLVVEMEQVLLTLIETNRPTVLLVTHLPEDAATVADRAVVLsgRPAKIVAD 212
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIAL--REGKIVAQ 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-187 |
1.03e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 51.94 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIggvdTLF----SGRVLVDGVVAAEAPPAGF------------VFQD 84
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLL----TRFydidEGEILLDGHDLRDYTLASLrnqvalvsqnvhLFND 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 85 prllpwlTALDNIRAVRPETTESE--------AEAMlmrvglkGFERYYPH-----------ELSGGMQRRVALARAFSV 145
Cdd:PRK11176 432 -------TIANNIAYARTEQYSREqieeaarmAYAM-------DFINKMDNgldtvigengvLLSGGQRQRIAIARALLR 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2534501033 146 NPRLLLLDEPFVSLDrtlvVEME---QVLLTLIETNRpTVLLVTH 187
Cdd:PRK11176 498 DSPILILDEATSALD----TESEraiQAALDELQKNR-TSLVIAH 537
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-187 |
1.40e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGFVFQdprllpwLTALDN------- 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQ-------LTGIENiefkmlc 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 -------IRAVRPETTE-SEAEAMLmrvglkgferYYP-HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEM 167
Cdd:PRK13546 113 mgfkrkeIKAMTPKIIEfSELGEFI----------YQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|
gi 2534501033 168 EQVLLTLIETNRpTVLLVTH 187
Cdd:PRK13546 183 LDKIYEFKEQNK-TIFFVSH 201
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-171 |
1.60e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRV-LVDGVvaaeapPAGFVFQdpRLLPWLTA----LDNI 97
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI------KLGYFAQ--HQLEFLRAdespLQHL 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2534501033 98 RAVRPETTESEAEAMLMRVGLKGFERYYPHE-LSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtlvVEMEQVL 171
Cdd:PRK10636 399 ARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMRQAL 469
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
130-233 |
3.51e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.63 E-value: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 130 SGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIEtnrpTVLLVTHLPEDAATVADRAVVLSGRpaKI 209
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSHAREFLNTVVTDILHLHGQ--KL 419
|
90 100
....*....|....*....|....
gi 2534501033 210 VAdYRFASAAGQRPRAerEHIANQ 233
Cdd:PLN03073 420 VT-YKGDYDTFERTRE--EQLKNQ 440
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-155 |
4.48e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 50.12 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLV-DGVVAAEAppagfvFQD---PR-----------LL 88
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGGDMADAR------HRRavcPRiaympqglgknLY 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 89 PWLTALDNI----------RAVRpettESEAEAMLMRVGLKGF-ERyyPH-ELSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:NF033858 91 PTLSVFENLdffgrlfgqdAAER----RRRIDELLRATGLAPFaDR--PAgKLSGGMKQKLGLCCALIHDPDLLILDEP 163
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
129-219 |
5.52e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.63 E-value: 5.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 129 LSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPE------DAATVADRAVVL 202
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEipdfvqFAGVLADCTLAE 215
|
90
....*....|....*..
gi 2534501033 203 SGRPAKIVADYRFASAA 219
Cdd:PRK10938 216 TGEREEILQQALVAQLA 232
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-162 |
5.55e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 49.71 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 22 PLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMI------GGVDTLFSGRVLVD---------GVVAAEAPpagFVFQDpr 86
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIqrhfdvSEGDIRFHDIPLTKlqldswrsrLAVVSQTP---FLFSD-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 87 llpwlTALDNIRAVRPETTESEAEAM---------LMR--------VGLKGFeryyphELSGGMQRRVALARAFSVNPRL 149
Cdd:PRK10789 404 -----TVANNIALGRPDATQQEIEHVarlasvhddILRlpqgydteVGERGV------MLSGGQKQRISIARALLLNAEI 472
|
170
....*....|....
gi 2534501033 150 LLLDEPFVSLD-RT 162
Cdd:PRK10789 473 LILDDALSAVDgRT 486
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
24-159 |
5.86e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-----VAAEAPPAG--FVFQDPRLLPWLTALDN 96
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeidfkSSKEALENGisMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IravrpetteseaeaMLMRVGLKGF----ERYY---------------PHE----LSGGMQRRVALARAFSVNPRLLLLD 153
Cdd:PRK10982 94 M--------------WLGRYPTKGMfvdqDKMYrdtkaifdeldididPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMD 159
|
....*.
gi 2534501033 154 EPFVSL 159
Cdd:PRK10982 160 EPTSSL 165
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
23-201 |
6.18e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.56 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLR-MIGGVDTLfSGRVLVdGV---VAaeappagfVFQDPR--LLPWLTALDN 96
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKlMLGQLQAD-SGRIHC-GTkleVA--------YFDQHRaeLDPEKTVMDN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 IravrpetTESEAEAMLmrvglKGFER----------YYPHE-------LSGGMQRRVALARAFSVNPRLLLLDEPFVSL 159
Cdd:PRK11147 404 L-------AEGKQEVMV-----NGRPRhvlgylqdflFHPKRamtpvkaLSGGERNRLLLARLFLKPSNLLILDEPTNDL 471
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2534501033 160 DrtlvVEMEQVLLTLIETNRPTVLLVTHlpedaatvaDRAVV 201
Cdd:PRK11147 472 D----VETLELLEELLDSYQGTVLLVSH---------DRQFV 500
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-242 |
8.89e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 8.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 16 FDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAaeappagFVFQDPrllpWL---T 92
Cdd:PTZ00243 668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIA-------YVPQQA----WImnaT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 ALDNIRAVRPETTESEAEA----------------MLMRVGLKGFEryypheLSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:PTZ00243 737 VRGNILFFDEEDAARLADAvrvsqleadlaqlgggLETEIGEKGVN------LSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 157 VSLDrTLVVE--MEQVLLTLIETNrpTVLLVTH----LPEDAATVA--DRAVVLSGRPAKIVADYRFASAAGQrpRAERE 228
Cdd:PTZ00243 811 SALD-AHVGErvVEECFLGALAGK--TRVLATHqvhvVPRADYVVAlgDGRVEFSGSSADFMRTSLYATLAAE--LKENK 885
|
250
....*....|....
gi 2534501033 229 HIANQIAGAAAERL 242
Cdd:PTZ00243 886 DSKEGDADAEVAEV 899
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-187 |
1.61e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 21 TPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGG--VDTLFSGRVLVDGVVAAEAPP-----AG--FVFQDPRLLPWL 91
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPeerahLGifLAFQYPIEIPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDNIR----AVRPETTESEAEAM---------LMRVGLKG--FERYYPHELSGGMQRRVALARAFSVNPRLLLLDEPF 156
Cdd:CHL00131 100 SNADFLRlaynSKRKFQGLPELDPLefleiinekLKLVGMDPsfLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190
....*....|....*....|....*....|.
gi 2534501033 157 VSLDRTLVVEMEQVLLTLIETNRpTVLLVTH 187
Cdd:CHL00131 180 SGLDIDALKIIAEGINKLMTSEN-SIILITH 209
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1-212 |
1.72e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 1 MSSGPRLEIDVEGKKFDFLPTPLLDGFRLEIEPSSVVALVGPSGVG--KSTLLRMIGGVD---------TLFSGRVLVDG 69
Cdd:NF000106 6 ISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDagrrpwrf*TWCANRRALRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 70 VVAAEAPPAGFVFQDPRLLPWLTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYPHELSGGMQRRVALARAFSVNPRL 149
Cdd:NF000106 86 TIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 150 LLLDEPFVSLDRTLVVEMEQVLLTLIEtNRPTVLLVTHLPEDAATVADRAVVLSgrPAKIVAD 212
Cdd:NF000106 166 LYLDEPTTGLDPRTRNEVWDEVRSMVR-DGATVLLTTQYMEEAEQLAHELTVID--RGRVIAD 225
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-187 |
1.75e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.43 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGF------VFQDPRLLPWLTALDNiRAVRP 102
Cdd:PRK10522 344 LTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYrklfsaVFTDFHLFDQLLGPEG-KPANP 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 103 ETTESEAEAMLMR--VGLKGFeRYYPHELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRP 180
Cdd:PRK10522 423 ALVEKWLERLKMAhkLELEDG-RISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGK 501
|
....*..
gi 2534501033 181 TVLLVTH 187
Cdd:PRK10522 502 TIFAISH 508
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
59-187 |
2.66e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 59 TLF--SGRVLVDGVVAAEAPPA------GFVFQDPRLLPwLTALDNIRAVRPETTESEAEAMLMRVGLKGFERYYPHE-- 128
Cdd:PTZ00265 1271 TVFknSGKILLDGVDICDYNLKdlrnlfSIVSQEPMLFN-MSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKyd 1349
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2534501033 129 ---------LSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTH 187
Cdd:PTZ00265 1350 tnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
129-210 |
3.97e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 3.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 129 LSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEdAATVADRAVVLS-GRPA 207
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPE-LLGITDRILVMSnGLVA 470
|
...
gi 2534501033 208 KIV 210
Cdd:PRK10982 471 GIV 473
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-187 |
6.09e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 1 MSSGPRLEIDVEGKkfdflptPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVD--TLFSGRVLVDGVVAAEAPP- 77
Cdd:PRK09580 1 MLSIKDLHVSVEDK-------AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPe 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 78 --AG----FVFQDPRLLPWL-------TALDNIRAVRPETT----------ESEAEAMLMRVGLkgFERYYPHELSGGMQ 134
Cdd:PRK09580 74 drAGegifMAFQYPVEIPGVsnqfflqTALNAVRSYRGQEPldrfdfqdlmEEKIALLKMPEDL--LTRSVNVGFSGGEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 135 RRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRpTVLLVTH 187
Cdd:PRK09580 152 KRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTH 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
129-190 |
6.30e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 6.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 129 LSGGmQR-------RVALARAFSVNPRLLLLDEPFVSLDRTLVvemEQVLLTLIETNR----PTVLLVTHLPE 190
Cdd:cd03240 116 CSGG-EKvlasliiRLALAETFGSNCGILALDEPTTNLDEENI---EESLAEIIEERKsqknFQLIVITHDEE 184
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-160 |
8.61e-06 |
|
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: 45.62 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 16 FDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAaeappagFVFQDPRLLPWlTALD 95
Cdd:cd03291 45 LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRIS-------FSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 96 NI---------------RAVRPETTESE-AEAMLMRVGLKGFEryypheLSGGMQRRVALARAFSVNPRLLLLDEPFVSL 159
Cdd:cd03291 117 NIifgvsydeyryksvvKACQLEEDITKfPEKDNTVLGEGGIT------LSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
.
gi 2534501033 160 D 160
Cdd:cd03291 191 D 191
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-211 |
9.14e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.06 E-value: 9.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 6 RLEID-VEGKKfdfLPTPlldgFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV-VAAEAPP----AG 79
Cdd:PRK11288 257 RLRLDgLKGPG---LREP----ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpIDIRSPRdairAG 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 80 FVF--QDPR---LLPWLTALDNI-----RAVRP------ETTESE-AEAMLMRVGLKGFERYYP-HELSGGMQRRVALAR 141
Cdd:PRK11288 330 IMLcpEDRKaegIIPVHSVADNInisarRHHLRagclinNRWEAEnADRFIRSLNIKTPSREQLiMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2534501033 142 AFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEdAATVADRAVVLS-GRPAKIVA 211
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPE-VLGVADRIVVMReGRIAGELA 479
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
39-171 |
1.41e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 39 LVGPSGVGKSTLLRMIGGVDTLFSGRVLVD-GVVAAEAPPAGFVFQDPRLL-----------------------PWLTAL 94
Cdd:PRK15064 32 LIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLGKLRQDQFAFEEFTVLdtvimghtelwevkqerdriyalPEMSEE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 DNIRAVRPE---------TTESEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLV 164
Cdd:PRK15064 112 DGMKVADLEvkfaemdgyTAEARAGELLLGVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTI 191
|
....*..
gi 2534501033 165 VEMEQVL 171
Cdd:PRK15064 192 RWLEDVL 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
115-202 |
1.44e-05 |
|
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: 45.59 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 115 RVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEdAA 193
Cdd:TIGR02633 389 RLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAE-VL 467
|
....*....
gi 2534501033 194 TVADRAVVL 202
Cdd:TIGR02633 468 GLSDRVLVI 476
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
23-188 |
2.10e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDG----------VVAAEAPPAGFVFQDPRLLPWLT 92
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqeTPALPQPALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 93 A--------------------LDNIRAVrpeTTESEAEAMLMRVGLKGFERYYP-HELSGGMQRRVALARAFSVNPRLLL 151
Cdd:PRK10636 96 AqlhdanerndghaiatihgkLDAIDAW---TIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2534501033 152 LDEPFVSLDRTLVVEMEQVL------LTLIETNR----PTVLLVTHL 188
Cdd:PRK10636 173 LDEPTNHLDLDAVIWLEKWLksyqgtLILISHDRdfldPIVDKIIHI 219
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-162 |
2.92e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 24 LDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGFVFQdprllpwLTALDNI------ 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQ-------LTGIENIelkglm 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 98 --------RAVRPETTESEAEAMLMRVGLKGFeryyphelSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRT 162
Cdd:PRK13545 113 mgltkekiKEIIPEIIEFADIGKFIYQPVKTY--------SSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-187 |
3.35e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.58 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 19 LPtPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEappagFVFQDPR----LLPWLTAL 94
Cdd:PLN03232 1248 LP-PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK-----FGLTDLRrvlsIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 95 --DNIR-AVRPETTESEAE--AMLMRVGLKGFERYYPHEL-----------SGGMQRRVALARAFSVNPRLLLLDEPFVS 158
Cdd:PLN03232 1322 fsGTVRfNIDPFSEHNDADlwEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190
....*....|....*....|....*....|.
gi 2534501033 159 LDrtlvVEMEQVLLTLI--ETNRPTVLLVTH 187
Cdd:PLN03232 1402 VD----VRTDSLIQRTIreEFKSCTMLVIAH 1428
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
15-203 |
3.38e-05 |
|
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: 43.74 E-value: 3.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 15 KFDFLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTL----LRMIggvdTLFSGRVLVDGVVAAEAP------PAGFVFQD 84
Cdd:cd03288 28 RYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMV----DIFDGKIVIDGIDISKLPlhtlrsRLSIILQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 85 PRLLPwltalDNIR-AVRPET--TESEAEAMLMRVGLKGFERYYPHEL-----------SGGMQRRVALARAFSVNPRLL 150
Cdd:cd03288 104 PILFS-----GSIRfNLDPECkcTDDRLWEALEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2534501033 151 LLDEPFVSLDRTLVVEMEQVLLTLIETNrpTVLLVTHLPEDAATvADRAVVLS 203
Cdd:cd03288 179 IMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLS 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
128-210 |
6.29e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.62 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 128 ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPTVLLVTHLPEDAAtVADRAVVLS-GRP 206
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIIT-VCDRIAVFCeGRL 487
|
....
gi 2534501033 207 AKIV 210
Cdd:PRK09700 488 TQIL 491
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-160 |
9.37e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 43.09 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 5 PRLEID---VEGKKfdflPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPA--- 78
Cdd:COG3845 256 VVLEVEnlsVRDDR----GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRerr 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 79 ----GFVFQDPR---LLPWLTALDNI-------------RAVRPETTESEAEAMLmrvglkgfERY---YPHE------L 129
Cdd:COG3845 332 rlgvAYIPEDRLgrgLVPDMSVAENLilgryrrppfsrgGFLDRKAIRAFAEELI--------EEFdvrTPGPdtparsL 403
|
170 180 190
....*....|....*....|....*....|.
gi 2534501033 130 SGGMQRRVALARAFSVNPRLLLLDEPFVSLD 160
Cdd:COG3845 404 SGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
128-205 |
9.88e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 9.88e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 128 ELSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLI-ETNRPTVLLVTHLpeDAATVADRAVVLSGR 205
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRL--STIRYANTIFVLSNR 655
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-207 |
1.77e-04 |
|
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: 42.08 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 25 DGFRL----EIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVlvdgvvaaEAPP---------AGFVFQDprllpWL 91
Cdd:COG1245 86 NGFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--------DEEPswdevlkrfRGTELQD-----YF 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 92 TALDN--IRAVR--------PETTESEAEAMLMRVGLKGFERYYPH-------------ELSGGMQRRVALARAFSVNPR 148
Cdd:COG1245 153 KKLANgeIKVAHkpqyvdliPKVFKGTVRELLEKVDERGKLDELAEklglenildrdisELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 149 LLLLDEPFVSLDRTLVVEMEQVLLTLIETNRPtVLLVTHlpeDAAT---VADRAVVLSGRPA 207
Cdd:COG1245 233 FYFFDEPSSYLDIYQRLNVARLIRELAEEGKY-VLVVEH---DLAIldyLADYVHILYGEPG 290
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-220 |
2.10e-04 |
|
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: 42.24 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 23 LLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGVVAAEAPPAGFVF------QDPRLLPWLTALDn 96
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFkitiipQDPVLFSGSLRMN- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 97 iraVRPETTESEAEA--MLMRVGLKGFERYYP----HE-------LSGGMQRRVALARAFSVNPRLLLLDEPFVSLDrtl 163
Cdd:TIGR00957 1380 ---LDPFSQYSDEEVwwALELAHLKTFVSALPdkldHEcaeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVD--- 1453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2534501033 164 vVEMEQVLLTLIET--NRPTVLLVTH-----LPEDAATVADRAVVLS-GRPAKIVAD----YRFASAAG 220
Cdd:TIGR00957 1454 -LETDNLIQSTIRTqfEDCTVLTIAHrlntiMDYTRVIVLDKGEVAEfGAPSNLLQQrgifYSMAKDAG 1521
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-70 |
2.53e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.53e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2534501033 19 LPtPLLDGFRLEIEPSSVVALVGPSGVGKSTLLRMIGGVDTLFSGRVLVDGV 70
Cdd:PLN03130 1251 LP-PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGC 1301
|
|
| BMS1 |
COG5192 |
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and ... |
10-52 |
3.71e-04 |
|
GTP-binding protein required for 40S ribosome biogenesis [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227519 [Multi-domain] Cd Length: 1077 Bit Score: 41.26 E-value: 3.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2534501033 10 DVEGKKfdfLPTPLLDGFRLEIEPSSVVALVGPSGVGKSTLLR 52
Cdd:COG5192 48 DIEEKK---LHVPMVDRTPKDLPPPFIVAVVGPPGTGKSTLIR 87
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
25-51 |
3.74e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 37.58 E-value: 3.74e-04
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
129-202 |
4.74e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 4.74e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2534501033 129 LSGGMQRRVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNrPTVLLVTHLPEDAATVADRAVVL 202
Cdd:PRK15439 404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVM 476
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
129-155 |
1.20e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 39.60 E-value: 1.20e-03
10 20
....*....|....*....|....*..
gi 2534501033 129 LSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEP 422
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
36-51 |
1.25e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 38.92 E-value: 1.25e-03
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
129-155 |
1.43e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 1.43e-03
10 20
....*....|....*....|....*..
gi 2534501033 129 LSGGMQRRVALARAFSVNPRLLLLDEP 155
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEP 432
|
|
| BMS1 |
cd01882 |
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is ... |
10-52 |
1.78e-03 |
|
Bms1, an essential GTPase, promotes assembly of preribosomal RNA processing complexes; Bms1 is an essential, evolutionarily conserved, nucleolar protein. Its depletion interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits. Bms1, the putative endonuclease Rc11, and the essential U3 small nucleolar RNA form a stable subcomplex that is believed to control an early step in the formation of the 40S subumit. The C-terminal domain of Bms1 contains a GTPase-activating protein (GAP) that functions intramolecularly. It is believed that Rc11 activates Bms1 by acting as a guanine-nucleotide exchange factor (GEF) to promote GDP/GTP exchange, and that activated (GTP-bound) Bms1 delivers Rc11 to the preribosomes.
Pssm-ID: 206669 [Multi-domain] Cd Length: 231 Bit Score: 38.47 E-value: 1.78e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2534501033 10 DVEGKKfdfLPTPLLDGfRLEIEPSSVVALVGPSGVGKSTLLR 52
Cdd:cd01882 19 DLEEKK---LHVPVVDR-TPEEPPPLVVVVVGPPGVGKSTLIR 57
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
136-187 |
2.24e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 38.87 E-value: 2.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2534501033 136 RVALARAFSVNPRLLLLDEPFVSLDRTLVVEMEQVLLTLIETNRP----TVLLVTH 187
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQqrnfQLLVITH 1268
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
36-51 |
3.40e-03 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 37.79 E-value: 3.40e-03
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
29-187 |
4.56e-03 |
|
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: 36.92 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 29 LEIEPSSVVALVGPSGVGKSTLLRMIGGVDtlfSGRVLVDGVVAAEAPPAGFVFQDPRLLPwlTALDNIRAVRPETTese 108
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKSTLVNEGLYAS---GKARLISFLPKFSRNKLIFIDQLQFLID--VGLGYLTLGQKLST--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 109 aeamlmrvglkgferyypheLSGGMQRRVALARAFSVNPR--LLLLDEPFVSLDrtlvvemEQVLLTLIETNRP------ 180
Cdd:cd03238 88 --------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-------QQDINQLLEVIKGlidlgn 140
|
....*..
gi 2534501033 181 TVLLVTH 187
Cdd:cd03238 141 TVILIEH 147
|
|
| flhF |
PRK05703 |
flagellar biosynthesis protein FlhF; |
17-49 |
5.99e-03 |
|
flagellar biosynthesis protein FlhF;
Pssm-ID: 235570 [Multi-domain] Cd Length: 424 Bit Score: 37.57 E-value: 5.99e-03
10 20 30
....*....|....*....|....*....|...
gi 2534501033 17 DFLPTPLLDgfrlEIEPSSVVALVGPSGVGKST 49
Cdd:PRK05703 208 NMIPVRVED----ILKQGGVVALVGPTGVGKTT 236
|
|
| NTPase_1 |
pfam03266 |
NTPase; This domain is found across all species from bacteria to human, and the function was ... |
37-195 |
9.22e-03 |
|
NTPase; This domain is found across all species from bacteria to human, and the function was determined first in a hyperthermophilic bacterium to be an NTPase. The structure of one member-sequence represents a variation of the RecA fold, and implies that the function might be that of a DNA/RNA modifying enzyme. The sequence carries both a Walker A and Walker B motif which together are characteriztic of ATPases or GTPases. The protein exhibits an increased expression profile in human liver cholangiocarcinoma when compared to normal tissue.
Pssm-ID: 460869 Cd Length: 168 Bit Score: 35.68 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 37 VALVGPSGVGKSTLLRMIggVDTLFSGRVLVDGVVAAEAP----PAGFvfqdprllpwltaldNIRAVrpettESEAEAM 112
Cdd:pfam03266 2 IFITGPPGVGKTTLVLKV--AELLKSSGVKVGGFYTPEVReggrRIGF---------------KIVDL-----ASGEEGW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2534501033 113 LMRVGLKGFER---YYPH--ELSGGMQRrvALARAFSvNPRLLLLDE--PFVSLDRTLVVEMEQVLltliETNRPtVLLV 185
Cdd:pfam03266 60 LARVGAVSGPRvgkYVVNveSFEEIAVP--ALRRALE-EADLIIIDEigPMELKSKKFREAVREVL----DSGKP-VLAV 131
|
170
....*....|
gi 2534501033 186 THLPEDAATV 195
Cdd:pfam03266 132 IHRRSDSPLL 141
|
|
| |
