|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-216 |
5.09e-109 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 312.36 E-value: 5.09e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLG-GEA---VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQR 76
Cdd:COG1136 1 MSPLLELRNLTKSYGtGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 AVTRNRLLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALV 156
Cdd:COG1136 81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 157 TEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
19-216 |
4.30e-96 |
|
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: 278.99 E-value: 4.30e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQSFNLLPRLS 98
Cdd:cd03255 19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFRRRHIGFVFQSFNLLPDLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:cd03255 99 ALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKE 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 179 IIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:cd03255 179 VMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-216 |
4.11e-92 |
|
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: 269.69 E-value: 4.11e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 2 SSIISLHGVTRWLGGEA----VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRA 77
Cdd:COG4181 6 APIIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 78 VTRNRLLGFVFQSFNLLPRLSVLDNVALPLSYRGIRlaSARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVT 157
Cdd:COG4181 86 RLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 158 EPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:COG4181 164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
19-220 |
1.54e-79 |
|
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: 237.25 E-value: 1.54e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQSFNLLPRLS 98
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:TIGR02211 100 ALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1796960594 179 IIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGVFD 220
Cdd:TIGR02211 180 IFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-220 |
1.78e-74 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 224.55 E-value: 1.78e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnR 82
Cdd:COG2884 1 MIRFENVSkRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 LLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQ-IAKVqLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRI 161
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRrVREV-LDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMAQCMD-RCLLVRNGGVFD 220
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLELVDRMPkRVLELEDGRLVR 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-216 |
8.36e-69 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 210.44 E-value: 8.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQSFNLLPRLS 98
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 179 IIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:PRK11629 184 IFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDG 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-216 |
2.04e-68 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 210.33 E-value: 2.04e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTR----WLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqr 76
Cdd:COG1116 4 AAPALELRGVSKrfptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 avtrnrlLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALV 156
Cdd:COG1116 82 -------RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 157 TEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDP----AMAqcmDRCLLVRNG 216
Cdd:COG1116 155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdeavFLA---DRVVVLSAR 215
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-200 |
2.57e-68 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 209.47 E-value: 2.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNrl 83
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRLSVLDNVAL-PLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHD 200
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEG-MTMVVVTHE 195
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-220 |
5.45e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 206.45 E-value: 5.45e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 3 SIISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRN 81
Cdd:COG3638 1 PMLELRNLSkRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 RLlGFVFQSFNLLPRLSVLDNVALP-LSYRG-----IRLASA--RQIAKVQLEKVGLEPRAkYRPAD-LSGGQRQRVAIA 152
Cdd:COG3638 81 RI-GMIFQQFNLVPRLSVLTNVLAGrLGRTStwrslLGLFPPedRERALEALERVGLADKA-YQRADqLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMA-QCMDRCLLVRNGG-VFD 220
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLArRYADRIIGLRDGRvVFD 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-200 |
2.58e-66 |
|
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: 203.47 E-value: 2.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEA----VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqravtr 80
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 nrlLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:cd03293 75 ---RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD 191
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
5-216 |
4.28e-65 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 200.44 E-value: 4.28e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtrnrll 84
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALaDRIAVMNEG 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-200 |
1.08e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 200.69 E-value: 1.08e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTR--WLGGEAV--LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQ-RAV 78
Cdd:COG1135 1 MIELENLSKtfPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 TRNrlLGFVFQSFNLLPRLSVLDNVALPLSYRGIrlaSARQI-AKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARAL 155
Cdd:COG1135 81 RRK--IGMIFQHFNLLSSRTVAENVALPLEIAGV---PKAEIrKRVAelLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1796960594 156 VTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHE 200
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-216 |
2.20e-63 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 200.32 E-value: 2.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtr 80
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 nrllGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:COG3842 80 ----GMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDP--AMAqcM-DRCLLVRNG 216
Cdd:COG3842 156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQeeALA--LaDRIAVMNDG 212
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
4-199 |
1.64e-62 |
|
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: 194.34 E-value: 1.64e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEA----VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQ-ADADQRAV 78
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 TRNrlLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:cd03258 81 RRR--IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTH 199
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH 199
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-200 |
1.88e-62 |
|
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: 194.43 E-value: 1.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTR 80
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLlGFVFQSFNLLPRLSVLDNVALPLS-YRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEP 159
Cdd:COG1127 82 RRI-GMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1796960594 160 RILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHD 201
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-205 |
3.89e-62 |
|
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: 192.74 E-value: 3.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNrlL 84
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQK--V 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVAL-PLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMAQ 205
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEG-MTMVVVTHEMGFAR 199
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-216 |
2.10e-61 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 191.53 E-value: 2.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 3 SIISLHGVTRWLG-GE---AVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAV 78
Cdd:PRK10584 5 NIVEVHHLKKSVGqGEhelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 TRNRLLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
7-209 |
2.74e-61 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 190.52 E-value: 2.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 7 LHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGF 86
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 87 VFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADE 166
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 167 PTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMAQCMDR 209
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLELNDEG-KTIIIVTHDPEVAKQADR 202
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-216 |
2.89e-60 |
|
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: 189.24 E-value: 2.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLG----GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAdadqRAVTR 80
Cdd:COG1124 2 LEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRR----RRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLLGFVFQ----SFNllPRLSVLDNVALPLSYRGIRLASARqIAKVqLEKVGLEPRAKYR-PADLSGGQRQRVAIARAL 155
Cdd:COG1124 78 RRRVQMVFQdpyaSLH--PRHTVDRILAEPLRIHGLPDREER-IAEL-LEQVGLPPSFLDRyPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 156 VTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLcDRVAVMQNG 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-216 |
1.32e-59 |
|
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: 186.94 E-value: 1.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEA----VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVT 79
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 RNRLlGFVFQ----SFNllPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEP---RAKYRPADLSGGQRQRVAIA 152
Cdd:cd03257 81 RKEI-QMVFQdpmsSLN--PRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLpeeVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIaDRVAVMYAG 222
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-216 |
3.40e-59 |
|
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: 185.61 E-value: 3.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLG-GEA---VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVT 79
Cdd:TIGR02982 1 VISIRNLNHYYGhGSLrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 RnRLLGFVFQSFNLLPRLSVLDNVALPLS-YRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALElQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDG 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-218 |
1.22e-58 |
|
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: 184.63 E-value: 1.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLl 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRM- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRLASA-RQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD-PAMAQCMDRCLLVRNGGV 218
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDlDTAFAIADRIAVLYDGKI 215
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
4-205 |
2.43e-58 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 183.22 E-value: 2.43e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNR 82
Cdd:TIGR02673 1 MIEFHNVSkAYPGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 LlGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:TIGR02673 81 I-GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNReQFMTLLMVTHDPAMAQ 205
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVD 201
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
5-218 |
1.06e-56 |
|
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: 179.45 E-value: 1.06e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAvtrnR 82
Cdd:COG1122 1 IELENLSfSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnGLL-KPTSGEVLVDGKDITKKNLRELR----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 LLGFVFQ-SFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRI 161
Cdd:COG1122 76 KVGLVFQnPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMA-QCMDRCLLVRNGGV 218
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEG-KTVIIVTHDLDLVaELADRVIVLDDGRI 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-216 |
2.50e-56 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 189.16 E-value: 2.50e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTR-WLGGE---AVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQR 76
Cdd:PRK10535 1 MTALLELKDIRRsYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 AVTRNRLLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALV 156
Cdd:PRK10535 81 AQLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 157 TEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
4-205 |
5.56e-56 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 177.98 E-value: 5.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRl 83
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 lGFVFQSFNLLPRLSVLDNVAL-PLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:PRK09493 80 -GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQ 205
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAE 200
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
5-220 |
7.26e-56 |
|
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: 177.76 E-value: 7.26e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQA-DADQRAVTRNr 82
Cdd:cd03256 1 IEVENLSkTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkGKALRQLRRQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 lLGFVFQSFNLLPRLSVLDNVALP-LSYRGI-----RLAS--ARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARA 154
Cdd:cd03256 80 -IGMIFQQFNLIERLSVLENVLSGrLGRRSTwrslfGLFPkeEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 155 LVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQC-MDRCLLVRNGG-VFD 220
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRiVFD 226
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-217 |
9.92e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 180.73 E-value: 9.92e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSsiISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGsevaqADADQRAVTR 80
Cdd:COG1118 1 MS--IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-----RDLFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:COG1118 74 ERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDP--AMAQCmDRcLLVRNGG 217
Cdd:COG1118 154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQeeALELA-DR-VVVMNQG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-218 |
1.01e-55 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 184.72 E-value: 1.01e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVT-----RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAV 78
Cdd:COG1123 260 LLEVRNLSkrypvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 TRnRLLGFVFQ----SFNllPRLSVLDNVALPLSYRGI-RLASARQIAKVQLEKVGLEPRAKYR-PADLSGGQRQRVAIA 152
Cdd:COG1123 340 LR-RRVQMVFQdpysSLN--PRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLADRyPHELSGGQRQRVAIA 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGV 218
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIaDRVAVMYDGRI 483
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-220 |
1.92e-55 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 176.82 E-value: 1.92e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQAdadqravt 79
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIlGLL-PPTSGTVRLFGKPPRRA-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 rNRLLGFVFQSFNL---LPrLSVLDNVALPLSYRG--IRLASARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIA 152
Cdd:COG1121 74 -RRRIGYVPQRAEVdwdFP-ITVRDVVLMGRYGRRglFRRPSRADREAVDeaLERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMA-QCMDRCLLVRNGGVFD 220
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVrEYFDRVLLLNRGLVAH 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-218 |
3.04e-55 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 179.50 E-value: 3.04e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIiSLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtr 80
Cdd:COG3839 1 MASL-ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 nrllGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:COG3839 78 ----AMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDP--AMAqcM-DRCLLVRNGGV 218
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQveAMT--LaDRIAVMNDGRI 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-218 |
9.43e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.85 E-value: 9.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQ-RavtrnRL 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwR-----RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRlSVLDNVALPLSYRGIRLAsaRQIAKVQLEKVGLEPRAKYRPAD-LSGGQRQRVAIARALVTEPRIL 162
Cdd:COG4619 76 VAYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQ-CMDRCLLVRNGGV 218
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-219 |
1.03e-54 |
|
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: 175.23 E-value: 1.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAvtrnR 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALaGLL-KPSSGEVLLDGRDLASLSRRELA----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 LLGFVFQSFNLLPRLSVLDNVAL---PlsYRG-IRLASARQIAKVQ--LEKVGLEPRAkYRPAD-LSGGQRQRVAIARAL 155
Cdd:COG1120 76 RIAYVPQEPPAPFGLTVRELVALgryP--HLGlFGRPSAEDREAVEeaLERTGLEHLA-DRPVDeLSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 156 VTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMA-QCMDRCLLVRNGGVF 219
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAaRYADRLVLLKDGRIV 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
5-216 |
3.15e-54 |
|
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: 171.60 E-value: 3.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVaqADADQRAVTRNRLL 84
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--TDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPlsyrgirlasarqiakvqlekvgleprakyrpadLSGGQRQRVAIARALVTEPRILLA 164
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLaDRVVVLRDG 177
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
5-216 |
1.14e-53 |
|
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: 171.59 E-value: 1.14e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLD----QPCHGSLVLDGSEVAQADADQRAVT 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDlipgAPDEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 RNrlLGFVFQSFNLLPrLSVLDNVALPLSYRGIRLASAR-QIAKVQLEKVGLEPRAKYR--PADLSGGQRQRVAIARALV 156
Cdd:cd03260 81 RR--VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDEVKDRlhALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 157 TEPRILLADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDPAMAQ-CMDRCLLVRNG 216
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAArVADRTAFLLNG 216
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
20-199 |
1.18e-53 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 175.37 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnRLLGFVFQSFNLLPRLSV 99
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR-RQIGMIFQHFNLLSSRTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 100 LDNVALPLsyrgiRLA--SARQI-AKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:PRK11153 100 FDNVALPL-----ELAgtPKAEIkARVTelLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
|
170 180
....*....|....*....|....*
gi 1796960594 175 TAQDIIELLTTLNREQFMTLLMVTH 199
Cdd:PRK11153 175 TTRSILELLKDINRELGLTIVLITH 199
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
24-218 |
1.74e-53 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 171.48 E-value: 1.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 24 SFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTrnrllgFVFQSFNLLPRLSVLDNV 103
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVS------MLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 104 ALPLSyRGIRLaSARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIE 181
Cdd:COG3840 93 GLGLR-PGLKL-TAEQRAQVEqaLERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLD 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 182 LLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGV 218
Cdd:COG3840 171 LVDELCRERGLTVLMVTHDPEDAARIaDRVLLVADGRI 208
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-216 |
2.07e-53 |
|
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: 171.27 E-value: 2.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtrnrll 84
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMsDRIAVMNKG 207
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-216 |
4.10e-53 |
|
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: 169.57 E-value: 4.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRLLGFVFQSFNL- 93
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQNPDDq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDG 173
Cdd:cd03225 88 FFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDP 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 174 DTAQDIIELLTTLNREQfMTLLMVTHDPA-MAQCMDRCLLVRNG 216
Cdd:cd03225 168 AGRRELLELLKKLKAEG-KTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-200 |
1.24e-52 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 170.04 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqRAVtrnrllgfVFQSFNLLPRLS 98
Cdd:COG4525 22 ALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-RGV--------VFQKDALLPWLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:COG4525 93 VLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQ 172
|
170 180
....*....|....*....|..
gi 1796960594 179 IIELLTTLNREQFMTLLMVTHD 200
Cdd:COG4525 173 MQELLLDVWQRTGKGVFLITHS 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-218 |
4.89e-52 |
|
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: 175.09 E-value: 4.89e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWL--GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQPCH--GSLVLDGSEVAQADADQ 75
Cdd:COG1123 1 MTPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGGRisGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 76 RAvtrnRLLGFVFQSF-NLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARA 154
Cdd:COG1123 81 RG----RRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 155 LVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPA-MAQCMDRCLLVRNGGV 218
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGvVAEIADRVVVMDDGRI 221
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
19-204 |
2.66e-51 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 166.51 E-value: 2.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAD--------ADQRAVTRNRL-LGFVFQ 89
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPdrdgelvpADRRQLQRIRTrLGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 90 SFNLLPRLSVLDNVAL-PLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:COG4598 103 SFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPT 182
|
170 180 190
....*....|....*....|....*....|....*.
gi 1796960594 169 GNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMA 204
Cdd:COG4598 183 SALDPELVGEVLKVMRDLAEEG-RTMLVVTHEMGFA 217
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
20-218 |
6.61e-51 |
|
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: 165.89 E-value: 6.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQ-RAVTRNRlLGFVFQSFNLLPRLS 98
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElRELRRKK-ISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1796960594 179 IIELLTTLNREQFMTLLMVTHDPAMA-QCMDRCLLVRNGGV 218
Cdd:cd03294 199 MQDELLRLQAELQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-219 |
5.48e-50 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 161.93 E-value: 5.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 6 SLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQadadqravtRNRLL 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIlGLL-KPTSGSIRVFGKPLEK---------ERKRI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLP--RLSVLDNVALPL--SYRGIRLASARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:cd03235 71 GYVPQRRSIDRdfPISVRDVVLMGLygHKGLFRRLSKADKAKVDeaLERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHD--PAMAQCmDRCLLVRNGGVF 219
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREG-MTILVVTHDlgLVLEYF-DRVLLLNRTVVA 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-218 |
5.85e-50 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 163.31 E-value: 5.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRavtrnrll 84
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 gFVFQSFNLLPRLSVLDNVALPLsyRGIRLASARQiakvQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:PRK11247 85 -LMFQDARLLPWKKVIDNVGLGL--KGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGV 218
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMaDRVLLIEEGKI 212
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-216 |
2.30e-49 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.00 E-value: 2.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRavtrnRL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLlGLL-RPTSGEVRVLGEDVARDPAEVR-----RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMAQ--CmDRCLLVRNG 216
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEG-KTVLLSTHYLEEAErlC-DRVAIIDKG 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
19-200 |
5.63e-49 |
|
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: 162.53 E-value: 5.63e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDQPCH--GSLVLDGSEVAQADADQRAVTRNRLLGFVFQ----SF 91
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPGItsGEILFDGEDLLKLSEKELRKIRGREIQMIFQdpmtSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 92 NllPRLSVLDNVALPL-SYRGIRLASARQIAKVQLEKVGLEP---RAKYRPADLSGGQRQRVAIARALVTEPRILLADEP 167
Cdd:COG0444 100 N--PVMTVGDQIAEPLrIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQRVMIARALALEPKLLIADEP 177
|
170 180 190
....*....|....*....|....*....|...
gi 1796960594 168 TGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:COG0444 178 TTALDVTIQAQILNLLKDLQRELGLAILFITHD 210
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
5-218 |
2.41e-48 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 158.42 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADAdqravtRNRLL 84
Cdd:TIGR00968 1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHA------RDRKI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRgiRLASARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:TIGR00968 75 GFVFQHYALFKHLTVRDNIAFGLEIR--KHPKAKIKARVEelLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMA-QCMDRCLLVRNGGV 218
Cdd:TIGR00968 153 LLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAmEVADRIVVMSNGKI 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
15-216 |
7.86e-48 |
|
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: 156.41 E-value: 7.86e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnRLLGFVFQSFNLL 94
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 175 TAQDIIELLTTLNREQfMTLLMVTHDPAMAQCMD-RCLLVRNG 216
Cdd:cd03292 171 TTWEIMNLLKKINKAG-TTVVVATHAKELVDTTRhRVIALERG 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
5-218 |
1.77e-47 |
|
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: 156.35 E-value: 1.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtrnrll 84
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNV------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGI--RLASARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRseRPPEAEIRAKVHelLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMA-QCMDRCLLVRNGGV 218
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
10-218 |
6.67e-47 |
|
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: 153.80 E-value: 6.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 10 VTRWLGGEAVLqDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTrnrllgFVFQ 89
Cdd:cd03298 5 KIRFSYGEQPM-HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVS------MLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 90 SFNLLPRLSVLDNVALPLSyRGIRL-ASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:cd03298 78 ENNLFAHLTVEQNVGLGLS-PGLKLtAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 169 GNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGV 218
Cdd:cd03298 157 AALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLaQRVVFLDNGRI 207
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
4-221 |
1.33e-46 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 153.99 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADA-DQRAVTRN 81
Cdd:TIGR02315 1 MLEVENLSkVYPNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 rlLGFVFQSFNLLPRLSVLDNVALP-LSY----RGI--RLASA-RQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIAR 153
Cdd:TIGR02315 81 --IGMIFQHYNLIERLTVLENVLHGrLGYkptwRSLlgRFSEEdKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 154 ALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTH--DPAMAQCmDRCLLVRNGG-VFDA 221
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHqvDLAKKYA-DRIVGLKAGEiVFDG 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-200 |
3.14e-46 |
|
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: 153.66 E-value: 3.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAvt 79
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLItGFY-RPTSGRILFDGRDITGLPPHRIA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 rnRL-LGFVFQSFNLLPRLSVLDNVALPLSYRG---------------IRLASARQIAKVQLEKVGLEPRAKYRPADLSG 143
Cdd:COG0411 78 --RLgIARTFQNPRLFPELTVLENVLVAAHARLgrgllaallrlprarREEREARERAEELLERVGLADRADEPAGNLSY 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 144 GQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:COG0411 156 GQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
5-218 |
5.68e-46 |
|
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: 159.92 E-value: 5.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRL 83
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR----RQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSfNLLPRLSVLDNVALplsyrGIRLASARQIAKVqLEKVGLEPRAKYRPAD-----------LSGGQRQRVAIA 152
Cdd:COG4988 413 IAWVPQN-PYLFAGTIRENLRL-----GRPDASDEELEAA-LEAAGLDEFVAALPDGldtplgeggrgLSGGQAQRLALA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVLDDGRI 549
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
15-200 |
9.15e-46 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 152.55 E-value: 9.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQravtrnrllGFVFQSFNLL 94
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
|
170 180
....*....|....*....|....*.
gi 1796960594 175 TAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-216 |
3.85e-45 |
|
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: 147.91 E-value: 3.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqravTRNRLLGFVFQSFNLL 94
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLE----SLRKNIAYVPQDPFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRlSVLDNValplsyrgirlasarqiakvqlekvgleprakyrpadLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:cd03228 89 SG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1796960594 175 TAQDIIELLTTLNREqfMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:cd03228 131 TEALILEALRALAKG--KTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
18-216 |
6.71e-45 |
|
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: 156.38 E-value: 6.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 18 AVlQDVSFSLPTGQSCAIVGASGSGKSTL-LNLIGLLdqPCHGSLVLDGSEVAQADADQRAVTRNRLlGFVFQ----SFN 92
Cdd:COG4172 301 AV-DGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLRRRM-QVVFQdpfgSLS 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 llPRLSVLDNVALPLSYRGIRLASARQIAKVQ--LEKVGLEPRAKYR-PADLSGGQRQRVAIARALVTEPRILLADEPTG 169
Cdd:COG4172 377 --PRMTVGQIIAEGLRVHGPGLSAAERRARVAeaLEEVGLDPAARHRyPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 170 NLDGDTAQDIIELLTTLNREQFMTLLMVTHD----PAMAqcmDRCLLVRNG 216
Cdd:COG4172 455 ALDVSVQAQILDLLRDLQREHGLAYLFISHDlavvRALA---HRVMVMKDG 502
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-216 |
7.67e-45 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 152.55 E-value: 7.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSsiISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADAdqravtR 80
Cdd:PRK10851 1 MS--IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLLGFVFQSFNLLPRLSVLDNVALPLSY--RGIRLASARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALV 156
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAFGLTVlpRRERPNAAAIKAKVTqlLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 157 TEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD--PAMaQCMDRCLLVRNG 216
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqeEAM-EVADRVVVMSQG 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-203 |
7.75e-45 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 148.87 E-value: 7.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 13 WLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnRLLGFVFQSFN 92
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PRK10908 90 LLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180 190
....*....|....*....|....*....|.
gi 1796960594 173 GDTAQDIIELLTTLNREQfMTLLMVTHDPAM 203
Cdd:PRK10908 170 DALSEGILRLFEEFNRVG-VTVLMATHDIGL 199
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
35-216 |
1.36e-44 |
|
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: 151.49 E-value: 1.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 35 IVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtrnrllGFVFQSFNLLPRLSVLDNVALPLSYRGIRL 114
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHI------NMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 115 ASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTL 194
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170 180
....*....|....*....|...
gi 1796960594 195 LMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:TIGR01187 155 VFVTHDQEEAMTMsDRIAIMRKG 177
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-200 |
1.50e-44 |
|
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: 148.74 E-value: 1.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 9 GVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAvtrnRL-LGF 86
Cdd:cd03219 5 GLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsGFL-RPTSGSVLFDGEDITGLPPHEIA----RLgIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 87 VFQSFNLLPRLSVLDNVALPLSYRGIRLAS----------ARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALV 156
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGSGLLlararreereARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 157 TEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHD 200
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERG-ITVLLVEHD 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-216 |
2.68e-44 |
|
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: 148.22 E-value: 2.68e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADAdqraVTRNRL 83
Cdd:cd03295 1 IEFENVTkRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP----VELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEP---RAKYrPADLSGGQRQRVAIARALVTEPR 160
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPaefADRY-PHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLaDRIAIMKNG 212
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
22-218 |
3.01e-44 |
|
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: 151.41 E-value: 3.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGsEVAQADADQRAV-TRNRLLGFVFQSFNLLPRLSVL 100
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGIFLpPHRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 101 DNvalpLSYrGIRLASARQiAKVQLEKV----GLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTA 176
Cdd:COG4148 96 GN----LLY-GRKRAPRAE-RRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 177 QDIIELLTTLNREQFMTLLMVTHDPA-MAQCMDRCLLVRNGGV 218
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRV 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-216 |
5.74e-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: 146.84 E-value: 5.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqRAVtrnrllgfVFQSFNLLPRLSV 99
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD-RMV--------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 100 LDNVALPLS--YRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQ 177
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1796960594 178 DIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLsDRVVMLTNG 191
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-216 |
9.03e-44 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 150.48 E-value: 9.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 2 SSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRn 81
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNT- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 rllgfVFQSFNLLPRLSVLDNVALplsyrGIRLA--SARQIAKVQLEK---VGLEPRAKYRPADLSGGQRQRVAIARALV 156
Cdd:PRK09452 91 -----VFQSYALFPHMTVFENVAF-----GLRMQktPAAEITPRVMEAlrmVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 157 TEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:PRK09452 161 NKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMsDRIVVMRDG 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
5-216 |
1.27e-43 |
|
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: 145.48 E-value: 1.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtrnrll 84
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:cd03301 75 AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMaDRIAVMNDG 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
5-218 |
1.51e-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: 146.16 E-value: 1.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDqPCHGSLVLDGsevaqADADQRAVTRNRL 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLK-PDSGSILIDG-----EDVRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQFmTLLMVTHDPAMAQCM-DRCLLVRNGGV 218
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALcDRVVILHKGKV 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-204 |
1.04e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.00 E-value: 1.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSsiISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEV---AQADADQ-R 76
Cdd:COG4161 1 MS--IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 AVTRNrlLGFVFQSFNLLPRLSVLDN-VALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARAL 155
Cdd:COG4161 79 LLRQK--VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 156 VTEPRILLADEPTGNLDGD-TAQ--DIIELLTtlnrEQFMTLLMVTHDPAMA 204
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEiTAQvvEIIRELS----QTGITQVIVTHEVEFA 204
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
20-168 |
2.36e-42 |
|
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: 140.09 E-value: 2.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVaqaDADQRAVTRNRLlGFVFQSFNLLPRLSV 99
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEI-GYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 100 LDNVALPLSYRGIRLASARQIAKVQLEKVGLEP----RAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-219 |
3.21e-42 |
|
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: 141.03 E-value: 3.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRLLGFVFQSfnll 94
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA----RKIAYVPQA---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 prlsvldnvalplsyrgirlasarqiakvqLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:cd03214 82 ------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796960594 175 TAQDIIELLTTLNREQFMTLLMVTHDPAMA-QCMDRCLLVRNGGVF 219
Cdd:cd03214 132 HQIELLELLRRLARERGKTVVMVLHDLNLAaRYADRVILLKDGRIV 177
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-218 |
4.14e-42 |
|
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: 150.75 E-value: 4.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAvtrnRLLGFVFQSFNL 93
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlGLY-EPTSGRILIDGIDLRQIDPASLR----RQIGVVLQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRlSVLDNVALplSYRGIRLASARQIAKVqlekVGLEPRAKYRP-----------ADLSGGQRQRVAIARALVTEPRIL 162
Cdd:COG2274 561 FSG-TIRENITL--GDPDATDEEIIEAARL----AGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRIL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:COG2274 634 ILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-205 |
4.86e-42 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 142.80 E-value: 4.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 3 SIISLHgvtRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQ----------AD 72
Cdd:PRK10619 7 NVIDLH---KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 73 ADQRAVTRNRLLgFVFQSFNLLPRLSVLDNV-ALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYR-PADLSGGQRQRVA 150
Cdd:PRK10619 84 KNQLRLLRTRLT-MVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKyPVHLSGGQQQRVS 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 151 IARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQ 205
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFAR 216
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-219 |
5.26e-42 |
|
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: 143.36 E-value: 5.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAVTRNRLlGFVFQsF--NLLPR 96
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLnGLL-KPTSGTVTIDGRDITAKKKKKLKDLRKKV-GLVFQ-FpeHQLFE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 LSVLDNVAL-PLSYrGIRLASARQIAKVQLEKVGLEPRAKYR-PADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:TIGR04521 98 ETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPK 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 175 TAQDIIELLTTLNREQFMTLLMVTHDpaM---AQCMDRCLLVRNGGVF 219
Cdd:TIGR04521 177 GRKEILDLFKRLHKEKGLTVILVTHS--MedvAEYADRVIVMHKGKIV 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-205 |
8.06e-42 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 141.69 E-value: 8.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSsiISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEV---AQADADQ-R 76
Cdd:PRK11124 1 MS--IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 AVTRNrlLGFVFQSFNLLPRLSVLDN-VALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARAL 155
Cdd:PRK11124 79 ELRRN--VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 156 VTEPRILLADEPTGNLDGD-TAQ--DIIELLttlnREQFMTLLMVTHDPAMAQ 205
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEiTAQivSIIREL----AETGITQVIVTHEVEVAR 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
15-216 |
1.23e-41 |
|
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: 141.32 E-value: 1.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtrnrllGFVFQSFNLL 94
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDI------SYVPQNYALF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPLSYRGI-RLASARQIAKVQlEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDG 173
Cdd:cd03299 84 PHMTVYKNIAYGLKKRKVdKKEIERKVLEIA-EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 174 DTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALaDKVAIMLNG 206
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
18-200 |
1.28e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 143.72 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 18 AVlQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnRLLGFVFQ----SFNl 93
Cdd:COG4608 33 AV-DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQdpyaSLN- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 lPRLSVLDNVALPLSYRGIRLASARQiAKVQ--LEKVGLEPRAKYR-PADLSGGQRQRVAIARALVTEPRILLADEPTGN 170
Cdd:COG4608 110 -PRMTVGDIIAEPLRIHGLASKAERR-ERVAelLELVGLRPEHADRyPHEFSGGQRQRIGIARALALNPKLIVCDEPVSA 187
|
170 180 190
....*....|....*....|....*....|.
gi 1796960594 171 LDGDT-AQdIIELLTTLNREQFMTLLMVTHD 200
Cdd:COG4608 188 LDVSIqAQ-VLNLLEDLQDELGLTYLFISHD 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-216 |
1.63e-40 |
|
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: 135.84 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 6 SLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRLLG 85
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 86 FVFQsfnllprlsvldnvalplsyrgirlasarqiakvqlekvgleprakyrpadLSGGQRQRVAIARALVTEPRILLAD 165
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 166 EPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMAQ-CMDRCLLVRNG 216
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAElAADRVIVLKDG 156
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
3-216 |
1.90e-40 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 138.73 E-value: 1.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 3 SIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEV--AQADADQRAVTR 80
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 N--RLLGFVFQSFNLLPRLSVLDNVAL-PLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVT 157
Cdd:PRK11264 82 QlrQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 158 EPRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMAQ-CMDRCLLVRNG 216
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARdVADRAIFMDQG 220
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-201 |
3.83e-40 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 136.45 E-value: 3.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRavtrnRLL 84
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-----RRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRlASARQIAKVqLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFWAALYGLR-ADREAIDEA-LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDP 201
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQP 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
5-218 |
7.50e-40 |
|
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: 143.37 E-value: 7.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT-RWLGGEA-VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDqPCHGSLVLDGSEVAQADADQRAvtrn 81
Cdd:COG4987 334 LELEDVSfRYPGAGRpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlRFLD-PQSGSITLGGVDLRDLDEDDLR---- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 RLLGFVFQS---FNLlprlSVLDNvalplsyrgIRL----ASARQIAKVqLEKVGLEPRAKYRP-----------ADLSG 143
Cdd:COG4987 409 RRIAVVPQRphlFDT----TLREN---------LRLarpdATDEELWAA-LERVGLGDWLAALPdgldtwlgeggRRLSG 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 144 GQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:COG4987 475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
22-216 |
1.67e-39 |
|
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: 135.12 E-value: 1.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPtGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQSFNLLPRLSVLD 101
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 102 NVALplSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIE 181
Cdd:cd03297 95 NLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 1796960594 182 LLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLaDRIVVMEDG 208
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-200 |
2.26e-39 |
|
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: 141.75 E-value: 2.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKS-TLLNLIGLLDQP---CHGSLVLDGSEVAQADADQ-RAVtRNRLLGFVFQ---- 89
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERElRRI-RGNRIAMIFQepmt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 90 SFNllPRLSVLDNVALPLS-YRGIRLASARQIAKVQLEKVGL-EPRAKYR--PADLSGGQRQRVAIARALVTEPRILLAD 165
Cdd:COG4172 104 SLN--PLHTIGKQIAEVLRlHRGLSGAAARARALELLERVGIpDPERRLDayPHQLSGGQRQRVMIAMALANEPDLLIAD 181
|
170 180 190
....*....|....*....|....*....|....*
gi 1796960594 166 EPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:COG4172 182 EPTTALDVTVQAQILDLLKDLQRELGMALLLITHD 216
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-218 |
3.19e-39 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 134.48 E-value: 3.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSLVLDGSEVAQADADQRAvtrnRL 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLL-PPRSGSIRFDGRDITGLPPHERA----RA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 -LGFVFQSFNLLPRLSVLDNVALPLsYRGIRLASARQIAKVqlekVGLEPRAKYR---PA-DLSGGQRQRVAIARALVTE 158
Cdd:cd03224 76 gIGYVPEGRRIFPELTVEENLLLGA-YARRRAKRKARLERV----YELFPRLKERrkqLAgTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMA-QCMDRCLLVRNGGV 218
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEG-VTILLVEQNARFAlEIADRAYVLERGRV 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-216 |
3.86e-39 |
|
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: 132.91 E-value: 3.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRavtrnRL 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlGLL-KPDSGEIKVLGKDIKKEPEEVK-----RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRLSVLDNValplsyrgirlasarqiakvqlekvgleprakyrpaDLSGGQRQRVAIARALVTEPRILL 163
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMAQ--CmDRCLLVRNG 216
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAErlC-DRVAILNNG 171
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
19-218 |
6.65e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 134.87 E-value: 6.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAqaDADQRAVTRNRLlGFVFQS-FNLLPR 96
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLnGLL-LPTSGKVTVDGLDTL--DEENLWEIRKKV-GMVFQNpDNQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 LSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTA 176
Cdd:TIGR04520 93 ATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1796960594 177 QDIIELLTTLNREQFMTLLMVTHDP---AMAqcmDRCLLVRNGGV 218
Cdd:TIGR04520 173 KEVLETIRKLNKEEGITVISITHDMeeaVLA---DRVIVMNKGKI 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-221 |
8.34e-39 |
|
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: 134.06 E-value: 8.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 2 SSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHG-SLVLDGSEVAQAD-ADQRavt 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDvWELR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 rnRLLGFVFQSF--NLLPRLSVLDNValpLS--------YRGIrlaSARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQ 147
Cdd:COG1119 78 --KRIGLVSPALqlRFPRDETVLDVV---LSgffdsiglYREP---TDEQRERARelLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 148 RVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPA-MAQCMDRCLLVRNGGVFDA 221
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGITHVLLLKDGRVVAA 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-218 |
1.99e-38 |
|
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: 136.01 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQSFNLLPRLSVLD 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 102 NvaLPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIE 181
Cdd:TIGR02142 95 N--LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 182 LLTTLNREQFMTLLMVTHDPA-MAQCMDRCLLVRNGGV 218
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQeVLRLADRVVVLEDGRV 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-205 |
2.19e-38 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 133.24 E-value: 2.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLL---N-LIGLLDQpCH--GSLVLDGSEVAQADAD 74
Cdd:COG1117 8 LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrMNDLIPG-ARveGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 75 QRAVTRNrlLGFVFQSFNLLPrLSVLDNVALPLSYRGIRlaSARQI-AKVQ--LEKVGL--EPRAK-YRPA-DLSGGQRQ 147
Cdd:COG1117 87 VVELRRR--VGMVFQKPNPFP-KSIYDNVAYGLRLHGIK--SKSELdEIVEesLRKAALwdEVKDRlKKSAlGLSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 148 RVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFmTLLMVTHDpaMAQ 205
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDY-TIVIVTHN--MQQ 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-219 |
2.42e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 132.40 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 24 SFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTrnrllgFVFQSFNLLPRLSVLDNV 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVS------MLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 104 ALPLSyRGIRLaSARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIE 181
Cdd:PRK10771 93 GLGLN-PGLKL-NAAQREKLHaiARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1796960594 182 LLTTLNREQFMTLLMVTH--DPAmAQCMDRCLLVRNGGVF 219
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHslEDA-ARIAPRSLVVADGRIA 209
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-219 |
3.20e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 136.12 E-value: 3.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTr 80
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPIN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 nrllgFVFQSFNLLPRLSVLDNVALPLsyRGIRLASARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:PRK11607 95 -----MMFQSYALFPHMTVEQNIAFGL--KQDKLPKAEIASRVNemLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 159 PRILLADEPTGNLDG---DTAQdiIELLTTLNREQfMTLLMVTHDPAMAQCMDRCLLVRNGGVF 219
Cdd:PRK11607 168 PKLLLLDEPMGALDKklrDRMQ--LEVVDILERVG-VTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-216 |
3.68e-38 |
|
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: 131.79 E-value: 3.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVL--DGSEVAQADADQRAVT--RNRLLGFVFQSFNLL 94
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASPREILalRRRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPR--AKYrPADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:COG4778 106 PRVSALDVVAEPLLERGVDREEARARARELLARLNLPERlwDLP-PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1796960594 173 GDTAQDIIELLTTLnREQFMTLLMVTHDPA-MAQCMDRCLLVRNG 216
Cdd:COG4778 185 AANRAVVVELIEEA-KARGTAIIGIFHDEEvREAVADRVVDVTPF 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-218 |
4.12e-38 |
|
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: 130.03 E-value: 4.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEA--VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnR 82
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG----D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 LLGFVFQSFNLLPRlSVLDNValplsyrgirlasarqiakvqlekvgleprakyrpadLSGGQRQRVAIARALVTEPRIL 162
Cdd:cd03246 77 HVGYLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-211 |
4.42e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 131.06 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 6 SLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQP--CHGSLVLDGSEVAQADADQRAVtrnr 82
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPAEQRRI---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 llGFVFQSFNLLPRLSVLDNVALPLSyRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:COG4136 79 --GILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCL 211
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-217 |
6.07e-37 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 132.15 E-value: 6.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 7 LHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTrnrllgF 86
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC------M 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 87 VFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADE 166
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 167 PTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGG 217
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKG 213
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
20-216 |
1.09e-36 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 131.35 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnrlLGFVFQSFNLLPRLSV 99
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------IAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 100 LDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDI 179
Cdd:NF040840 90 FENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1796960594 180 IELLTTLNREQFMTLLMVTH--DPAMaQCMDRCLLVRNG 216
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHnfEEAL-SLADRVGIMLNG 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-200 |
6.79e-36 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 128.54 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnRLLGFVFQ----SFNllP 95
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKIQIVFQnpygSLN--P 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 96 RLSVLDNVALPLSYRgIRLASARQIAKVQ--LEKVGLEPRAKYR-PADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PRK11308 108 RKKVGQILEEPLLIN-TSLSAAERREKALamMAKVGLRPEHYDRyPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180
....*....|....*....|....*...
gi 1796960594 173 GDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK11308 187 VSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-220 |
6.86e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.44 E-value: 6.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVT-RWLGGEA-VLQDVSFSLPTGQSCAIVGASGSGKSTLL-NLIGLLDqPCHGSLVLDGSEVAQADA-DQR 76
Cdd:PRK13635 2 KEEIIRVEHISfRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLLL-PEAGTITVGGMVLSEETVwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 avtrnRLLGFVFQS-FNLLPRLSVLDNVALPLSYRGIrlASARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIAR 153
Cdd:PRK13635 81 -----RQVGMVFQNpDNQFVGATVQDDVAFGLENIGV--PREEMVERVDqaLRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 154 ALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGVFD 220
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-216 |
2.02e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 125.93 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 13 WLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQ------PCHGSLVLDGSEVAQADAdqraVTRNRLLGF 86
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDA----IKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 87 VFQSFNLLPRLSVLDNVALPLSYRGIRlaSARQIAKVQ---LEKVGLEPRAKYR---PAD-LSGGQRQRVAIARALVTEP 159
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIAYPLKSHGIK--EKREIKKIVeecLRKVGLWKEVYDRlnsPASqLSGGQQQRLTIARALALKP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 160 RILLADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDP-AMAQCMDRCLLVRNG 216
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPqQVARVADYVAFLYNG 228
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
5-218 |
3.23e-35 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 130.67 E-value: 3.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDqPCHGSLVLDGSEVAQADADQ-Ravtrn 81
Cdd:COG1132 340 IEFENVSfSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLlRFYD-PTSGRILIDGVDIRDLTLESlR----- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 RLLGFVFQSFNLLPRlSVLDNVALplsyrGIRLASARQIAKVqLEKVGLEPRAKYRP-----------ADLSGGQRQRVA 150
Cdd:COG1132 414 RQIGVVPQDTFLFSG-TIRENIRY-----GRPDATDEEVEEA-AKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIA 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 151 IARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:COG1132 487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
8-216 |
4.07e-35 |
|
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: 125.30 E-value: 4.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 8 HGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnRLLGFV 87
Cdd:TIGR02769 15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFR-RDVQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 88 FQ----SFNllPRLSVLDNVALPLSYRgIRLASARQIAKVQ--LEKVGLEPR-AKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:TIGR02769 94 FQdspsAVN--PRMTVRQIIGEPLRHL-TSLDESEQKARIAelLDMVGLRSEdADKLPRQLSGGQLQRINIARALAVKPK 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:TIGR02769 171 LIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFcQRVAVMDKG 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-199 |
4.62e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.37 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQ---ADADQRA 77
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFrspRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 78 VtrnrllGFVFQSFNLLPRLSVLDNVAL---PLSYRGIRLASARQIAKVQLEKVGLE--PRAKYRpaDLSGGQRQRVAIA 152
Cdd:COG1129 81 I------AIIHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDidPDTPVG--DLSVAQQQLVEIA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTH 199
Cdd:COG1129 153 RALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISH 198
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2-216 |
5.80e-35 |
|
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: 123.94 E-value: 5.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 2 SSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSLVLDGSEVAQADADQRAvtr 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRIA--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 nRL-LGFVFQSFNLLPRLSVLDNVALplsyrGIRLASARQIAKVQLEKVG-----LEPRAKYRPADLSGGQRQRVAIARA 154
Cdd:COG0410 77 -RLgIGYVPEGRRIFPSLTVEENLLL-----GAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 155 LVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMA-QCMDRCLLVRNG 216
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREG-VTILLVEQNARFAlEIADRAYVLERG 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-204 |
6.21e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 124.57 E-value: 6.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 13 WLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLL-----DQPCHGSLVLDGSEVAQADADQRAVTRNrlLGFV 87
Cdd:PRK14267 13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRRE--VGMV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 88 FQSFNLLPRLSVLDNVALPLSYRGIrLASARQIAKV---QLEKVGLEPRAKYR----PADLSGGQRQRVAIARALVTEPR 160
Cdd:PRK14267 91 FQYPNPFPHLTIYDNVAIGVKLNGL-VKSKKELDERvewALKKAALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDPAMA 204
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQA 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
20-219 |
9.50e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 124.75 E-value: 9.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLL-NLIGLLdQPCHGSLVLdGSEVAQADADQRAVTRNRL-LGFVFQsF--NLLP 95
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLqHLNGLL-QPTSGTVTI-GERVITAGKKNKKLKPLRKkVGIVFQ-FpeHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 96 RLSVLDNVAL-PLSYrGIRLASARQIAKVQLEKVGLEPRAKYR-PADLSGGQRQRVAIARALVTEPRILLADEPTGNLDG 173
Cdd:PRK13634 100 EETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLPEELLARsPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 174 DTAQDIIELLTTLNREQFMTLLMVTH--DPAmAQCMDRCLLVRNGGVF 219
Cdd:PRK13634 179 KGRKEMMEMFYKLHKEKGLTTVLVTHsmEDA-ARYADQIVVMHKGTVF 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
9.75e-35 |
|
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: 128.94 E-value: 9.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 2 SSIISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqravTR 80
Cdd:TIGR02857 319 ASSLEFSGVSvAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAD----SW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLLGFVFQSFNLLPRlSVLDNVALplsyrGIRLASARQIAKVqLEKVGLEPRAKYRP-----------ADLSGGQRQRV 149
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAG-TIAENIRL-----ARPDASDAEIREA-LERAGLDEFVAALPqgldtpigeggAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 150 AIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLV 213
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAALADRIVVL 529
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-204 |
1.13e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.48 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 3 SIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN----LIGLLDQP-CHGSLVLDGSEVAQADAdqra 77
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEArVSGEVYLDGQDIFKMDV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 78 VTRNRLLGFVFQSFNLLPRLSVLDNVALPLSYRgiRLASAR----QIAKVQLEKVGLEPRAKYR---PA-DLSGGQRQRV 149
Cdd:PRK14247 78 IELRRRVQMVFQIPNPIPNLSIFENVALGLKLN--RLVKSKkelqERVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 150 AIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDPAMA 204
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQA 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
24-218 |
2.01e-34 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 121.89 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 24 SFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTrnrllgFVFQSFNLLPRLSVLDNV 103
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVS------MLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 104 ALPLSyRGIRLASARQIAKVQL-EKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIEL 182
Cdd:TIGR01277 92 GLGLH-PGLKLNAEQQEKVVDAaQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 1796960594 183 LTTLNREQFMTLLMVTHDPA-MAQCMDRCLLVRNGGV 218
Cdd:TIGR01277 171 VKQLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-218 |
2.40e-34 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 123.11 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTR 80
Cdd:PRK11701 3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLL-----GFVFQS--FNLLPRLSVLDNVALPLSYRGIR-LASARQIAKVQLEKVGLEP-RAKYRPADLSGGQRQRVAI 151
Cdd:PRK11701 83 RRRLlrtewGFVHQHprDGLRMQVSAGGNIGERLMAVGARhYGDIRATAGDWLERVEIDAaRIDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 152 ARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGV 218
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLaHRLLVMKQGRV 230
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-219 |
6.63e-34 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 122.04 E-value: 6.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLL-NLIGLL--DQPCHGSLVLDGSEVAQADADQRA 77
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSAGSHIELLGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 78 VTRNRL-LGFVFQSFNLLPRLSVLDNVAL------PLSYRGIRLAS--ARQIAKVQLEKVGLEPRAKYRPADLSGGQRQR 148
Cdd:PRK09984 81 IRKSRAnTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSWFTreQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 149 VAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTH--DPAMAQCmDRCLLVRNGGVF 219
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHqvDYALRYC-ERIVALRQGHVF 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-217 |
8.02e-34 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 123.99 E-value: 8.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIiSLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVtr 80
Cdd:PRK11000 1 MASV-TLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 nrllGFVFQSFNLLPRLSVLDNVALplsyrGIRLASAR---------QIAKV-QLEKVgLEprakYRPADLSGGQRQRVA 150
Cdd:PRK11000 78 ----GMVFQSYALYPHLSVAENMSF-----GLKLAGAKkeeinqrvnQVAEVlQLAHL-LD----RKPKALSGGQRQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 151 IARALVTEPRILLADEPTGNLDGD-TAQDIIElLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGG 217
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAAlRVQMRIE-ISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAG 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-218 |
8.14e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 124.76 E-value: 8.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQ-ADADQRAVTRNRLlGFVFQSFNLLPRLS 98
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRRKKI-AMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1796960594 179 IIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGV 218
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIgDRIAIMQNGEV 243
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
18-218 |
9.06e-34 |
|
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: 120.39 E-value: 9.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 18 AVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqRAVTRnRLLGFVFQSfnllPRL 97
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLR-RNIGYVPQD----VTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 ---SVLDNVALPLSY-------RGIRLASARQIakVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEP 167
Cdd:cd03245 90 fygTLRDNITLGAPLadderilRAAELAGVTDF--VNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 168 TGNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-218 |
1.24e-33 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 119.67 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqravtRNRLLGFVFQSFNL-LPRL 97
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE-------RRKSIGYVMQDVDYqLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 SVLDNValplsYRGIRLASAR-QIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTA 176
Cdd:cd03226 88 SVREEL-----LLGLKELDAGnEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNM 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 177 QDIIELLTTLNREQfMTLLMVTHDPA-MAQCMDRCLLVRNGGV 218
Cdd:cd03226 163 ERVGELIRELAAQG-KAVIVITHDYEfLAKVCDRVLLLANGAI 204
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-218 |
1.25e-33 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 121.33 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 8 HGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnRLLGFV 87
Cdd:PRK10419 16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFR-RDIQMV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 88 FQ----SFNllPRLSVLDNVALPLSYRgIRLASARQIAKVQ--LEKVGLEPR-AKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:PRK10419 95 FQdsisAVN--PRKTVREIIREPLRHL-LSLDKAERLARASemLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQ--CmDRCLLVRNGGV 218
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVErfC-QRVMVMDNGQI 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
19-203 |
2.05e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 120.71 E-value: 2.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRLLGFVFQ----SFNll 94
Cdd:COG4167 28 AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRC----KHIRMIFQdpntSLN-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSV---LDnvaLPLsyrgiRL-----ASARQIAKVQ-LEKVGLEP-RAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:COG4167 102 PRLNIgqiLE---EPL-----RLntdltAEEREERIFAtLRLVGLLPeHANFYPHMLSSGQKQRVALARALILQPKIIIA 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAM 203
Cdd:COG4167 174 DEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGI 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-200 |
4.75e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 124.43 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 12 RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKST----LLNLIglldqPCHGSLVLDGSEVAQADADQRAVTRNRLlGFV 87
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRI-QVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 88 FQSFN--LLPRLSVLDNVALPLSYRGIRLASARQIAKV--QLEKVGLEPRAKYR-PADLSGGQRQRVAIARALVTEPRIL 162
Cdd:PRK15134 368 FQDPNssLNPRLNVLQIIEEGLRVHQPTLSAAQREQQViaVMEEVGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLI 447
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-172 |
7.33e-33 |
|
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: 117.68 E-value: 7.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQScAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAqadaDQRAVTRnRLL 84
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR-RRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
....*...
gi 1796960594 165 DEPTGNLD 172
Cdd:cd03264 155 DEPTAGLD 162
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-218 |
7.75e-33 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 121.10 E-value: 7.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTR-WLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADAdqravtRNRL 83
Cdd:PRK11650 4 LKLQAVRKsYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------ADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRLSVLDNVALPLSYRGI-------RLASARQIakvqLEkvgLEPRAKYRPADLSGGQRQRVAIARALV 156
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRGMpkaeieeRVAEAARI----LE---LEPLLDRKPRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 157 TEPRILLADEPTGNLDGD-TAQDIIELLtTLNREQFMTLLMVTHDPAMAQCM-DRcLLVRNGGV 218
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKlRVQMRLEIQ-RLHRRLKTTSLYVTHDQVEAMTLaDR-VVVMNGGV 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
19-218 |
9.97e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.94 E-value: 9.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSLVLDGSEVAQADADQravTRNRLlGFVFQS-FNLLPR 96
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKiLTGLL-KPQSGEIKIDGITISKENLKE---IRKKI-GIIFQNpDNQFIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 LSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTA 176
Cdd:PRK13632 99 ATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1796960594 177 QDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:PRK13632 179 REIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-200 |
1.39e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 118.65 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIG---LLDQpchGSLVLDGSEVAQADADQRAvtrnRLLGFVFQsfNLL- 94
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAgslPPDS---GSILIDGKDVTKLPEYKRA----KYIGRVFQ--DPMm 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 ---PRLSVLDNVALPLS---YRGIRLA---SARQIAKVQLEKV--GLEPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:COG1101 92 gtaPSMTIEENLALAYRrgkRRGLRRGltkKRRELFRELLATLglGLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLL 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:COG1101 172 LDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-212 |
5.90e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.02 E-value: 5.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLvldgsevaqadadqrAVTRNRLLGFVFQSFNL- 93
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 --LPrLSVLDNVALPL-SYRGI--RL-ASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEP 167
Cdd:NF040873 68 dsLP-LTVRDLVAMGRwARRGLwrRLtRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1796960594 168 TGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPAMAQCMDRCLL 212
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARG-ATVVVVTHDLELVRRADPCVL 190
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-218 |
7.91e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.14 E-value: 7.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEA---VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADA-DQR 76
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 avtrnRLLGFVFQS-FNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARAL 155
Cdd:PRK13650 81 -----HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 156 VTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-216 |
1.11e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.52 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSLVLDGSEVAQ---ADAdqr 76
Cdd:COG3845 2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKiLYGLY-QPDSGEILIDGKPVRIrspRDA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 avtRNRLLGFVFQSFNLLPRLSVLDNVAL---PLSYRGIRLASARQIAKVQLEKVGLE--PRAKyrPADLSGGQRQRVAI 151
Cdd:COG3845 78 ---IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDvdPDAK--VEDLSVGEQQRVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 152 ARALVTEPRILLADEPTGNLdgdTAQDIIELLTTLNR--EQFMTLLMVTH--DPAMAQCmDRCLLVRNG 216
Cdd:COG3845 153 LKALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHklREVMAIA-DRVTVLRRG 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-219 |
1.98e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.18 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRLL 84
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA----KRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVAL---PLSyRGiRLaSARQIAKVQ--LEKVGLEPRAkYRPAD-LSGGQRQRVAIARALVTE 158
Cdd:COG4604 78 AILRQENHINSRLTVRELVAFgrfPYS-KG-RL-TAEDREIIDeaIAYLDLEDLA-DRYLDeLSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGVF 219
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYaDHIVAMKDGRVV 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
16-216 |
2.95e-31 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 119.95 E-value: 2.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdqPCHGSLVLDGSEVAQADADQ-RavtrnRLLGFVFQSfNL 93
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELRELDPESwR-----KHLSWVGQN-PQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRLSVLDNVALplsyrGIRLASARQIAKVqLEKV-----------GLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:PRK11174 434 LPHGTLRDNVLL-----GNPDASDEQLQQA-LENAwvseflpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQDG 559
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
4-221 |
3.28e-31 |
|
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: 114.54 E-value: 3.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVL---DGSEV---AQADADQRA 77
Cdd:TIGR02323 3 LLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELelyQLSEAERRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 78 VTRNRLlGFVFQSF--NLLPRLSVLDNVALPLSYRGIR-LASARQIAKVQLEKVGLEP-RAKYRPADLSGGQRQRVAIAR 153
Cdd:TIGR02323 83 LMRTEW-GFVHQNPrdGLRMRVSAGANIGERLMAIGARhYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 154 ALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGVFDA 221
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLaQRLLVMQQGRVVES 230
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
15-218 |
3.32e-31 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 114.16 E-value: 3.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSLVLDGSEVAQADADQRAvtrNRLLGFVFQSFNL 93
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLL-PVKSGSIRLDGEDITKLPPHERA---RAGIAYVPQGREI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRLSVLDNVALPLSYRGirlASARQIAKVQLE--KVGLEPRAKyRPADLSGGQRQRVAIARALVTEPRILLADEPTGNL 171
Cdd:TIGR03410 87 FPRLTVEENLLTGLAALP---RRSRKIPDEIYElfPVLKEMLGR-RGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1796960594 172 DGDTAQDIIELLTTLNREQFMTLLMVTH--DPAMaQCMDRCLLVRNGGV 218
Cdd:TIGR03410 163 QPSIIKDIGRVIRRLRAEGGMAILLVEQylDFAR-ELADRYYVMERGRV 210
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
18-216 |
3.57e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 119.97 E-value: 3.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 18 AVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAD-ADQRavtrnRLLGFVFQSfnllPR 96
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDpADLR-----RNIGYVPQD----PR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 L---SVLDNVALplsyrGIRLASARQIAKVqLEKVGLEPRAKYRP-----------ADLSGGQRQRVAIARALVTEPRIL 162
Cdd:TIGR03375 550 LfygTLRDNIAL-----GAPYADDEEILRA-AELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPIL 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:TIGR03375 624 LLDEPTSAMDNRSEERFKDRLKRWLAG--KTLVLVTHRTSLLDLVDRIIVMDNG 675
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-200 |
6.53e-31 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 114.48 E-value: 6.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAqadadqrAVTR 80
Cdd:PRK11831 4 VANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIP-------AMSR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRL------LGFVFQSFNLLPRLSVLDNVALPLSyRGIRLASA--RQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIA 152
Cdd:PRK11831 77 SRLytvrkrMSMLFQSGALFTDMNVFDNVAYPLR-EHTQLPAPllHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK11831 156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-220 |
7.25e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.51 E-value: 7.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 17 EAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLL--DQPCHGSLVLDGSEVaqaDADQRAVTRNRLlGFVFQS-FN 92
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLInGLLlpDDNPNSKITVDGITL---TAKTVWDIREKV-GIVFQNpDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PRK13640 96 QFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 173 GDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGVFD 220
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLA 223
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-218 |
1.41e-30 |
|
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: 117.93 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAvtrnRLLGFVFQSFNL 93
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELG----RHIGYLPQDVEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRlSVLDNVAlplsyrgiRLASAR--------QIAKV-----QLEKvGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:COG4618 418 FDG-TIAENIA--------RFGDADpekvvaaaKLAGVhemilRLPD-GYDTRIGEGGARLSGGQRQRIGLARALYGDPR 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-216 |
1.45e-30 |
|
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: 112.32 E-value: 1.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqRAVTRNRlLGFVFQSFNLL 94
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSM-IGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRlSVLDNVALPLSY----RGIRLASARQIAKV--QLEKvGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:cd03254 90 SG-TIMENIRLGRPNatdeEVIEAAKEAGAHDFimKLPN-GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 169 GNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:cd03254 168 SNIDTETEKLIQEALEKLMKGR--TSIIIAHRLSTIKNADKILVLDDG 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-201 |
2.61e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 116.69 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 12 RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDqPCHGSLVLDGSEVAQADADQRAvtrnRLLGFVFQS 90
Cdd:TIGR02868 343 GYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLaGLLD-PLQGEVTLDGVPVSSLDQDEVR----RRVSVCAQD 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 91 FNLLPRlSVLDNVALplsyrGIRLASARQIAKVqLEKVGLEPRAKYRP-----------ADLSGGQRQRVAIARALVTEP 159
Cdd:TIGR02868 418 AHLFDT-TVRENLRL-----ARPDATDEELWAA-LERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1796960594 160 RILLADEPTGNLDGDTAQDIIELLttLNREQFMTLLMVTHDP 201
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-221 |
2.66e-30 |
|
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: 111.81 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEA--VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqravTRNR 82
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPA----WLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 LLGFVFQSfNLLPRLSVLDNVALP---LSYRGI----RLASARQ-IAKVQLekvGLEPRAKYRPADLSGGQRQRVAIARA 154
Cdd:cd03252 77 QVGVVLQE-NVLFNRSIRDNIALAdpgMSMERVieaaKLAGAHDfISELPE---GYDTIVGEQGAGLSGGQRQRIAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 155 LVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNGGVFDA 221
Cdd:cd03252 153 LIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-218 |
4.99e-30 |
|
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: 116.06 E-value: 4.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQ--PCHGSLVLD------------------ 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 65 -----GSEVAQADAD----QRAVTRN--RLLGFVFQ-SFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEP 132
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDfwnlSDKLRRRirKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 133 RAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDP-AMAQCMDRCL 211
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPeVIEDLSDKAI 240
|
....*..
gi 1796960594 212 LVRNGGV 218
Cdd:TIGR03269 241 WLENGEI 247
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-216 |
1.44e-29 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 110.59 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAVTRNRL 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 -----LGFVFqsfnllprlSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRA--KYRpaDLSGGQRQRVAIARALV 156
Cdd:COG4559 81 pqhssLAFPF---------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAgrSYQ--TLSGGEQQRVQLARVLA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 157 -------TEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFmTLLMVTHDPAM-AQCMDRCLLVRNG 216
Cdd:COG4559 150 qlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGG-GVVAVLHDLNLaAQYADRILLLHQG 216
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-221 |
1.66e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 3 SIISLHGVTRWLGGEA--VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAD-ADQRavt 79
Cdd:PRK13648 6 SIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNfEKLR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 rnRLLGFVFQS-FNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:PRK13648 83 --KHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGVFDA 221
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-216 |
1.72e-29 |
|
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: 107.51 E-value: 1.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADAdQRAvtRNRL 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLY-KPDSGEILVDGKEVSFASP-RDA--RRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQsfnllprlsvldnvalplsyrgirlasarqiakvqlekvgleprakyrpadLSGGQRQRVAIARALVTEPRILL 163
Cdd:cd03216 77 IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTH--DPAMAQCmDRCLLVRNG 216
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrlDEVFEIA-DRVTVLRDG 158
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
21-216 |
2.43e-29 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 109.38 E-value: 2.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 21 QDVSFSLPTGQSCAIVGASGSGKS-TLLNLIGLLDQ---PCHGSLVLDGSEVAQADadqravTRNRLLGFVFQS----FN 92
Cdd:TIGR02770 3 QDLNLSLKRGEVLALVGESGSGKSlTCLAILGLLPPgltQTSGEILLDGRPLLPLS------IRGRHIATIMQNprtaFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 llPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRA---KYRPADLSGGQRQRVAIARALVTEPRILLADEPTG 169
Cdd:TIGR02770 77 --PLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 170 NLDGDTAQDIIELLTTLNREQFMTLLMVTHD-PAMAQCMDRCLLVRNG 216
Cdd:TIGR02770 155 DLDVVNQARVLKLLRELRQLFGTGILLITHDlGVVARIADEVAVMDDG 202
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-216 |
1.50e-28 |
|
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: 106.60 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqravtRNRLl 84
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------RNRI- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQCM-DRCLLVRNG 216
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELcDRVLLLNKG 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-218 |
1.66e-28 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 106.68 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 18 AVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQadaDQRAVTRNrlLGFVFQSFNLLPRL 97
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---EPAEARRR--LGFVSDSTGLYDRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 SVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQ 177
Cdd:cd03266 94 TARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 178 DIIELLTTLnREQFMTLLMVTH--DPAMAQCmDRCLLVRNGGV 218
Cdd:cd03266 174 ALREFIRQL-RALGKCILFSTHimQEVERLC-DRVVVLHRGRV 214
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-200 |
1.83e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 111.70 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 7 LHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSE----VAQadaDQRAVTRNR 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigyLPQ---EPPLDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 LLGFVFQSFN----LLPRLSVLDNVALPLSYRGIRLASA-------------RQIAKVqLEKVGLEPRAKYRP-ADLSGG 144
Cdd:COG0488 78 VLDTVLDGDAelraLEAELEELEAKLAEPDEDLERLAELqeefealggweaeARAEEI-LSGLGFPEEDLDRPvSELSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 145 QRQRVAIARALVTEPRILLADEPTGNLDGDTaqdiIELLttlnrEQFM-----TLLMVTHD 200
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWL-----EEFLknypgTVLVVSHD 208
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
19-218 |
4.60e-28 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 110.99 E-value: 4.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADAdqraVTRNRLLGFVFQSfNLLPRLS 98
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADP----AWLRRQMGVVLQE-NVLFSRS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALplSYRGIRLASARQIAK-------VQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNL 171
Cdd:TIGR01846 547 IRDNIAL--CNPGAPFEHVIHAAKlagahdfISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSAL 624
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1796960594 172 DGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:TIGR01846 625 DYESEALIMRNMREICRGR--TVIIIAHRLSTVRACDRIIVLEKGQI 669
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-199 |
4.85e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 108.42 E-value: 4.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQSFNLLPRLSVLD 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 102 NvalpLSYrGIRLASARQIAK-VQLekVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDII 180
Cdd:PRK11144 96 N----LRY-GMAKSMVAQFDKiVAL--LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170
....*....|....*....
gi 1796960594 181 ELLTTLNREQFMTLLMVTH 199
Cdd:PRK11144 169 PYLERLAREINIPILYVSH 187
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-200 |
5.67e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.57 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 2 SSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqravTRN 81
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE----IYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 RLLGFVFQSfnllPRL---SVLDNVALPLSYRGIRLASARQIAkvQLEKVGL-EPRAKYRPADLSGGQRQRVAIARALVT 157
Cdd:PRK10247 81 QQVSYCAQT----PTLfgdTVYDNLIFPWQIRNQQPDPAIFLD--DLERFALpDTILTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 158 EPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-216 |
6.41e-28 |
|
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: 104.99 E-value: 6.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVaqadadQRAVTRNRLL 84
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY------QKNIEALRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIakvqLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPA-MAQCMDRCLLVRNG 216
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSeIQKVADRIGIINKG 202
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-217 |
6.56e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.67 E-value: 6.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNrlLGFVFQ--SFNLLPRl 97
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKK--VGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 SVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEpRAKYR---PADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLD-YEDYKdksPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 175 TAQDIIELLTTLNREQFMTLLMVTHD-PAMAQCMDRcLLVRNGG 217
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADR-IIVMNKG 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-211 |
6.74e-28 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.87 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSLVLDGSEVAQADADQRAVTRNRLlGFVFQ----SFNllPR 96
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARaIIGLV-KATDGEVAWLGKDLLGMKDDEWRAVRSDI-QMIFQdplaSLN--PR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 LSVLDNVALPLS--YRGIRLASARQIAKVQLEKVGLEPRAKYR-PADLSGGQRQRVAIARALVTEPRILLADEPTGNLDG 173
Cdd:PRK15079 115 MTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLLPNLINRyPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190
....*....|....*....|....*....|....*....
gi 1796960594 174 DTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM-DRCL 211
Cdd:PRK15079 195 SIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHIsDRVL 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-200 |
7.34e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 106.32 E-value: 7.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTL-LNLIGLLdQPCHGSLVLDGSEVaqaDADQRAVTRNR-LLGFVFQ-SFN 92
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGIL-KPTSGEVLIKGEPI---KYDKKSLLEVRkTVGIVFQnPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPRLSVLDNVAL-PLSYrGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNL 171
Cdd:PRK13639 90 QLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168
|
170 180
....*....|....*....|....*....
gi 1796960594 172 DGDTAQDIIELLTTLNREQfMTLLMVTHD 200
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEG-ITIIISTHD 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
14-216 |
7.59e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.01 E-value: 7.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAVTRNRL-----LGFV 87
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRRAVLpqhssLSFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 88 FqsfnllprlSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALV------TEPRI 161
Cdd:PRK13548 91 F---------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRW 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMA-QCMDRCLLVRNG 216
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAaRYADRIVLLHQG 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
19-218 |
1.59e-27 |
|
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: 104.12 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRavtrnRLLGFVFQSFNLLPRLS 98
Cdd:cd03263 17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-----QSLGYCPQFDALFDELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:cd03263 92 VREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1796960594 179 IIELLTTLNREQfmTLLMVTHDPAMAQ--CmDRCLLVRNGGV 218
Cdd:cd03263 172 IWDLILEVRKGR--SIILTTHSMDEAEalC-DRIAIMSDGKL 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-216 |
1.86e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKS-TLLNLIGLLDQP----CHGSLVLDGSEVAQADADQ-RAVTRNRLlGFVFQS-- 90
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTlRGVRGNKI-AMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 91 FNLLPRLSVLDNVALPLS-YRGIRLASARQIAKVQLEKVGLEpRAKYRPAD----LSGGQRQRVAIARALVTEPRILLAD 165
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIR-QAAKRLTDyphqLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 166 EPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMA-QCMDRCLLVRNG 216
Cdd:PRK15134 182 EPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrKLADRVAVMQNG 233
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-199 |
2.01e-27 |
|
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: 104.23 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSevaqadaDQRAVTRNRL---LGFVFQS---FN 92
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ-------DIREVTLDSLrraIGVVPQDtvlFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LlprlSVLDNVAlplsYrGIRLASARQI---AKV-QLEKVGLEPRAKY------RPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:cd03253 89 D----TIGYNIR----Y-GRPDATDEEVieaAKAaQIHDKIMRFPDGYdtivgeRGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTL--NReqfmTLLMVTH 199
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVskGR----TTIVIAH 194
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-216 |
2.89e-27 |
|
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: 103.60 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVlQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQadaDQRAVTRNrl 83
Cdd:cd03265 1 IEVENLVKKYGDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR---EPREVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTH--DPAMAQCmDRCLLVRNG 216
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHymEEAEQLC-DRVAIIDHG 208
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-218 |
3.41e-27 |
|
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: 103.50 E-value: 3.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 9 GVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDQP--CHGSLVLDGSEVaqadadQRAVTRNRLlG 85
Cdd:cd03234 12 KAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQPR------KPDQFQKCV-A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 86 FVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAK----VQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRI 161
Cdd:cd03234 85 YVRQDDILLPGLTVRETLTYTAILRLPRKSSDAIRKKrvedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPA--MAQCMDRCLLVRNGGV 218
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRN-RIVILTIHQPRsdLFRLFDRILLLSSGEI 222
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-218 |
6.40e-27 |
|
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: 101.86 E-value: 6.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 12 RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDqPCH--GSLVLDGSevaqadaDQRAVTRNRLLGFVF 88
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRT-GLGvsGEVLINGR-------PLDKRSFRKIIGYVP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 89 QSFNLLPRLSVLDNVALPLSYRGIrlasarqiakvqlekvgleprakyrpadlSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:cd03213 89 QDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPT 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 169 GNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPA--MAQCMDRCLLVRNGGV 218
Cdd:cd03213 140 SGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPSseIFELFDKLLLLSQGRV 190
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
19-218 |
7.00e-27 |
|
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: 103.00 E-value: 7.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRavtrNRLLGFVFQSFNLLPRlS 98
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL----RSQIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSY-------RGIRLASARQ-IAKvqLEKvGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGN 170
Cdd:cd03249 93 IAENIRYGKPDatdeeveEAAKKANIHDfIMS--LPD-GYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 171 LDGDTAQDIIELLTTLNREqfMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:cd03249 170 LDAESEKLVQEALDRAMKG--RTTIVIAHRLSTIRNADLIAVLQNGQV 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-218 |
9.03e-27 |
|
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: 102.55 E-value: 9.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRavtrNRLLGFVFQSFNLLPRlS 98
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQEPVLFAR-S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGI-RLASARQIAK----VQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDG 173
Cdd:cd03248 104 LQDNIAYGLQSCSFeCVKEAAQKAHahsfISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1796960594 174 DTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:cd03248 184 ESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
19-216 |
9.22e-27 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 107.05 E-value: 9.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqravTRNRLLGFVFQSFNLLPRlS 98
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE----TFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVAlplsyRGIRLASARQI-AKVQLEKV---------GLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:TIGR01842 408 VAENIA-----RFGENADPEKIiEAAKLAGVhelilrlpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 169 GNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:TIGR01842 483 SNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVLQDG 529
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
17-218 |
1.05e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 103.33 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 17 EAVlQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvTRNRLlgfVFQ--SFNLL 94
Cdd:PRK15112 27 EAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRS-QRIRM---IFQdpSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPLSYRGIRLASARQIAKVQ-LEKVGLEP-RAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PRK15112 102 PRQRISQILDFPLRLNTDLEPEQREKQIIEtLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1796960594 173 GDTAQDIIELLTTLNREQFMTLLMVT-HDPAMAQCMDRCLLVRNGGV 218
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTqHLGMMKHISDQVLVMHQGEV 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-218 |
1.56e-26 |
|
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: 101.92 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVaqadadqRAVTRN---RLLGFVFQS-- 90
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV-------RDYTLAslrRQIGLVSQDvf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 91 -FNLlprlSVLDNVALplSYRGIRLASARQIAKV--------QLEKvGLEPRAKYRPADLSGGQRQRVAIARALVTEPRI 161
Cdd:cd03251 87 lFND----TVAENIAY--GRPGATREEVEEAARAanahefimELPE-GYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 162 LLADEPTGNLDGDT---AQDIIELLTTlNReqfmTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:cd03251 160 LILDEATSALDTESerlVQAALERLMK-NR----TTFVIAHRLSTIENADRIVVLEDGKI 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
16-218 |
1.59e-26 |
|
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: 106.75 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqRAVTRnrllgfvfQSFNLLP 95
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLR--------QFINYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 96 RL------SVLDNVALPlSYRGI---RLASARQIAKVQ--LEKV--GLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:TIGR01193 555 QEpyifsgSILENLLLG-AKENVsqdEIWAACEIAEIKddIENMplGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREqfmTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-216 |
2.20e-26 |
|
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: 100.08 E-value: 2.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADAdqravTRNRLLGFVFQSFNLLPRlS 98
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-----ALSSLISVLNQRPYLFDT-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNValplsyrGIRLasarqiakvqlekvgleprakyrpadlSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:cd03247 91 LRNNL-------GRRF---------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 179 IIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:cd03247 137 LLSLIFEVLKDK--TLIWITHHLTGIEHMDKILFLENG 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
19-216 |
8.55e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 101.70 E-value: 8.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVL---DGSEVAQADADQRAVTRN-------------- 81
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVLEKLviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 ---RLLGFVFQ--SFNLLPRLSVLDNVALPLSYrGIRLASARQIAKVQLEKVGL-EPRAKYRPADLSGGQRQRVAIARAL 155
Cdd:PRK13651 102 eirRRVGVVFQfaEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 156 VTEPRILLADEPTGNLDGDTAQDIIELLTTLNrEQFMTLLMVTHDPAMA-QCMDRCLLVRNG 216
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVlEWTKRTIFFKDG 241
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-199 |
9.35e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 101.42 E-value: 9.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQadadqRAVTR 80
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-----RARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLLGFVFQSFNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTH 199
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTH 196
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
15-200 |
9.78e-26 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.83 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRLLGFVFQSFNLL 94
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVAL------PLSYRGiRLASARQIAKVqLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:PRK10253 94 GDITVQELVARgryphqPLFTRW-RKEDEEAVTKA-MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190
....*....|....*....|....*....|..
gi 1796960594 169 GNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKGYTLAAVLHD 203
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
22-200 |
1.99e-25 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 100.95 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPTGQSCAIVGASGSGKS-TLLNLIGLLDQPCH--GSLVLDGSEVAQADADQRAVTRNRLLGFVFQ----SFNll 94
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREILNLPEKELNKLRAEQISMIFQdpmtSLN-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPLS-YRGIRLASARQIAKVQLEKVGLePRAKYR----PADLSGGQRQRVAIARALVTEPRILLADEPTG 169
Cdd:PRK09473 112 PYMRVGEQLMEVLMlHKGMSKAEAFEESVRMLDAVKM-PEARKRmkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTT 190
|
170 180 190
....*....|....*....|....*....|.
gi 1796960594 170 NLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK09473 191 ALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
19-219 |
3.39e-25 |
|
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: 98.38 E-value: 3.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRL-LGFVFQSFNLLPRL 97
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA----RLgIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 SVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQ 177
Cdd:cd03218 91 TVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 178 DIIELLTTLnREQFMTLLMVTH--DPAMAQCmDRCLLVRNGGVF 219
Cdd:cd03218 171 DIQKIIKIL-KDRGIGVLITDHnvRETLSIT-DRAYIIYEGKVL 212
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
15-187 |
3.73e-25 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 102.73 E-value: 3.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAqaDADQRAVTRNrlLGFVFQSFNLL 94
Cdd:TIGR03797 464 DGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA--GLDVQAVRRQ--LGVVLQNGRLM 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRlSVLDNVA--LPLSyrgirLASARQIAKVqlekVGLEPRAKYRP-----------ADLSGGQRQRVAIARALVTEPRI 161
Cdd:TIGR03797 540 SG-SIFENIAggAPLT-----LDEAWEAARM----AGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLIARALVRKPRI 609
|
170 180
....*....|....*....|....*.
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLN 187
Cdd:TIGR03797 610 LLFDEATSALDNRTQAIVSESLERLK 635
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-199 |
3.75e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 100.68 E-value: 3.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSI-ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSL-VLDGSEVAQADADQRAV 78
Cdd:PRK13536 37 MSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 trnrllGFVFQSFNLLPRLSVLDNVALPLSYRGIrlaSARQIAKV---QLEKVGLEPRAKYRPADLSGGQRQRVAIARAL 155
Cdd:PRK13536 117 ------GVVPQFDNLDLEFTVRENLLVFGRYFGM---STREIEAVipsLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 156 VTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTH 199
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTH 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
15-200 |
3.90e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 98.93 E-value: 3.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnRLLGFVFQSfNLL 94
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQH-HLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PR-LSVLDNVAL---P-LSYRGiRLASA-RQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:PRK11231 88 PEgITVRELVAYgrsPwLSLWG-RLSAEdNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
170 180 190
....*....|....*....|....*....|..
gi 1796960594 169 GNLDGDTAQDIIELLTTLNrEQFMTLLMVTHD 200
Cdd:PRK11231 167 TYLDINHQVELMRLMRELN-TQGKTVVTVLHD 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-199 |
4.83e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 4.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQ-SFNLLPRLS 98
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGL-EPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQ 177
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180
....*....|....*....|..
gi 1796960594 178 DIIELLTTLNREQfMTLLMVTH 199
Cdd:PRK13649 183 ELMTLFKKLHQSG-MTIVLVTH 203
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-205 |
5.13e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.24 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRnRLLGFVFQS--FNLLPRL 97
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 SVLDNVALPLSYRGIRL--ASARQIAKVqLEKVGLEPRAKYR-PADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPgkAAAARVAWL-LERVGLLPEHAWRyPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190
....*....|....*....|....*....|.
gi 1796960594 175 TAQDIIELLTTLNREQFMTLLMVTHDPAMAQ 205
Cdd:PRK10261 498 IRGQIINLLLDLQRDFGIAYLFISHDMAVVE 528
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
12-200 |
1.06e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.38 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 12 RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLL-NLIGLLdQPCHGSLVLDGSEVaqaDADQRAVTRNR-LLGFVFQ 89
Cdd:PRK13636 14 NYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFqNLNGIL-KPSSGRILFDGKPI---DYSRKGLMKLReSVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 90 S-FNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPrAKYRPAD-LSGGQRQRVAIARALVTEPRILLADEP 167
Cdd:PRK13636 90 DpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190
....*....|....*....|....*....|...
gi 1796960594 168 TGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-220 |
1.31e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 100.65 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 23 VSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSL-VLDGSE---VAQADADQRAVTRnRLLGFVFQSFNLLPRLS 98
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEwvdMTKPGPDGRGRAK-RYIGILHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLsyrGIRLAS--ARQIAKVQLEKVGLEPRA------KYrPADLSGGQRQRVAIARALVTEPRILLADEPTGN 170
Cdd:TIGR03269 382 VLDNLTEAI---GLELPDelARMKAVITLKMVGFDEEKaeeildKY-PDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 171 LDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQ--CmDRCLLVRNGGVFD 220
Cdd:TIGR03269 458 MDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLdvC-DRAALMRDGKIVK 508
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1-216 |
2.50e-24 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 96.69 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVlQDVSFSLPTGQSCAIVGASGSGKS-TLLNLIGLLD---QPCHGSLVLDGSEVAQADadqr 76
Cdd:PRK10418 1 MPQQIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPVAPCA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 avTRNRLLGFVFQ----SFNllPRLSVLDNVALPLSYRGiRLASARQIAKVqLEKVGLEPRA---KYRPADLSGGQRQRV 149
Cdd:PRK10418 76 --LRGRKIATIMQnprsAFN--PLHTMHTHARETCLALG-KPADDATLTAA-LEAVGLENAArvlKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 150 AIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD-PAMAQCMDRCLLVRNG 216
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHG 217
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-205 |
3.26e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 96.38 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLL---NLIGLLDQPCH--GSLVLDGSEVAQADADq 75
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPEVTitGSIVYNGHNIYSPRTD- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 76 rAVTRNRLLGFVFQSFNLLPrLSVLDNVALPLSYRGIR-LASARQIAKVQLEKVGLEPRAKYRPAD----LSGGQRQRVA 150
Cdd:PRK14239 81 -TVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 151 IARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFmTLLMVTHdpAMAQ 205
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDY-TMLLVTR--SMQQ 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
3-187 |
3.83e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 95.87 E-value: 3.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 3 SIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLDGSEVAQADADQRAvtrn 81
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIvGLV-KPDSGRIFLDGEDITHLPMHKRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 RL-LGF------VFQsfnllpRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARA 154
Cdd:COG1137 77 RLgIGYlpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 1796960594 155 LVTEPRILLADEPTGNLD----GDtAQDIIELLTTLN 187
Cdd:COG1137 151 LATNPKFILLDEPFAGVDpiavAD-IQKIIRHLKERG 186
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-200 |
5.75e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 96.44 E-value: 5.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQ-SFNLLPRLS 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVAL-PLSYrGIRLASARQIAKVQLEKVGL-EPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTA 176
Cdd:PRK13641 103 VLKDVEFgPKNF-GFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180
....*....|....*....|....
gi 1796960594 177 QDIIELLTTLNREQFmTLLMVTHD 200
Cdd:PRK13641 182 KEMMQLFKDYQKAGH-TVILVTHN 204
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-216 |
6.46e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqravTR 80
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAS------TT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRL---LGFVFQSFNLLPRLSVLDNV---ALPLSYRGIRLASARQIAKVQLEKVGLE--PRAKYRpaDLSGGQRQRVAIA 152
Cdd:PRK11288 75 AALaagVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDidPDTPLK--YLSIGQRQMVEIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTH--DPAMAQCmDRCLLVRNG 216
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHrmEEIFALC-DAITVFKDG 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-220 |
8.54e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 8.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdQPCHGSLVLdGSEVAQADADQravtrnr 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLaGEL-EPDSGTVKL-GETVKIGYFDQ------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 llgfvfQSFNLLPRLSVLDNVAlpLSYRGIRLASARQIakvqLEKVGLEPRAKYRP-ADLSGGQRQRVAIARALVTEPRI 161
Cdd:COG0488 386 ------HQEELDPDKTVLDELR--DGAPGGTEQEVRGY----LGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNV 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 162 LLADEPTGNLDGDTaqdiIELLttlnrEQFM-----TLLMVTHDPA-MAQCMDRCLLVRNGGVFD 220
Cdd:COG0488 454 LLLDEPTNHLDIET----LEAL-----EEALddfpgTVLLVSHDRYfLDRVATRILEFEDGGVRE 509
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-216 |
1.22e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 97.97 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQ-RAvtrnrLLGFVFQSFNL 93
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAlRQ-----AISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRlSVLDNVALplsyrGIRLASARQIAKVqLEKVGLEPRAKY------------RPadLSGGQRQRVAIARALVTEPRI 161
Cdd:PRK11160 426 FSA-TLRDNLLL-----AAPNASDEALIEV-LQQVGLEKLLEDdkglnawlgeggRQ--LSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLttlnrEQFM---TLLMVTHD-PAMAQcMDRCLLVRNG 216
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELL-----AEHAqnkTVLMITHRlTGLEQ-FDRICVMDNG 549
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
15-205 |
1.85e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 94.46 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLL---NLIGLLDQPC--HGSLVLDGSEVAQADADQRAVTRNrlLGFVFQ 89
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGFrvEGKVTFHGKNLYAPDVDPVEVRRR--IGMVFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 90 SFNLLPRlSVLDNVAL------------PLSYRGIRLASARQIAKVQLEKVGLEprakyrpadLSGGQRQRVAIARALVT 157
Cdd:PRK14243 99 KPNPFPK-SIYDNIAYgaringykgdmdELVERSLRQAALWDEVKDKLKQSGLS---------LSGGQQQRLCIARAIAV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 158 EPRILLADEPTGNLDGDTAQDIIELLTTLnREQFmTLLMVTHDpaMAQ 205
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMHEL-KEQY-TIIIVTHN--MQQ 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
19-199 |
2.39e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSL-VLD-------GSEVAQADADQRAVTR----NRLLGF 86
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqVGDiyigdkkNNHELITNPYSKKIKNfkelRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 87 VFQ--SFNLLPRLSVLDNVALPLSYrGIRLASARQIAKVQLEKVGL-EPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190
....*....|....*....|....*....|....*.
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTH 199
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANN-KTVFVITH 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-201 |
2.60e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGsevaQADADQRAVTRNRLLGfvFQSFnLL 94
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG----GDIDDPDVAEACHYLG--HRNA-MK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALplsYRGIRLASARQIAKVqLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:PRK13539 86 PALTVAENLEF---WAAFLGGEELDIAAA-LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....*..
gi 1796960594 175 TAQDIIELLTTlNREQFMTLLMVTHDP 201
Cdd:PRK13539 162 AVALFAELIRA-HLAQGGIVIAATHIP 187
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-218 |
3.46e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 97.10 E-value: 3.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqrAVTRNRLLGFVFQSFNLLPRlS 98
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD----HHYLHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSY---RGIRLASARQIAK--VQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDG 173
Cdd:TIGR00958 571 VRENIAYGLTDtpdEEIMAAAKAANAHdfIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1796960594 174 DTAQdiieLLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:TIGR00958 651 ECEQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-199 |
4.04e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 4.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLdGSEVAQADADQRAVTRNRL-LGFVFQ-SFNLLPRL 97
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEIKPVRKkVGVVFQfPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 SVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRA-KYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTA 176
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180
....*....|....*....|...
gi 1796960594 177 QDIIELLTTLNREQfMTLLMVTH 199
Cdd:PRK13643 181 IEMMQLFESIHQSG-QTVVLVTH 202
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
19-199 |
5.51e-23 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 96.55 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAdadQRAVTRNRLlGFVFQSFNLLpRLS 98
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEI---PREVLANSV-AMVDQDIFLF-EGT 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVAL---PLSYRGIRLAsAR--QIAKVQLEKVG-LEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:TIGR03796 569 VRDNLTLwdpTIPDADLVRA-CKdaAIHDVITSRPGgYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
170 180
....*....|....*....|....*..
gi 1796960594 173 GDTAQDIIELLttlnREQFMTLLMVTH 199
Cdd:TIGR03796 648 PETEKIIDDNL----RRRGCTCIIVAH 670
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-220 |
5.83e-23 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 96.18 E-value: 5.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGsevaqadADQRAVTRNRL---LGFVFQSFNLLPR 96
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDG-------TDIRTVTRASLrrnIAVVFQDAGLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 lSVLDNVAL---PLSYRGIRLASARQIAKVQLEK--VGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNL 171
Cdd:PRK13657 424 -SIEDNIRVgrpDATDEEMRAAAERAQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 172 DGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNG-----GVFD 220
Cdd:PRK13657 503 DVETEAKVKAALDELMKGR--TTFIIAHRLSTVRNADRILVFDNGrvvesGSFD 554
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
20-218 |
9.28e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 92.85 E-value: 9.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQadadQRAVTRNRLLGFVFQS-FNLLPRLS 98
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA----ENVWNLRRKIGMVFQNpDNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1796960594 179 IIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
19-218 |
9.57e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.84 E-value: 9.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAqaDADQRAVTRNRLlGFVFQS-FNLLPRL 97
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLWDIRNKA-GMVFQNpDNQIVAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 SVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQ 177
Cdd:PRK13633 102 IVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1796960594 178 DIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:PRK13633 182 EVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-216 |
1.07e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 93.25 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDqPCHGSLVLDGSEVAQADADQ------- 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIlGILA-PDSGEVLWDGEPLDPEDRRRigylpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 76 RAvtrnrllgfvfqsfnLLPRLSVLDNvalpLSY----RGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAI 151
Cdd:COG4152 80 RG---------------LYPKMKVGEQ----LVYlarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 152 ARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDpaMAQ----CmDRCLLVRNG 216
Cdd:COG4152 141 IAALLHDPELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQ--MELveelC-DRIVIINKG 205
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-216 |
1.47e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 91.98 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtr 80
Cdd:PRK11300 2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 nrLLGFV--FQSFNLLPRLSVLDNV-----------------ALPLSYRGIRLASARqiAKVQLEKVGLEPRAKYRPADL 141
Cdd:PRK11300 79 --RMGVVrtFQHVRLFREMTVIENLlvaqhqqlktglfsgllKTPAFRRAESEALDR--AATWLERVGLLEHANRQAGNL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 142 SGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDpaMAQCM---DRCLLVRNG 216
Cdd:PRK11300 155 AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD--MKLVMgisDRIYVVNQG 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-218 |
1.69e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 92.16 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 2 SSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrn 81
Cdd:PRK10575 9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 RLLGFVFQSFNLLPRLSVLDNVAL---PLSYRGIRLASA-RQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVT 157
Cdd:PRK10575 85 RKVAYLPQQLPAAEGMTVRELVAIgryPWHGALGRFGAAdREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 158 EPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQ--CmDRCLLVRNGGV 218
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAAryC-DYLVALRGGEM 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
10-216 |
3.76e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.31 E-value: 3.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 10 VTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHG-----SLVLDGSEVAQAdadQRAVTRNRLL 84
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNY---RDVLEFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPrLSVLDNV-ALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPAD----LSGGQRQRVAIARALVTEP 159
Cdd:PRK14271 104 GMLFQRPNPFP-MSIMDNVlAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 160 RILLADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDPAM-AQCMDRCLLVRNG 216
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQaARISDRAALFFDG 238
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-216 |
4.17e-22 |
|
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: 89.90 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAqadadqravtrnrLLGFvfqSFNLLPRLS 98
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSS-------------LLGL---GGGFNPELT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIrlaSARQIAKV--------QLEKVGLEPRAKYrpadlSGGQRQRVAIARALVTEPRILLADEPTGN 170
Cdd:cd03220 101 GRENIYLNGRLLGL---SRKEIDEKideiiefsELGDFIDLPVKTY-----SSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 171 LDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQ--CmDRCLLVRNG 216
Cdd:cd03220 173 GDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKrlC-DRALVLEKG 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-200 |
5.27e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.48 E-value: 5.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 17 EAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQpCHGSLVLDGS-EVAQADADQRAVTRNRL---LGFVFQSFN 92
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFFNQNIYERRVNLNRLrrqVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPrLSVLDNVALplsyrGIRLASAR------QIAKVQLEKVGLEPRAKYR----PADLSGGQRQRVAIARALVTEPRIL 162
Cdd:PRK14258 99 LFP-MSVYDNVAY-----GVKIVGWRpkleidDIVESALKDADLWDEIKHKihksALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 163 LADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-199 |
8.47e-22 |
|
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: 89.09 E-value: 8.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqRAVTRNRLLG-----FVFQ 89
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIipqdpVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 90 S---FNLLP--------RLSVLDNVALplsyrgirlasarqIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:cd03244 92 GtirSNLDPfgeysdeeLWQALERVGL--------------KEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLttlnREQF--MTLLMVTH 199
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTI----REAFkdCTVLTIAH 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-216 |
1.31e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 92.23 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 18 AVLQDVSFSLPTGQSCAIVGASGSGKS-TLLNLIGLLDQP-----CHGSL-------VLDGSEvaQADADQRAVtRNRLL 84
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAgglvqCDKMLlrrrsrqVIELSE--QSAAQMRHV-RGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQS--FNLLPRLSVLDNVALPLS-YRGIRLASARQIAKVQLEKVGLePRAKY----RPADLSGGQRQRVAIARALVT 157
Cdd:PRK10261 107 AMIFQEpmTSLNPVFTVGEQIAESIRlHQGASREEAMVEAKRMLDQVRI-PEAQTilsrYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 158 EPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPA-MAQCMDRCLLVRNG 216
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQG 245
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1-218 |
1.93e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadQRAVt 79
Cdd:PRK13647 1 MDNIIEVEDLHfRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEN--EKWV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 RNRLlGFVFQS-FNLLPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:PRK13647 78 RSKV-GLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNReQFMTLLMVTHDPAMA-QCMDRCLLVRNGGV 218
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAaEWADQVIVLKEGRV 216
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
23-203 |
2.45e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 89.80 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 23 VSFSLPTGQSCAIVGASGSGKS-TLLNLIGLLDQP---CHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQ----SFNll 94
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQdpmtSLN-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNV--ALPLSYRGIRlASARQIAKVQLEKVGL---EPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTG 169
Cdd:PRK11022 104 PCYTVGFQImeAIKVHQGGNK-KTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182
|
170 180 190
....*....|....*....|....*....|....
gi 1796960594 170 NLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAM 203
Cdd:PRK11022 183 ALDVTIQAQIIELLLELQQKENMALVLITHDLAL 216
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-217 |
2.47e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 91.41 E-value: 2.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWL-GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVL-DGSEVAqadadqravtrnr 82
Cdd:COG4178 363 LALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 llgFVFQ-SFnlLPRLSVLDNVALPLSYRGIrlaSARQIAKVqLEKVGLEPRAK--YRPAD----LSGGQRQRVAIARAL 155
Cdd:COG4178 430 ---FLPQrPY--LPLGTLREALLYPATAEAF---SDAELREA-LEAVGLGHLAErlDEEADwdqvLSLGEQQRLAFARLL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 156 VTEPRILLADEPTGNLDGDTAQDIIELLTTLNREqfMTLLMVTHDPAMAQCMDRCL-LVRNGG 217
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPG--TTVISVGHRSTLAAFHDRVLeLTGDGS 561
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-217 |
3.47e-21 |
|
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: 85.58 E-value: 3.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDgsevaqadadqravtrnrll 84
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 gfvfqsfnllprlsvldnvalplsyRGIRLASARQiakvqlekvgleprakyrpadLSGGQRQRVAIARALVTEPRILLA 164
Cdd:cd03221 61 -------------------------STVKIGYFEQ---------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 165 DEPTGNLDGDTAQDIIELLTTLNReqfmTLLMVTHDPA-MAQCMDRCLLVRNGG 217
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYfLDQVATKIIELEDGK 144
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
25-218 |
3.94e-21 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 87.60 E-value: 3.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 25 FSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAdadqravtrNRLLGFVFQ------SFNLLPRLS 98
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKG---------WRHIGYVPQrhefawDFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLS-YRGIRLASARQIAKVqLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQ 177
Cdd:TIGR03771 72 VMSGRTGHIGwLRRPCVADFAAVRDA-LRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 178 DIIELLTTLNREQfMTLLMVTHD--PAMAQCmDRCLLVrNGGV 218
Cdd:TIGR03771 151 LLTELFIELAGAG-TAILMTTHDlaQAMATC-DRVVLL-NGRV 190
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-216 |
4.26e-21 |
|
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: 90.93 E-value: 4.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAqadaDQRAVTRNRLLGFVFQSFNLLP 95
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA----DYTLASLRRQVALVSQDVVLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 96 RlSVLDNVAL--PLSYRGIRLASARQIAKVQlEKV-----GLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:TIGR02203 420 D-TIANNIAYgrTEQADRAEIERALAAAYAQ-DFVdklplGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 169 GNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEKADRIVVMDDG 543
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-216 |
7.35e-21 |
|
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: 85.56 E-value: 7.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRA------VTRNRllgfv 87
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIragiayVPEDR----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 88 fQSFNLLPRLSVLDNVALPLSyrgirlasarqiakvqlekvgleprakyrpadLSGGQRQRVAIARALVTEPRILLADEP 167
Cdd:cd03215 85 -KREGLVLDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1796960594 168 TGNLDGDTAQDIIELLTTLnREQFMTLLMVTHD-PAMAQCMDRCLLVRNG 216
Cdd:cd03215 132 TRGVDVGAKAEIYRLIREL-ADAGKAVLLISSElDELLGLCDRILVMYEG 180
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-200 |
2.64e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.48 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAdadqravT 79
Cdd:PRK15056 3 QQAGIVVNDVTvTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-------L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 RNRLLGFVFQSFNLLPRLSVLDNVALPLSYRG----IRLASA--RQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIAR 153
Cdd:PRK15056 76 QKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGhmgwLRRAKKrdRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1796960594 154 ALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHD 200
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
20-220 |
2.90e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.60 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQsfnlLPRLS 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGQTIVGDYAIPANLKKIKEVKRLRKEIGLVFQ----FPEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VL-DNVALPLSYRGIRLASARQIA--KV-QLEKVGLEPR--AKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PRK13645 103 LFqETIEKDIAFGPVNLGENKQEAykKVpELLKLVQLPEdyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 173 GDTAQDIIELLTTLNREQFMTLLMVTHDpaMAQCM---DRCLLVRNGGVFD 220
Cdd:PRK13645 183 PKGEEDFINLFERLNKEYKKRIIMVTHN--MDQVLriaDEVIVMHEGKVIS 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-216 |
3.01e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.15 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQ--RA----VTRNRllgfv 87
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaiRAgiayVPEDR----- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 88 fQSFNLLPRLSVLDNVALP----LSYRG-IRLASARQIAKVQLEKVGLEPRAKYRPA-DLSGGQRQRVAIARALVTEPRI 161
Cdd:COG1129 337 -KGEGLVLDLSIRENITLAsldrLSRGGlLDRRRERALAEEYIKRLRIKTPSPEQPVgNLSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDP----AMAqcmDRCLLVRNG 216
Cdd:COG1129 416 LILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVISSELpellGLS---DRILVMREG 470
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-218 |
3.32e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.52 E-value: 3.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVT--------------RWLGGEA--------VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCH 58
Cdd:COG1134 1 MSSMIEVENVSksyrlyhepsrslkELLLRRRrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 59 GSLVLDGSEVAqadadqravtrnrLLGF--VFQsfnllPRLSVLDNVALPLSYRGIrlaSARQIAKVqLEKV----GLEp 132
Cdd:COG1134 81 GRVEVNGRVSA-------------LLELgaGFH-----PELTGRENIYLNGRLLGL---SRKEIDEK-FDEIvefaELG- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 133 RAKYRPA-DLSGGQRQRVAIARALVTEPRILLADEPTGNldGDT-----AQDIIELLttlnREQFMTLLMVTHDPAMAQ- 205
Cdd:COG1134 138 DFIDQPVkTYSSGMRARLAFAVATAVDPDILLVDEVLAV--GDAafqkkCLARIREL----RESGRTVIFVSHSMGAVRr 211
|
250
....*....|....
gi 1796960594 206 -CmDRCLLVRNGGV 218
Cdd:COG1134 212 lC-DRAIWLEKGRL 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-200 |
3.68e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 85.99 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQsfnlLPRLSV 99
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 100 L-DNVALPLSYR----GIRLASARQIAKVQLEKVGLePR--AKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PRK13646 99 FeDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGF-SRdvMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180
....*....|....*....|....*...
gi 1796960594 173 GDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDENKTIILVSHD 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
19-216 |
5.26e-20 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 84.69 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLvldgsEVAQADADQRAVTRNRLLGFVF-QSFNLLPRL 97
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV-----RVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 SVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQ 177
Cdd:cd03267 111 PVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQE 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1796960594 178 DIIELLTTLNREQFMTLLMVTHD-PAMAQCMDRCLLVRNG 216
Cdd:cd03267 191 NIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVIDKG 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
19-200 |
1.12e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 85.34 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDQPCHGS---LVLDGSEVAQADADQRAVTRNRLLGFVFQ--SFN 92
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKDNWHVTadrFRWNGIDLLKLSPRERRKIIGREIAMIFQepSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPRLSVLDNV--ALPLS-YRGI---RLASARQIAKVQLEKVGLEPRAKYR---PADLSGGQRQRVAIARALVTEPRILL 163
Cdd:COG4170 102 LDPSAKIGDQLieAIPSWtFKGKwwqRFKWRKKRAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIAMAIANQPRLLI 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:COG4170 182 ADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHD 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-218 |
2.24e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.70 E-value: 2.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADAdqRAVtrNRLLGFVFQ-SFNL 93
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENI--REV--RKFVGLVFQnPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDG 173
Cdd:PRK13652 91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 174 DTAQDIIELLTTLNREQFMTLLMVTHD----PAMAQ---CMDRCLLVRNGGV 218
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQldlvPEMADyiyVMDKGRIVAYGTV 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-218 |
2.72e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAdadQRAVTR 80
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLLGFVFQSFNLLPRLSVLDNVALPlSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:PRK11614 79 REAVAIVPEGRRVFSRMTVEENLAMG-GFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMA-QCMDRCLLVRNGGV 218
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQAlKLADRGYVLENGHV 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-201 |
5.79e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.71 E-value: 5.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLI------GLLDQPchgSLVLDGSEVaqaDADQ-RAVTrnrllGFVFQSFN 92
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALafrspkGVKGSG---SVLLNGMPI---DAKEmRAIS-----AYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPRLSVLDNVALPLSYR-GIRLASARQIAKVQ--LEKVGLEPRAKYRPAD------LSGGQRQRVAIARALVTEPRILL 163
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRmPRRVTKKEKRERVDevLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDP 201
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGLAQKG-KTIICTIHQP 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
5-216 |
6.24e-19 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 80.98 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT-RWLGGEA----VLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSLVLDGSevaqadadqrav 78
Cdd:cd03250 1 ISVEDASfTWDSGEQetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 trnrlLGFVFQSFNLLPRlSVLDNVALPLSYRGIRLASArqIAKVQLEK------------VGlEprakyRPADLSGGQR 146
Cdd:cd03250 68 -----IAYVSQEPWIQNG-TIRENILFGKPFDEERYEKV--IKACALEPdleilpdgdlteIG-E-----KGINLSGGQK 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 147 QRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:cd03250 134 QRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-199 |
6.39e-19 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 84.38 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVT-RWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAdadQRAVT 79
Cdd:PRK10790 337 QSGRIDIDNVSfAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL---SHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 RNRLlGFVFQSFNLLPRlSVLDNVALPlsyrgiRLASARQIAKVqLEKVGLEPRAKYRPA-----------DLSGGQRQR 148
Cdd:PRK10790 414 RQGV-AMVQQDPVVLAD-TFLANVTLG------RDISEEQVWQA-LETVQLAELARSLPDglytplgeqgnNLSVGQKQL 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 149 VAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQfMTLLMVTH 199
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-REH-TTLVVIAH 533
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-216 |
7.05e-19 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 84.30 E-value: 7.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAqadaDQRAVTRNRLLGFVFQS---FNllpr 96
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR----DYTLASLRNQVALVSQNvhlFN---- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 lsvlDNVALPLSYrgirlASARQIAKVQLEKV---------------GLEPRAKYRPADLSGGQRQRVAIARALVTEPRI 161
Cdd:PRK11176 431 ----DTIANNIAY-----ARTEQYSREQIEEAarmayamdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPI 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEKADEILVVEDG 554
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-188 |
7.20e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.45 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqRAVTR 80
Cdd:PRK09700 2 ATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD---HKLAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 NRLLGFVFQSFNLLPRLSVLDNV---ALPL-SYRGIRL---ASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIAR 153
Cdd:PRK09700 79 QLGIGIIYQELSVIDELTVLENLyigRHLTkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158
|
170 180 190
....*....|....*....|....*....|....*
gi 1796960594 154 ALVTEPRILLADEPTGNLdgdTAQDIIELLTTLNR 188
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQ 190
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-201 |
7.69e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.87 E-value: 7.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQadadqRAVTRNRLL 84
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-----QRDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNvalpLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLA 164
Cdd:TIGR01189 76 LYLGHLPGLKPELSALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1796960594 165 DEPTGNLDGDTaqdiIELLTTLNREQFMT---LLMVTHDP 201
Cdd:TIGR01189 152 DEPTTALDKAG----VALLAGLLRAHLARggiVLLTTHQD 187
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-199 |
1.18e-18 |
|
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: 83.72 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDqPCHGSLVLDGsevaqadADQRAVTRNRL---LGFVFQS---F 91
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYD-VTSGRILIDG-------QDIRDVTQASLraaIGIVPQDtvlF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 92 NLlprlSVLDNVAlplsY-----------RGIRLAsarQIAK--VQLEKvGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:COG5265 445 ND----TIAYNIA----YgrpdaseeeveAAARAA---QIHDfiESLPD-GYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQfmTLLMVTH 199
Cdd:COG5265 513 PPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAH 551
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-221 |
1.44e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 82.97 E-value: 1.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADAdqRAVTRnrLL 84
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA--RAASR--RV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 GFVFQSFNLLPRLSVLDNVALPLSYRGIRLASA----RQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWtetdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQ--CmDRCLLVRNGGVFDA 221
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAAryC-DELVLLADGRVRAA 220
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-218 |
1.92e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.19 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTL-LNLIGLLdQPCHGSLVLDGseVAQADADQRAVTRnRLLGFVFQS--FN 92
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLL-RPQKGKVLVSG--IDTGDFSKLQGIR-KLVGIVFQNpeTQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPRlSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PRK13644 90 FVGR-TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796960594 173 GDTAQDIIELLTTLNrEQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:PRK13644 169 PDSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGKI 213
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-200 |
8.01e-18 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 79.00 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSevaqadadqravtr 80
Cdd:PRK09544 1 MTSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 81 nRLLGFVFQSFNLLPrlsvldnvALPLSY-RGIRLASARQIAKV--QLEKVGLEPRAKYRPADLSGGQRQRVAIARALVT 157
Cdd:PRK09544 67 -LRIGYVPQKLYLDT--------TLPLTVnRFLRLRPGTKKEDIlpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 158 EPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-219 |
2.22e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.31 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGlldqpchgslvldGSEVAQADADQravtrnrl 83
Cdd:COG2401 30 VLEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-------------GALKGTPVAGC-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 lgFVFQSFNLLPRLSVLDNVAlplsyrgiRLASARQIAKVqLEKVGLEPRAKYR--PADLSGGQRQRVAIARALVTEPRI 161
Cdd:COG2401 89 --VDVPDNQFGREASLIDAIG--------RKGDFKDAVEL-LNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCM--DRCLLVRNGGVF 219
Cdd:COG2401 158 LVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLqpDLLIFVGYGGVP 217
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
16-210 |
3.91e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.24 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrNRLLGFVFQSFNLLP 95
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA---RRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 96 RLSVLDNVALPLSYRGIRLASARQI-AKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:PRK10895 92 RLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1796960594 175 TAQDIIELLTTLnREQFMTLLMVTHDpaMAQCMDRC 210
Cdd:PRK10895 172 SVIDIKRIIEHL-RDSGLGVLITDHN--VRETLAVC 204
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-201 |
5.38e-17 |
|
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: 75.99 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGsevaQADADQRAVTRNRLLGFVFQSfNLL 94
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG----GPLDFQRDSIARGLLYLGHAP-GIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALplsYRGIRLASARQIAKVQLEKVGLEPRAKyrpADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:cd03231 86 TTLSVLENLRF---WHADHSDEQVEEALARVGLNGFEDRPV---AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....*..
gi 1796960594 175 TAQDIIELLTTlNREQFMTLLMVTHDP 201
Cdd:cd03231 160 GVARFAEAMAG-HCARGGMVVLTTHQD 185
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-221 |
2.08e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.30 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 3 SIISLHGVtrWLG-GEA-VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIG---LLDQpchGSLVLDGS-EVAQADADQ- 75
Cdd:PRK11147 2 SLISIHGA--WLSfSDApLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDD---GRIIYEQDlIVARLQQDPp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 76 RAVTrnrllGFVF---------------------------QSFNLLPRLSVLDNValpLSYRGIRLASARqIAKVqLEKV 128
Cdd:PRK11147 77 RNVE-----GTVYdfvaegieeqaeylkryhdishlvetdPSEKNLNELAKLQEQ---LDHHNLWQLENR-INEV-LAQL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 129 GLEPRAKYrpADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTaqdiIELLttlnrEQFM-----TLLMVTHDPAM 203
Cdd:PRK11147 147 GLDPDAAL--SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET----IEWL-----EGFLktfqgSIIFISHDRSF 215
|
250 260
....*....|....*....|....*
gi 1796960594 204 AQCM-------DRCLLVRNGGVFDA 221
Cdd:PRK11147 216 IRNMatrivdlDRGKLVSYPGNYDQ 240
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-199 |
2.11e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 77.47 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDqPCHGSLVLDGSEVaqaDADQRAvTRNRLlGFVFQSFNLLPRLSVL 100
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKmLTGLLP-ASEGEAWLFGQPV---DAGDIA-TRRRV-GYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 101 DNvaLPLSYRGIRLASARQIAKVQ--LEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDgDTAQD 178
Cdd:NF033858 358 QN--LELHARLFHLPAAEIAARVAemLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD-PVARD 434
|
170 180
....*....|....*....|..
gi 1796960594 179 II-ELLTTLNREQFMTLLMVTH 199
Cdd:NF033858 435 MFwRLLIELSREDGVTIFISTH 456
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-199 |
3.53e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.37 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLldQPcHGS----LVLDGSEVAQAD-ADQRA 77
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKvLSGV--YP-HGSyegeILFDGEVCRFKDiRDSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 78 vtrnrlLGFVF--QSFNLLPRLSVLDNVAL--PLSYRGI---RLASARqiAKVQLEKVGLEPRAKYRPADLSGGQRQRVA 150
Cdd:NF040905 78 ------LGIVIihQELALIPYLSIAENIFLgnERAKRGVidwNETNRR--ARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1796960594 151 IARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTH 199
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-171 |
3.92e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.24 E-value: 3.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQ---ADADQra 77
Cdd:PRK15439 8 APPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpAKAHQ-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 78 vtrnrlLG--FVFQSFNLLPRLSVLDNVALPLSYRgiRLASARQIAKVQLEKVGLEPRAKyrPADLSGGQRQRVAIARAL 155
Cdd:PRK15439 86 ------LGiyLVPQEPLLFPNLSVKENILFGLPKR--QASMQKMKQLLAALGCQLDLDSS--AGSLEVADRQIVEILRGL 155
|
170
....*....|....*.
gi 1796960594 156 VTEPRILLADEPTGNL 171
Cdd:PRK15439 156 MRDSRILILDEPTASL 171
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-199 |
1.06e-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: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLD-QPCHGSLVLDGSEVAQADADQRAvtrnRL-LGFVFQSf 91
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKyEVTEGEILFKGEDITDLPPEERA----RLgIFLAFQY- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 92 nllprlsvldnvalPLSYRGIRLASArqiakvqLEKVGleprakyrpADLSGGQRQRVAIARALVTEPRILLADEPTGNL 171
Cdd:cd03217 86 --------------PPEIPGVKNADF-------LRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180
....*....|....*....|....*...
gi 1796960594 172 DGDTAQDIIELLTTLnREQFMTLLMVTH 199
Cdd:cd03217 136 DIDALRLVAEVINKL-REEGKSVLIITH 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
15-199 |
1.69e-15 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 72.79 E-value: 1.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLD-QPCHGSLVLDGSEVAQADADQRAvtrnRL-LGFVFQS- 90
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmGHPKyEVTSGSILLDGEDILELSPDERA----RAgIFLAFQYp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 91 --------FNLLpRLSvLDNVALPLsyrgIRLASARQIAKVQLEKVGLEPRAKYRPAD--LSGGQRQRVAIARALVTEPR 160
Cdd:COG0396 87 veipgvsvSNFL-RTA-LNARRGEE----LSAREFLKLLKEKMKELGLDEDFLDRYVNegFSGGEKKRNEILQMLLLEPK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTH 199
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPD-RGILIITH 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
20-217 |
2.42e-15 |
|
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: 71.12 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLI------GLLDqpchGSLVLDGSevaqadadQRAVTRNRLLGFVFQSFNL 93
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktaGVIT----GEILINGR--------PLDKNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRLSVldNVALPLSyrgirlasarqiakvqlekvgleprAKYRpaDLSGGQRQRVAIARALVTEPRILLADEPTGNLDG 173
Cdd:cd03232 91 SPNLTV--REALRFS-------------------------ALLR--GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796960594 174 DTAQDIIELLTTLNREQfMTLLMVTHDPAMA--QCMDRCLLVRNGG 217
Cdd:cd03232 142 QAAYNIVRFLKKLADSG-QAILCTIHQPSASifEKFDRLLLLKRGG 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-188 |
2.96e-15 |
|
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: 73.71 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLdQPC---HGSLVLDGSE-VAQADADqravT 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHgtwDGEIYWSGSPlKASNIRD----T 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 RNRLLGFVFQSFNLLPRLSVLDNVAL--PLSYRGIRLASARQIAKVQ--LEKVGLEPRAKYRP-ADLSGGQRQRVAIARA 154
Cdd:TIGR02633 76 ERAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAMYLRAKnlLRELQLDADNVTRPvGDYGGGQQQLVEIAKA 155
|
170 180 190
....*....|....*....|....*....|....
gi 1796960594 155 LVTEPRILLADEPTGNLDGDTAQDIIELLTTLNR 188
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKA 189
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-218 |
6.45e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 6.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQPCH-------GSLVLDGSEVAQADADQRAVTRNRLL--- 84
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPqaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 --GFVFqsfnllprlSVLDNVAL---PLSYRGIRLASA-RQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARAL--- 155
Cdd:PRK13547 93 qpAFAF---------SAREIVLLgryPHARRAGALTHRdGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 156 ------VTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAM-AQCMDRCLLVRNGGV 218
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLaARHADRIAMLADGAI 233
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-175 |
7.60e-15 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 72.66 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLdGSEVAQADADQravTRNrl 83
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQ---SRD-- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 lgfvfqsfNLLPRLSVLDNVALPLSYrgIRLASaRQI---AKV---------QLEKVGleprakyrpaDLSGGQRQRVAI 151
Cdd:TIGR03719 396 --------ALDPNKTVWEEISGGLDI--IKLGK-REIpsrAYVgrfnfkgsdQQKKVG----------QLSGGERNRVHL 454
|
170 180
....*....|....*....|....
gi 1796960594 152 ARALVTEPRILLADEPTGNLDGDT 175
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-216 |
9.98e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 71.66 E-value: 9.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 17 EAVlQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSLvldgsEVAQADADQRavtRNRLL---GFVF-QSF 91
Cdd:COG4586 36 EAV-DDISFTIEPGEIVGFIGPNGAGKSTTIKmLTGIL-VPTSGEV-----RVLGYVPFKR---RKEFArriGVVFgQRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 92 NLLPRLSVLDnvalplSYRGIRlasarQIAKVqlekvglePRAKYR------------------PA-DLSGGQRQRVAIA 152
Cdd:COG4586 106 QLWWDLPAID------SFRLLK-----AIYRI--------PDAEYKkrldelvelldlgelldtPVrQLSLGQRMRCELA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDpaMA---QCMDRCLLVRNG 216
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD--MDdieALCDRVIVIDHG 231
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-199 |
1.09e-14 |
|
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: 69.75 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqravtrnrlLGFVFQSFNLLPRLS 98
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-----------LEDLRSSLTIIPQDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQLEKVGLEprakyrpaDLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQD 178
Cdd:cd03369 92 TLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGL--------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180
....*....|....*....|...
gi 1796960594 179 IIELLttlnREQF--MTLLMVTH 199
Cdd:cd03369 164 IQKTI----REEFtnSTILTIAH 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
16-217 |
1.23e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.72 E-value: 1.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLdQPCH-GSLVLDgsevaqadadqravTRNRLLgFVFQSfNLL 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGL-WPWGsGRIGMP--------------EGEDLL-FLPQR-PYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPLSyrgirlasarqiakvqleKVgleprakyrpadLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:cd03223 76 PLGTLREQLIYPWD------------------DV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 175 TAQDIIELLttlnREQFMTLLMVTHDPAMAQCMDRCL-LVRNGG 217
Cdd:cd03223 126 SEDRLYQLL----KELGITVISVGHRPSLWKFHDRVLdLDGEGG 165
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-216 |
1.87e-14 |
|
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: 71.87 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSevaqadadqravtrnrlLGFVFQSFNL 93
Cdd:TIGR01271 436 LYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-----------------ISFSPQTSWI 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRlSVLDNVALPLSYRGIRLASArqIAKVQLEK-VGLEPRAKYRP-----ADLSGGQRQRVAIARALVTEPRILLADEP 167
Cdd:TIGR01271 499 MPG-TIKDNIIFGLSYDEYRYTSV--IKACQLEEdIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 168 TGNLDGDTAQDIIE-----LLTTLNReqfmtlLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:TIGR01271 576 FTHLDVVTEKEIFEsclckLMSNKTR------ILVTSKLEHLKKADKILLLHEG 623
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-194 |
2.38e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSL-VLDGSevaQADADQRAVTRNR 82
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVeVLGGD---MADARHRRAVCPR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 L------LGfvfqsFNLLPRLSVLDNVA-------LPLSYRgirlasARQIAKVqLEKVGLEPRAKyRPA-DLSGGQRQR 148
Cdd:NF033858 78 IaympqgLG-----KNLYPTLSVFENLDffgrlfgQDAAER------RRRIDEL-LRATGLAPFAD-RPAgKLSGGMKQK 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796960594 149 VAIARALVTEPRILLADEPTGNLDgdtaqdiielltTLNREQFMTL 194
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVD------------PLSRRQFWEL 178
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
15-172 |
2.77e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRavtrnRLLGFVF-----Q 89
Cdd:COG3845 269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER-----RRLGVAYipedrL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 90 SFNLLPRLSVLDNVAL------PLSYRG-IRLASARQIAKVQLEKVGLEPRAKYRPAD-LSGGQRQRVAIARALVTEPRI 161
Cdd:COG3845 344 GRGLVPDMSVAENLILgryrrpPFSRGGfLDRKAIRAFAEELIEEFDVRTPGPDTPARsLSGGNQQKVILARELSRDPKL 423
|
170
....*....|.
gi 1796960594 162 LLADEPTGNLD 172
Cdd:COG3845 424 LIAAQPTRGLD 434
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-200 |
3.21e-14 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 70.73 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWL-GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPchgslvLDGSEVAQADADqravtrnr 82
Cdd:TIGR03719 4 IYTMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARPQPGIK-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 lLGFVFQSFNLLPRLSVLDNVALPLS--------YRGIRLASA----------RQIAKVQ--LEKVG-------LE---- 131
Cdd:TIGR03719 70 -VGYLPQEPQLDPTKTVRENVEEGVAeikdaldrFNEISAKYAepdadfdklaAEQAELQeiIDAADawdldsqLEiamd 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 132 ----PRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTaqdiIELLttlnrEQFM-----TLLMVTHD 200
Cdd:TIGR03719 149 alrcPPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWL-----ERHLqeypgTVVAVTHD 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
14-221 |
1.11e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVlQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDQPcHGSLVLDGSEVaQADADQRAVTRnrllGFVFQSFN 92
Cdd:PRK10762 263 LSGPGV-NDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPRT-SGYVTLDGHEV-VTRSPQDGLAN----GIVYISED 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 -----LLPRLSVLDNVALP----LSYRGIRLASARQIAKV----QLEKVGlEPRAKYRPADLSGGQRQRVAIARALVTEP 159
Cdd:PRK10762 336 rkrdgLVLGMSVKENMSLTalryFSRAGGSLKHADEQQAVsdfiRLFNIK-TPSMEQAIGLLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 160 RILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDpaMAQCM---DRCLLVRNG---GVFDA 221
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAEG-LSIILVSSE--MPEVLgmsDRILVMHEGrisGEFTR 479
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
19-218 |
1.29e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.97 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQravTRNRLlGFVFQSfnllPRL- 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS---WRSRL-AVVSQT----PFLf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 98 --SVLDNVALplsyrGIRLASARQIAKV-QLEKV---------GLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLAD 165
Cdd:PRK10789 402 sdTVANNIAL-----GRPDATQQEIEHVaRLASVhddilrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 166 EPTGNLDGDTAQDIIELLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTEASEILVMQHGHI 527
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-183 |
1.33e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLdqPcHGS----LVLDGSEV-AQADAD 74
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKvLSGVY--P-HGTyegeIIFEGEELqASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 75 qravTRNRLLGFVFQSFNLLPRLSVLDNVAL---PLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAI 151
Cdd:PRK13549 79 ----TERAGIAIIHQELALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190
....*....|....*....|....*....|..
gi 1796960594 152 ARALVTEPRILLADEPTGNLdgdTAQDIIELL 183
Cdd:PRK13549 155 AKALNKQARLLILDEPTASL---TESETAVLL 183
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-199 |
1.76e-13 |
|
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: 66.97 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 9 GVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSlVLDGSEVAQADADQRAVTRNRL-LGFV 87
Cdd:cd03290 6 GYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGK-VHWSNKNESEPSFEATRSRNRYsVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 88 FQSFNLLpRLSVLDNVAL--PLS---YRGIRLASARQiAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:cd03290 85 AQKPWLL-NATVEENITFgsPFNkqrYKAVTDACSLQ-PDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 1796960594 163 LADEPTGNLDGDTAQDII-ELLTTLNREQFMTLLMVTH 199
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTH 200
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
19-216 |
2.13e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQPCHGSLVLdgsevaqadADQRAVTRN--RLLGFVFQSFNLLP 95
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQGNNFTGTIL---------ANNRKPTKQilKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 96 RLSVLDNVA------LP--LSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEP 167
Cdd:PLN03211 154 HLTVRETLVfcsllrLPksLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 168 TGNLDGDTAQDIIELLTTLNREQfMTLLMVTHDPA--MAQCMDRCLLVRNG 216
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKG-KTIVTSMHQPSsrVYQMFDSVLVLSEG 283
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-177 |
2.21e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.49 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAD--ADQRAV 78
Cdd:PRK10762 1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGpkSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 trnrlLGFVFQSFNLLPRLSVLDNVALPLSYR----GIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARA 154
Cdd:PRK10762 81 -----IGIIHQELNLIPQLTIAENIFLGREFVnrfgRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180
....*....|....*....|....
gi 1796960594 155 LVTEPRILLADEPTGNL-DGDTAQ 177
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETES 179
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
23-209 |
2.29e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 67.91 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 23 VSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDQpchgSLVLDGSEVAQADADQRAVT---RNRLLG----FVFQSfnll 94
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAIcGVTKD----NWRVTADRMRFDDIDLLRLSpreRRKLVGhnvsMIFQE---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRlSVLD---NVALPL-------SYRG---IRLASARQIAKVQLEKVGL-EPRAKYR--PADLSGGQRQRVAIARALVTE 158
Cdd:PRK15093 98 PQ-SCLDpseRVGRQLmqnipgwTYKGrwwQRFGWRKRRAIELLHRVGIkDHKDAMRsfPYELTEGECQKVMIAIALANQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 159 PRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHD-PAMAQCMDR 209
Cdd:PRK15093 177 PRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADK 228
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-219 |
2.32e-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: 68.50 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEV-AQADADQRAvtrnrlLGFVFQSFNLL 94
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVRQS------LGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:TIGR01257 1016 HHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796960594 175 TAQDIIELLttLNREQFMTLLMVTHDPAMAQCM-DRCLLVRNGGVF 219
Cdd:TIGR01257 1096 SRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLgDRIAIISQGRLY 1139
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-216 |
3.13e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.89 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 21 QDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEV---AQADADQRA---VTRNRL-LGFvfqsfnl 93
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVKKGmayITESRRdNGF------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRLSVLDNVALPLSYRGIRLASA---------RQIAKVQLEKVGLEPRA-KYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKDGGYKGAmglfhevdeQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNrEQFMTLLMVTHD-PAMAQCMDRCLLVRNG 216
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLA-DDGKVILMVSSElPEIITVCDRIAVFCEG 485
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-199 |
3.62e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 3.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqravtRNRL 83
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSFNLLPRLSVLDNVALPLSYRGIRlasARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:PRK13543 84 MAYLGHLPGLKADLSTLENLHFLCGLHGRR---AKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQFMTLLmVTH 199
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISAHLRGGGAALV-TTH 195
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
14-219 |
7.15e-13 |
|
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: 66.03 E-value: 7.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSevaqadadqravtrnrlLGFVFQSFNL 93
Cdd:cd03291 47 LVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-----------------ISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 94 LPRlSVLDNVALPLSYRGIRLASArqIAKVQLEkvglEPRAKYRPAD----------LSGGQRQRVAIARALVTEPRILL 163
Cdd:cd03291 110 MPG-TIKENIIFGVSYDEYRYKSV--VKACQLE----EDITKFPEKDntvlgeggitLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 164 ADEPTGNLDGDTAQDIIE-LLTTLNREQfmTLLMVTHDPAMAQCMDRCLLVRNGGVF 219
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEsCVCKLMANK--TRILVTSKMEHLKKADKILILHEGSSY 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-179 |
1.09e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 66.47 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQpcHGSLVLDGsevaqadadqraVTRNRL-LGFVFQSFN 92
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSaLLRLLST--EGEIQIDG------------VSWNSVtLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPRLSVLDNVALPLSYRGIRLASARQIAKVQlEKVGLEPRAKYRPAD-----------LSGGQRQRVAIARALVTEPRI 161
Cdd:TIGR01271 1296 VIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVA-EEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKI 1374
|
170
....*....|....*...
gi 1796960594 162 LLADEPTGNLDGDTAQDI 179
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQII 1392
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-172 |
2.23e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 17 EAVLQDVSFSLPTGQSCAIVGASGSGKSTL-LNLIGLLdQPCHGSLVLDGSEVaqaDADQRAVTRNRL-LGFVFQSFNLL 94
Cdd:PRK13638 14 EPVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKPL---DYSKRGLLALRQqVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNvALPLSYRGIRLASArQIAKVQLEKVGLEPRAKYR--PAD-LSGGQRQRVAIARALVTEPRILLADEPTGNL 171
Cdd:PRK13638 90 IFYTDIDS-DIAFSLRNLGVPEA-EITRRVDEALTLVDAQHFRhqPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
.
gi 1796960594 172 D 172
Cdd:PRK13638 168 D 168
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
17-199 |
2.53e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 17 EAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVaqadaDQRAVTRNRLLGFVFQSFNLLPR 96
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-----KKDLCTYQKQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 LSVLDNVALPLSYRGIRLASARQIAKVQLEKVgleprAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTA 176
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAVGITELCRLFSLEHL-----IDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|...
gi 1796960594 177 QDIIELLTTlNREQFMTLLMVTH 199
Cdd:PRK13540 164 LTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-218 |
3.39e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.75 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRA------VTRNR----LLGFVFQ 89
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfalVTEERrstgIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 90 SFNllprlSVLDNVAlplSYRG-IRLASARQIAK-----VQLEKVGlEPRAKYRPADLSGGQRQRVAIARALVTEPRILL 163
Cdd:PRK10982 344 GFN-----SLISNIR---NYKNkVGLLDNSRMKSdtqwvIDSMRVK-TPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILM 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1796960594 164 ADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:PRK10982 415 LDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-216 |
4.84e-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: 64.46 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQPCHGSLVLDGSEVAQADADQRAVTRNRLLGFVFQSFNLLPRLSVL 100
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 101 DNVALPL--SYRG---IRLASARQIAKVQLEKVGLEPRAKYRP-ADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:TIGR02633 358 KNITLSVlkSFCFkmrIDAAAELQIIGSAIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVG 437
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1796960594 175 TAQDIIELLTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:TIGR02633 438 AKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEG 479
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
23-216 |
4.85e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 4.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 23 VSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVaqaDADQRAVTRnRLLGFVFQSFNLLPRLSVLDN 102
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR-KLFSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 103 VALPLSYRGIRLASARQIAKVQLEKvgleprAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIEL 182
Cdd:PRK10522 418 KPANPALVEKWLERLKMAHKLELED------GRISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQV 491
|
170 180 190
....*....|....*....|....*....|....
gi 1796960594 183 LTTLNREQFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:PRK10522 492 LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-200 |
4.90e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 4.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGE-AVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVL-DGSEVA------QADADQ 75
Cdd:PRK11819 6 IYTMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIKVGylpqepQLDPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 76 rAVTRNRLLGfVFQSFNLLPRL-SVLDNVALPLSYRGiRLAsARQiAKVQlEKVG----------LE--------Praky 136
Cdd:PRK11819 86 -TVRENVEEG-VAEVKAALDRFnEIYAAYAEPDADFD-ALA-AEQ-GELQ-EIIDaadawdldsqLEiamdalrcP---- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 137 rPAD-----LSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTaqdiIELLttlnrEQFM-----TLLMVTHD 200
Cdd:PRK11819 156 -PWDakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES----VAWL-----EQFLhdypgTVVAVTHD 219
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-181 |
5.13e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 64.58 E-value: 5.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT-RWLGGEA-VLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQpCHGSLVLDGSevaQADADQRAVTRN 81
Cdd:TIGR00957 637 ITVHNATfTWARDLPpTLNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS---VAYVPQQAWIQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 RLLgfvfqsfnllpRLSVLDNVAL-PLSYRGIRLASARqIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR 160
Cdd:TIGR00957 713 DSL-----------RENILFGKALnEKYYQQVLEACAL-LPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180
....*....|....*....|.
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIE 181
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFE 801
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-183 |
5.46e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.51 E-value: 5.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVL-QDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADQRAvtrnrllgfvfqsfNLL 94
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQ--------------DLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 ---------PRLSVLDNvaLPLSYRGIRLASARQIAKVqLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLAD 165
Cdd:PRK13538 78 ylghqpgikTELTALEN--LRFYQRLHGPGDDEALWEA-LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILD 154
|
170
....*....|....*...
gi 1796960594 166 EPTGNLDGDTAQDIIELL 183
Cdd:PRK13538 155 EPFTAIDKQGVARLEALL 172
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
5-218 |
5.68e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.05 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVT----RWLGGEA-VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVaqaDADQRAVT 79
Cdd:COG4615 328 LELRGVTyrypGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 RNRllgF--VFQSFNLLPRLSVLDNVALPlsyrgirlASARQ-IAKVQLE-KVGLEpRAKYRPADLSGGQRQRVAIARAL 155
Cdd:COG4615 405 RQL---FsaVFSDFHLFDRLLGLDGEADP--------ARARElLERLELDhKVSVE-DGRFSTTDLSQGQRKRLALLVAL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1796960594 156 VtEPR-ILLADEptgnldgdTA--QDII-------ELLTTLnREQFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:COG4615 473 L-EDRpILVFDE--------WAadQDPEfrrvfytELLPEL-KARGKTVIAISHDDRYFDLADRVLKMDYGKL 535
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-175 |
8.30e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.60 E-value: 8.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLdGSEVAqadadqravtrnrl 83
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK-------------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSF-NLLPRLSVLDNVALPLSYrgIRLASaRQI---AKV---------QLEKVGleprakyrpaDLSGGQRQRVA 150
Cdd:PRK11819 389 LAYVDQSRdALDPNKTVWEEISGGLDI--IKVGN-REIpsrAYVgrfnfkggdQQKKVG----------VLSGGERNRLH 455
|
170 180
....*....|....*....|....*
gi 1796960594 151 IARALVTEPRILLADEPTGNLDGDT 175
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
15-200 |
1.33e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 63.34 E-value: 1.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSlVLDGSEVAQADADQRAVTRnrllgfvfqsfnll 94
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGT-VFRSAKVRMAVFSQHHVDG-------------- 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 prlsvLDNVALPLSYRGIRLASA-RQIAKVQLEKVGLEPRAKYRPA-DLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PLN03073 585 -----LDLSSNPLLYMMRCFPGVpEQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
170 180
....*....|....*....|....*...
gi 1796960594 173 GDTAQDIIELLTTLNReqfmTLLMVTHD 200
Cdd:PLN03073 660 LDAVEALIQGLVLFQG----GVLMVSHD 683
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-215 |
1.55e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.12 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI--------------------------------------------GLLD 54
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefSLTK 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 55 QPCH----------GSLVLDGSEVAqaDADQRAVtRNrLLGFVFQSfNLLPRLSVLDNV-------ALPLSYRGIRLASA 117
Cdd:PTZ00265 1263 EGGSgedstvfknsGKILLDGVDIC--DYNLKDL-RN-LFSIVSQE-PMLFNMSIYENIkfgkedaTREDVKRACKFAAI 1337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 118 RQIAKVQLEK--VGLEPRAKyrpaDLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLL 195
Cdd:PTZ00265 1338 DEFIESLPNKydTNVGPYGK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
|
250 260
....*....|....*....|
gi 1796960594 196 MVTHDPAMAQCMDRCLLVRN 215
Cdd:PTZ00265 1414 TIAHRIASIKRSDKIVVFNN 1433
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-200 |
2.05e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.39 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLdqPCHGSLVLDGSEVAQADADQRAVTRnrllGFVFQSFNLLPRLS 98
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVqLEKVGLEPraKY-RPAD-LSGGQRQRVAIARALVT-------EPRILLADEPTG 169
Cdd:COG4138 86 VFQYLALHQPAGASSEAVEQLLAQL-AEALGLED--KLsRPLTqLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMN 162
|
170 180 190
....*....|....*....|....*....|...
gi 1796960594 170 NLdgDTAQDIIeLLTTLNR--EQFMTLLMVTHD 200
Cdd:COG4138 163 SL--DVAQQAA-LDRLLRElcQQGITVVMSSHD 192
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-207 |
2.26e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 5 ISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDQPCHGSLVLDGSevaqadadQRAVTRN-- 81
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItGDHPQGYSNDLTLFGR--------RRGSGETiw 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 ---RLLGFVFQSFNLLPRLSV-LDNVALPLSYRGIRLASA-----RQIAKVQLEKVGLEPRAKYRP-ADLSGGQRQRVAI 151
Cdd:PRK10938 333 dikKHIGYVSSSLHLDYRVSTsVRNVILSGFFDSIGIYQAvsdrqQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1796960594 152 ARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMA-QCM 207
Cdd:PRK10938 413 VRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDApACI 469
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-218 |
4.36e-11 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 61.02 E-value: 4.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDqpCHGSLVLDGsevaqadadqraVTRNRL-LGFVFQSFN 92
Cdd:cd03289 15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDG------------VSWNSVpLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 93 LLPRLSVLDNVALPLSYRGIRLASARQIAKVQlEKVGLEPRAKYRPAD-----------LSGGQRQRVAIARALVTEPRI 161
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVA-EEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLttlnREQFM--TLLMVTHD-PAMAQCmDRCLLVRNGGV 218
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTL----KQAFAdcTVILSEHRiEAMLEC-QRFLVIEENKV 214
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-199 |
4.56e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSE------------------------------- 67
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrskigvvsqdpllfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 68 -----------------------VAQADADQRAVTRNRLLGfvfqSFNLLPRLSVLDN-VALPLSYRGIRLASARQIAKV 123
Cdd:PTZ00265 480 ikyslyslkdlealsnyynedgnDSQENKNKRNSCRAKCAG----DLNDMSNTTDSNElIEMRKNYQTIKDSEVVDVSKK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 124 QL--EKVGLEPRaKY------RPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLL 195
Cdd:PTZ00265 556 VLihDFVSALPD-KYetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
....
gi 1796960594 196 MVTH 199
Cdd:PTZ00265 635 IIAH 638
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-217 |
5.15e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 61.66 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 30 GQSCAIVGASGSGKSTLLNLiglLDQPCHGSLVLDGSEVAQADAdqRAVTRNRLLGFVFQSFNLLPRLSVLDnvALPLSy 109
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRP--LDSSFQRSIGYVQQQDLHLPTSTVRE--SLRFS- 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 110 rgirlASARQIAKVQL-EK----------VGLEpraKYRPA-------DLSGGQRQRVAIARALVTEPRILL-ADEPTGN 170
Cdd:TIGR00956 861 -----AYLRQPKSVSKsEKmeyveeviklLEME---SYADAvvgvpgeGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 171 LDGDTAQDIIELLTTL-NREQfmTLLMVTHDPA---MAQcMDRCLLVRNGG 217
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLaDHGQ--AILCTIHQPSailFEE-FDRLLLLQKGG 980
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-181 |
5.61e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLnliglldqpchgslvldGSEVAQADADQRAVTRNRLLGFVFQSFNLLpRLS 98
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLL-----------------QSLLSQFEISEGRVWAERSIAYVPQQAWIM-NAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQI----AKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:PTZ00243 737 VRGNILFFDEEDAARLADAVRVsqleADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
....*..
gi 1796960594 175 TAQDIIE 181
Cdd:PTZ00243 817 VGERVVE 823
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
20-196 |
6.43e-11 |
|
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: 59.58 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPC---HGSLVLDGsevaqADADQRAVTRNRLLGFVFQSFNLLPR 96
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNG-----IPYKEFAEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 97 LSVLDNVALPLSYRGirlasaRQIAKVqlekvgleprakyrpadLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTA 176
Cdd:cd03233 98 LTVRETLDFALRCKG------NEFVRG-----------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180
....*....|....*....|
gi 1796960594 177 QDIIELLTTLNREQFMTLLM 196
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFV 174
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
19-220 |
7.86e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 7.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQ-ADADQRavtrnRLLGFVFQS------- 90
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLR-----RVLSIIPQSpvlfsgt 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 91 --FNLLPrLSVLDNVALplsYRGIRLASARQIakVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:PLN03232 1326 vrFNIDP-FSEHNDADL---WEALERAHIKDV--IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 169 GNLDGDTAQdiieLLTTLNREQFM--TLLMVTHDPAMAQCMDRCLLVRNGGVFD 220
Cdd:PLN03232 1400 ASVDVRTDS----LIQRTIREEFKscTMLVIAHRLNTIIDCDKILVLSSGQVLE 1449
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-200 |
8.75e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNL-IGLLdQPCHGSlVLDGSEVAQADADQ-RAvtrnrllgfvfqsf 91
Cdd:PRK11147 329 IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGR-IHCGTKLEVAYFDQhRA-------------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 92 NLLPRLSVLDNVA-------------LPLSYrgirlasarqiakvqLEKVGLEP-RAKYRPADLSGGQRQRVAIARALVT 157
Cdd:PRK11147 393 ELDPEKTVMDNLAegkqevmvngrprHVLGY---------------LQDFLFHPkRAMTPVKALSGGERNRLLLARLFLK 457
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1796960594 158 EPRILLADEPTGNLDGDTaqdiIELLTTLNREQFMTLLMVTHD 200
Cdd:PRK11147 458 PSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-209 |
1.25e-10 |
|
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: 58.10 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGlldqpchgslvldgsevaqadadqRAVTRNRLLGFvfqsfnllprlsv 99
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL------------------------YASGKARLISF------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 100 ldnvaLPLSYRG--IRLASARQIAKVQLEKVGLEprakyRPAD-LSGGQRQRVAIARALV--TEPRILLADEPTGNLDGD 174
Cdd:cd03238 54 -----LPKFSRNklIFIDQLQFLIDVGLGYLTLG-----QKLStLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQ 123
|
170 180 190
....*....|....*....|....*....|....*
gi 1796960594 175 TAQDIIELLTTLnREQFMTLLMVTHDPAMAQCMDR 209
Cdd:cd03238 124 DINQLLEVIKGL-IDLGNTVILIEHNLDVLSSADW 157
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
20-216 |
1.78e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQPCHGSLVLDGSeVAQADAdqravtrnrlLGFVFQSfnllprlS 98
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-VAYVPQ----------VSWIFNA-------T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPLSYRGIRLASARQIAKVQ----------LEKVGleprakYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:PLN03232 695 VRENILFGSDFESERYWRAIDVTALQhdldllpgrdLTEIG------ERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1796960594 169 GNLDGDTAQDIIEllTTLNRE-QFMTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:PLN03232 769 SALDAHVAHQVFD--SCMKDElKGKTRVLVTNQLHFLPLMDRIILVSEG 815
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-197 |
1.83e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 22 DVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQPCHGSLVLDGSEV-----AQADADQRA-VTRNRllgfvfQSFNLL 94
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVkirnpQQAIAQGIAmVPEDR------KRDGIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSVLDNVALPL---SYRGIRLASARQIAKVQLEKVGLE---PRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:PRK13549 354 PVMGVGKNITLAAldrFTGGSRIDDAAELKTILESIQRLKvktASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180
....*....|....*....|....*....
gi 1796960594 169 GNLDGDTAQDIIELLTTLNREQfMTLLMV 197
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLVQQG-VAIIVI 461
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-218 |
2.90e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLN-LIGLLDQPCHGSLVLDGS--EVAQADADQRAVTR-NRLLGFVFQSfnllp 95
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTvaYVPQVSWIFNATVRdNILFGSPFDP----- 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 96 rlsvldnvalPLSYRGIRLASARQiaKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDT 175
Cdd:PLN03130 708 ----------ERYERAIDVTALQH--DLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1796960594 176 AQDIIEllTTLNRE-QFMTLLMVTHDPAMAQCMDRCLLVRNGGV 218
Cdd:PLN03130 776 GRQVFD--KCIKDElRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
19-199 |
1.31e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqravtrnrLLGFVFQsFNLLPRLS 98
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG----------LHDLRFK-ITIIPQDP 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VLDNVALPL------SYRGIRLASARQIAK----VQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:TIGR00957 1370 VLFSGSLRMnldpfsQYSDEEVWWALELAHlktfVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
170 180 190
....*....|....*....|....*....|...
gi 1796960594 169 GNLDGDTAqdiiELLTTLNREQF--MTLLMVTH 199
Cdd:TIGR00957 1450 AAVDLETD----NLIQSTIRTQFedCTVLTIAH 1478
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-199 |
6.38e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGllDQPCH----GSLVLDGSEVAQADADQRA----------------V 78
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPAYkileGDILFKGESILDLEPEERAhlgiflafqypieipgV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 TRNRLLGFVF---QSFNLLPRLSvldnvalPLSYrgirlasaRQIAKVQLEKVGLEPRAKYRPAD--LSGGQRQRVAIAR 153
Cdd:CHL00131 100 SNADFLRLAYnskRKFQGLPELD-------PLEF--------LEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1796960594 154 ALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTH 199
Cdd:CHL00131 165 MALLDSELAILDETDSGLDIDALKIIAEGINKLMTSE-NSIILITH 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-206 |
8.65e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 8.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 18 AVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGlldQPCHGSLVLDGSEVAQADADQRAVtRNRLLGFVF---QSFNLL 94
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIA---SNTDGFHIGVEGVITYDGITPEEI-KKHYRGDVVynaETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 95 PRLSV---LDNVAL----PLSYRGI-RLASARQIAKVQLEKVGLEPRAKYRPAD-----LSGGQRQRVAIARALVTEPRI 161
Cdd:TIGR00956 151 PHLTVgetLDFAARcktpQNRPDGVsREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1796960594 162 LLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMvthdpAMAQC 206
Cdd:TIGR00956 231 QCWDNATRGLDSATALEFIRALKTSANILDTTPLV-----AIYQC 270
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-216 |
1.31e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 1 MSSIISLHGVTRwLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTL-LNLIGLLdQPCHGSLVLDGSEVAQ--------- 70
Cdd:PRK10938 1 MSSLQISQGTFR-LSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALaRALAGEL-PLLSGERQSQFSHITRlsfeqlqkl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 71 -ADADQRavTRNRLLGFVFQSFNLLPRLSVLDNVALPlsYRGIRLASARQIAKVqlekvgLEPRAKYrpadLSGGQRQRV 149
Cdd:PRK10938 79 vSDEWQR--NNTDMLSPGEDDTGRTTAEIIQDEVKDP--ARCEQLAQQFGITAL------LDRRFKY----LSTGETRKT 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 150 AIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVT---HD-PAMAQ---CMDRCLLVRNG 216
Cdd:PRK10938 145 LLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG-ITLVLVLnrfDEiPDFVQfagVLADCTLAETG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
19-199 |
1.37e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQAD-ADQRAVtrnrlLGFVFQS------- 90
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGlMDLRKV-----LGIIPQApvlfsgt 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 91 --FNLLPrLSVLDNVALPLSYRGIRLASArqiakVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:PLN03130 1329 vrFNLDP-FNEHNDADLWESLERAHLKDV-----IRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
170 180 190
....*....|....*....|....*....|...
gi 1796960594 169 GNLDGDTAQDIIELLttlnREQFM--TLLMVTH 199
Cdd:PLN03130 1403 AAVDVRTDALIQKTI----REEFKscTMLIIAH 1431
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-188 |
1.39e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 9 GVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEV---AQADADQRAVTrnrllg 85
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGIS------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 86 FVFQSFNLLPRLSVLDNVAL---PLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRIL 162
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180
....*....|....*....|....*.
gi 1796960594 163 LADEPTGNLdgdTAQDIIELLTTLNR 188
Cdd:PRK10982 157 IMDEPTSSL---TEKEVNHLFTIIRK 179
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
16-203 |
1.97e-08 |
|
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: 53.98 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 16 GEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLdQPCHGSLVLDGSEVAQADADQRAVTRNRLLgfvfqsfnllp 95
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGRLTKPAKGKLFYVPQRPYMTLGTL----------- 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 96 rlsvLDNVALPLSY-----RGIRLASARQIAK-VQLE-----KVGLEPRAKYRPAdLSGGQRQRVAIARALVTEPRILLA 164
Cdd:TIGR00954 532 ----RDQIIYPDSSedmkrRGLSDKDLEQILDnVQLThilerEGGWSAVQDWMDV-LSGGEKQRIAMARLFYHKPQFAIL 606
|
170 180 190
....*....|....*....|....*....|....*....
gi 1796960594 165 DEPTGNLDGDTAQDIIELLttlnREQFMTLLMVTHDPAM 203
Cdd:TIGR00954 607 DECTSAVSVDVEGYMYRLC----REFGITLFSVSHRKSL 641
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
35-216 |
4.37e-08 |
|
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: 52.03 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 35 IVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVA----QADADQRAVTRNrLLGFVFQSFNLLPRLSVldNVALPLsyr 110
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYEGTVRD-LLSSITKDFYTHPYFKT--EIAKPL--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 111 girlasarqiakvQLEKVgLEPRAKyrpaDLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDT---AQDIIELLtTLN 187
Cdd:cd03237 104 -------------QIEQI-LDREVP----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrlmASKVIRRF-AEN 164
|
170 180
....*....|....*....|....*....
gi 1796960594 188 REQfmTLLMVTHDPAMAQCMDRCLLVRNG 216
Cdd:cd03237 165 NEK--TAFVVEHDIIMIDYLADRLIVFEG 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
14-216 |
6.38e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAvLQDVSFSLPTGQSCAIVGASGSGKSTLL-NLIGLLDQPChGSLVLDGSEVAQADadqravTRNRL-LGFVF--- 88
Cdd:PRK15439 274 LTGEG-FRNISLEVRAGEILGLAGVVGAGRTELAeTLYGLRPARG-GRIMLNGKEINALS------TAQRLaRGLVYlpe 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 89 --QSFNLLPRLSVLDNV-ALPLSYRGIRLASARQIAKvqLEKVGLEPRAKYRPAD-----LSGGQRQRVAIARALVTEPR 160
Cdd:PRK15439 346 drQSSGLYLDAPLAWNVcALTHNRRGFWIKPARENAV--LERYRRALNIKFNHAEqaartLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 161 ILLADEPTGNLDGDTAQDIIELLTTLNrEQFMTLLMVTHD----PAMAqcmDRCLLVRNG 216
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFISSDleeiEQMA---DRVLVMHQG 479
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-216 |
8.66e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 51.09 E-value: 8.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 23 VSFSLPTGQSCAIVGASGSGKSTLLNLI-GLLDQPchGSLVLDGSEVAQADADQRAVTRnrllGFVFQSFNLLPRLSVLD 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMaGLLPGS--GSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 102 NVALPLSyRGIRLASARQIAKVQLEKVGLEPRAKyRPAD-LSGGQRQRVAIA-------RALVTEPRILLADEPTGNLdg 173
Cdd:PRK03695 89 YLTLHQP-DKTRTEAVASALNEVAEALGLDDKLG-RSVNqLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSL-- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1796960594 174 DTAQDIieLLTTLNRE---QFMTLLMVTHD-PAMAQCMDRCLLVRNG 216
Cdd:PRK03695 165 DVAQQA--ALDRLLSElcqQGIAVVMSSHDlNHTLRHADRVWLLKQG 209
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-201 |
1.12e-07 |
|
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: 49.68 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 29 TGQSCAIVGASGSGKSTLLNLI-GLLDQPCHGSLVLDGSEVAQADADQRAVTRNrllgfvfqsfnllprlsvldnvalpl 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLLIIV-------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 108 syrgirlasarqiakvqlekvglepraKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLN 187
Cdd:smart00382 55 ---------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107
|
170
....*....|....*....
gi 1796960594 188 REQFM-----TLLMVTHDP 201
Cdd:smart00382 108 LLLLKseknlTVILTTNDE 126
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-200 |
1.71e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.05 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSE-VAQADADQravtrnr 82
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNErLGKLRQDQ------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 83 llgFVFQSFnllprlSVLDNV------------------ALPLSYR--GIRLA------------SARQIAKVQLEKVGL 130
Cdd:PRK15064 74 ---FAFEEF------TVLDTVimghtelwevkqerdriyALPEMSEedGMKVAdlevkfaemdgyTAEARAGELLLGVGI 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 131 EPRAKYRP-ADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTaqdIIELLTTLNrEQFMTLLMVTHD 200
Cdd:PRK15064 145 PEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVLN-ERNSTMIIISHD 211
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-172 |
1.79e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADadqravtrnrlLGFVFQSFNLLPRLS 98
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG-----------LRELRRQFSMIPQDP 1393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 99 VL------DNV-----ALPLS-YRGIRLASARQiaKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPR-ILLAD 165
Cdd:PTZ00243 1394 VLfdgtvrQNVdpfleASSAEvWAALELVGLRE--RVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMD 1471
|
....*..
gi 1796960594 166 EPTGNLD 172
Cdd:PTZ00243 1472 EATANID 1478
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-175 |
1.91e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 50.29 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 19 VLQDVSFSLPTGQSCAIVGASGSGKSTL----LNLIGLLDqpchGSLVLDGSEVAQADADqraVTRNRLlGFVFQS---- 90
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLPLH---TLRSRL-SIILQDpilf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 91 -----FNLLPRLSVLDNvalplsyrgiRLASARQIAkvQLEKV------GLEPRAKYRPADLSGGQRQRVAIARALVTEP 159
Cdd:cd03288 108 sgsirFNLDPECKCTDD----------RLWEALEIA--QLKNMvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175
|
170
....*....|....*.
gi 1796960594 160 RILLADEPTGNLDGDT 175
Cdd:cd03288 176 SILIMDEATASIDMAT 191
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-172 |
3.35e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGL-----LDQPCH-----GSLVLDGSEVAQA--DADqraVTRN 81
Cdd:PLN03073 187 VGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaidgIPKNCQilhveQEVVGDDTTALQCvlNTD---IERT 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 82 RLLGfvfQSFNLLPRLSVLDNVALPLSYRGIR-------LASAR--QIAKvQLEKV---GLEPRAKYRPADLS------- 142
Cdd:PLN03073 264 QLLE---EEAQLVAQQRELEFETETGKGKGANkdgvdkdAVSQRleEIYK-RLELIdayTAEARAASILAGLSftpemqv 339
|
170 180 190
....*....|....*....|....*....|....*..
gi 1796960594 143 -------GGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PLN03073 340 katktfsGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
14-216 |
3.45e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 14 LGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVaQADADQRAVTRNRLL--------G 85
Cdd:PRK11288 263 LKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAIRAGIMLcpedrkaeG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 86 FVfqsfnllPRLSVLDNVALplSYRG--------IRLASARQIAKVQLEKVGLE-PRAKYRPADLSGGQRQRVAIARALV 156
Cdd:PRK11288 342 II-------PVHSVADNINI--SARRhhlragclINNRWEAENADRFIRSLNIKtPSREQLIMNLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1796960594 157 TEPRILLADEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHD-PAMAQCMDRCLLVRNG 216
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDlPEVLGVADRIVVMREG 472
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-210 |
4.24e-07 |
|
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: 50.01 E-value: 4.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 2 SSIISLHGVTRWLGGEA--VLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEVAQADADqravt 79
Cdd:TIGR01257 1935 TDILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD----- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 rnrllgfVFQSFNLLPRLSVLDNVA-------LPLSYRGIRLASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIA 152
Cdd:TIGR01257 2010 -------VHQNMGYCPQFDAIDDLLtgrehlyLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQfMTLLMVTHdpAMAQCMDRC 210
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREG-RAVVLTSH--SMEECEALC 2137
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-208 |
6.55e-07 |
|
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: 47.99 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 34 AIVGASGSGKSTLLN-----LIGLLDQPCHG-----SLVLDGSEVAQADADQRAVTRNRLLgfVFQSFNllprlsVLDNV 103
Cdd:cd03240 26 LIVGQNGAGKTTIIEalkyaLTGELPPNSKGgahdpKLIREGEVRAQVKLAFENANGKKYT--ITRSLA------ILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 104 ALplsyrgirlasARQ--IAKVQLEKVGLeprakyrpadLSGGQRQ------RVAIARALVTEPRILLADEPTGNLDGDT 175
Cdd:cd03240 98 IF-----------CHQgeSNWPLLDMRGR----------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN 156
|
170 180 190
....*....|....*....|....*....|....
gi 1796960594 176 -AQDIIELLTTLNREQFMTLLMVTHDPAMAQCMD 208
Cdd:cd03240 157 iEESLAEIIEERKSQKNFQLIVITHDEELVDAAD 190
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
133-204 |
9.34e-07 |
|
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: 47.57 E-value: 9.34e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 133 RAKYRPA--DLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLMVTHDPAMA 204
Cdd:cd03222 62 TPVYKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVL 135
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
20-166 |
3.89e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 3.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLDGSEvaqadadqravtrnrllGFVFQSFNLLPRLSV 99
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------------ALIAISSGLNGQLTG 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1796960594 100 LDNVALPLSYRGIRLASARQIAKVQLE-----KVGLEPRAKYrpadlSGGQRQRVAIARALVTEPRILLADE 166
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEfadigKFIYQPVKTY-----SSGMKSRLGFAISVHINPDILVIDE 169
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-199 |
4.46e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.93 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLN--LIGLLDQPCHGSLVLDGS-----------EVAQADAD-----QR----- 76
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtLYPALANRLNGAKTVPGRytsieglehldKVIHIDQSpigrtPRsnpat 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 77 -------------AVTRNRLLGFV---FqSFNL--------------------LPRLSVLDNV---------ALPLSYRG 111
Cdd:TIGR00630 704 ytgvfdeirelfaETPEAKVRGYTpgrF-SFNVkggrceacqgdgvikiemhfLPDVYVPCEVckgkrynreTLEVKYKG 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 112 IRLA--------SAR-------QIA-KVQ-LEKVGLEPRAKYRPA-DLSGGQRQRVAIARAL---VTEPRILLADEPTGN 170
Cdd:TIGR00630 783 KNIAdvldmtveEAYeffeavpSISrKLQtLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTG 862
|
250 260 270
....*....|....*....|....*....|.
gi 1796960594 171 LDGDtaqDIIELLTTLNR--EQFMTLLMVTH 199
Cdd:TIGR00630 863 LHFD---DIKKLLEVLQRlvDKGNTVVVIEH 890
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
140-172 |
5.68e-06 |
|
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: 46.32 E-value: 5.68e-06
10 20 30
....*....|....*....|....*....|...
gi 1796960594 140 DLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-209 |
5.80e-06 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLL---------------------NLIGLLDQPCHGSLvlDGSEVAQAdADQRAV 78
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSI--EGLSPAIA-IDQKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 79 TRNrllgfvfqsfnllPRLSV------LDNVALPLSYRGI--RLAsarqiakvQLEKVGLEPRAKYRPAD-LSGGQRQRV 149
Cdd:cd03270 88 SRN-------------PRSTVgtvteiYDYLRLLFARVGIreRLG--------FLVDVGLGYLTLSRSAPtLSGGEAQRI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 150 AIAR----ALVTEPRILlaDEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQCMDR 209
Cdd:cd03270 147 RLATqigsGLTGVLYVL--DEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADH 207
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
117-218 |
5.91e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.27 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 117 ARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNREQFMTLLM 196
Cdd:NF000106 121 ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200
|
90 100
....*....|....*....|..
gi 1796960594 197 VTHDPAMAQCMDRCLLVRNGGV 218
Cdd:NF000106 201 TQYMEEAEQLAHELTVIDRGRV 222
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
140-172 |
8.53e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 8.53e-06
10 20 30
....*....|....*....|....*....|...
gi 1796960594 140 DLSGGQRQRVAIARALVTEPRILLADEPTGNLD 172
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-200 |
9.58e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.19 E-value: 9.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSlvldgsevaqadadqraVTRNRLLGFVFQSFNLLPRLSV 99
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK-----------------VDRNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 100 LDNVALPLSYRGIRLASARQIAK--VQLEKVG---LEPRAKYrpadlSGGQRQRVAIARALVTEPRILLADEPTGNLDGD 174
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPkiIEFSELGefiYQPVKKY-----SSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*.
gi 1796960594 175 TAQDIIELLTTLnREQFMTLLMVTHD 200
Cdd:PRK13546 178 FAQKCLDKIYEF-KEQNKTIFFVSHN 202
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-208 |
9.81e-06 |
|
ATP-binding cassette domain II 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: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.30 E-value: 9.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLN--LIGLLDQPCHGSLV----LDGSEVAQA-----DADQRAVTRNrllgfvf 88
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtLYPALARRLHLKKEqpgnHDRIEGLEHidkviVIDQSPIGRT------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 89 QSFNLLPRLSVLDNV----------------ALPLSYRGIRLA---------------SARQIA-KVQ-LEKVGLEPRAK 135
Cdd:cd03271 84 PRSNPATYTGVFDEIrelfcevckgkrynreTLEVRYKGKSIAdvldmtveealeffeNIPKIArKLQtLCDVGLGYIKL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1796960594 136 YRPA-DLSGGQRQRVAIARAL---VTEPRILLADEPTGNLDGDtaqDIIELLTTLNR--EQFMTLLMVTHDPAMAQCMD 208
Cdd:cd03271 164 GQPAtTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFH---DVKKLLEVLQRlvDKGNTVVVIEHNLDVIKCAD 239
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
34-200 |
1.23e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 34 AIVGASGSGKSTLLNLIGLL-------DQPCHGSLVLDGSEVA------------------QADADQRAVTRNRLLGFVF 88
Cdd:COG0419 27 LIVGPNGAGKSTILEAIRYAlygkarsRSKLRSDLINVGSEEAsvelefehggkryrierrQGEFAEFLEAKPSERKEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 89 QSFNLLPRLS----VLDNVALPLSYRGIRLASARQIAKVQLEKV-GLEPrakyrPADLSGGQRQRVAIARALvtepRILL 163
Cdd:COG0419 107 KRLLGLEIYEelkeRLKELEEALESALEELAELQKLKQEILAQLsGLDP-----IETLSGGERLRLALADLL----SLIL 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 1796960594 164 aDepTGNLDGDTAQDIIELLTTLNreqfmtllMVTHD 200
Cdd:COG0419 178 -D--FGSLDEERLERLLDALEELA--------IITHV 203
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-203 |
1.56e-05 |
|
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: 45.16 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 25 FSLPT---GQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSL--------VLD---GSEVAQ-----ADADQRAVTRNrll 84
Cdd:COG1245 91 YGLPVpkkGKVTGILGPNGIGKSTALKiLSGEL-KPNLGDYdeepswdeVLKrfrGTELQDyfkklANGEIKVAHKP--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 gfvfQSFNLLPRL------SVLDNValplSYRGIrlasARQIAkvqlEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:COG1245 167 ----QYVDLIPKVfkgtvrELLEKV----DERGK----LDELA----EKLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 159 PRILLADEPTGNLDGD---TAQDIIELLTTLNReqfmTLLMVTHDPAM 203
Cdd:COG1245 231 ADFYFFDEPSSYLDIYqrlNVARLIRELAEEGK----YVLVVEHDLAI 274
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-172 |
3.03e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 25 FSLPT---GQSCAIVGASGSGKSTLLN-LIGLLdQPCHGSL--------VLD---GSEVAQ-----ADADQRAVTRNrll 84
Cdd:PRK13409 91 YGLPIpkeGKVTGILGPNGIGKTTAVKiLSGEL-IPNLGDYeeepswdeVLKrfrGTELQNyfkklYNGEIKVVHKP--- 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 85 gfvfQSFNLLPRL------SVLDNValplSYRGIrlasARQIAkvqlEKVGLEPRAKYRPADLSGGQRQRVAIARALVTE 158
Cdd:PRK13409 167 ----QYVDLIPKVfkgkvrELLKKV----DERGK----LDEVV----ERLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
170
....*....|....
gi 1796960594 159 PRILLADEPTGNLD 172
Cdd:PRK13409 231 ADFYFFDEPTSYLD 244
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-200 |
4.09e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 7 LHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGlldqpchGSLVLDGSEVAQADadqravtrNRLLGF 86
Cdd:PRK15064 322 VENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVKWSE--------NANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 87 VFQ--SFNLLPRLSVLDNVAL-------PLSYRGI--R-LASARQIAK-VqleKVgleprakyrpadLSGGQRQRVAIAR 153
Cdd:PRK15064 387 YAQdhAYDFENDLTLFDWMSQwrqegddEQAVRGTlgRlLFSQDDIKKsV---KV------------LSGGEKGRMLFGK 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1796960594 154 ALVTEPRILLADEPTGNLDgdtaqdiIELLTTLNR--EQFM-TLLMVTHD 200
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMD-------MESIESLNMalEKYEgTLIFVSHD 494
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
141-217 |
5.24e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 141 LSGGQRQRVAIARALVTEPRILLADEPTGNLDGDTAQdiIELLTTLNR-EQFMTLLMVTHDPAMA--QCMDRCLLVRNGG 217
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAA--IVMRTVRNTvDTGRTVVCTIHQPSIDifEAFDELLLMKRGG 1097
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-202 |
5.63e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 42.74 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 25 FSLPT---GQSCAIVGASGSGKSTLLNLI--------GLLDQPCHGSLVLD---GSEVAQ-----ADADQRAVTRNrllg 85
Cdd:cd03236 18 HRLPVpreGQVLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDWDEILDefrGSELQNyftklLEGDVKVIVKP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 86 fvfQSFNLLPRlSVLDNVALPLSYrgirlASARQIAKVQLEKVGLEPRAKYRPADLSGGQRQRVAIARALVTEPRILLAD 165
Cdd:cd03236 94 ---QYVDLIPK-AVKGKVGELLKK-----KDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1796960594 166 EPTGNLD----GDTAQDIIELLTTLNreqfmTLLMVTHDPA 202
Cdd:cd03236 165 EPSSYLDikqrLNAARLIRELAEDDN-----YVLVVEHDLA 200
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
15-200 |
6.66e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 15 GGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLI--------GLLDQPCHGSL-----------------VLDGS-EV 68
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLkneisadgGSYTFPGNWQLawvnqetpalpqpaleyVIDGDrEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 69 AQADAD-QRAVTRNRllGFVFQSfnLLPRLSVLDnvALPLSYRGIRLASARQIAKVQLEkvgleprakyRP-ADLSGGQR 146
Cdd:PRK10636 92 RQLEAQlHDANERND--GHAIAT--IHGKLDAID--AWTIRSRAASLLHGLGFSNEQLE----------RPvSDFSGGWR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1796960594 147 QRVAIARALVTEPRILLADEPTGNLDGDTaqdIIELLTTLNREQfMTLLMVTHD 200
Cdd:PRK10636 156 MRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQ-GTLILISHD 205
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-205 |
1.41e-04 |
|
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: 40.81 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 21 QDVSFSLPTGQScaIVGASGSGKSTLLNLIGLLdqpchgslvldgsevaqadadqravtrnrllgFVFQSFNLLPRlsvl 100
Cdd:cd03227 14 NDVTFGEGSLTI--ITGPNGSGKSTILDAIGLA--------------------------------LGGAQSATRRR---- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 101 dnvalplSYRGIRLASARQIAKVQLEKVGLeprakyrpadlSGGQRQRVAIARALV---TEPRILLA-DEPTGNLDGDTA 176
Cdd:cd03227 56 -------SGVKAGCIVAAVSAELIFTRLQL-----------SGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDG 117
|
170 180
....*....|....*....|....*....
gi 1796960594 177 QDIIELLtTLNREQFMTLLMVTHDPAMAQ 205
Cdd:cd03227 118 QALAEAI-LEHLVKGAQVIVITHLPELAE 145
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
139-219 |
1.48e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 139 ADLSGGQRQRVAIARALVTE----PRILlaDEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTHDPAMAQCMDRCLLVR 214
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAEligiTYIL--DEPSIGLHPQDTHKLINVIKKL-RDQGNTVLLVEHDEQMISLADRIIDIG 551
|
....*.
gi 1796960594 215 NG-GVF 219
Cdd:PRK00635 552 PGaGIF 557
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-48 |
1.65e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 1.65e-04
10 20
....*....|....*....|....*....
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLN 48
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-48 |
2.10e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.10e-04
10 20
....*....|....*....|....*....
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLN 48
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
20-200 |
3.27e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 20 LQDVSFSLPTGQSCAIVGASGSGKSTLLN------LIGLLDQPCHGSLVLDG---SEVAQADAD-----QRAVT------ 79
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpaVEEFIEQGFCSNLSIQWgaiSRLVHITRDlpgrsQRSIPltyika 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 80 ------------RNRLLGFV---FqSFNL----------LPRLSVLDN----------------VALPLSYRGIRLASAR 118
Cdd:PRK00635 691 fddlrelfaeqpRSKRLGLTkshF-SFNTplgacaecqgLGSITTTDNrtsipcpsclgkrflpQVLEVRYKGKNIADIL 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 119 QIAKVQLEK-----------------VGLEPRAKYRP-ADLSGGQRQRVAIARAL---VTEPRILLADEPTGNLDGDTAQ 177
Cdd:PRK00635 770 EMTAYEAEKffldepsihekihalcsLGLDYLPLGRPlSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIK 849
|
250 260
....*....|....*....|...
gi 1796960594 178 DIIELLTTLNrEQFMTLLMVTHD 200
Cdd:PRK00635 850 ALIYVLQSLT-HQGHTVVIIEHN 871
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-200 |
4.49e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 4 IISLHGVTRWLGGEAVLQDVSFSLPTGQSCAIVGASGSGKSTLLNLIGLLDQPCHGSLVLdgsevaqadadqravTRNRL 83
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------------AKGIK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 84 LGFVFQSfnllpRLSVLDNVALPLSYRgIRLASarQIAKVQL-----------EKVGlEPRAKYrpadlSGGQRQRVAIA 152
Cdd:PRK10636 377 LGYFAQH-----QLEFLRADESPLQHL-ARLAP--QELEQKLrdylggfgfqgDKVT-EETRRF-----SGGEKARLVLA 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1796960594 153 RALVTEPRILLADEPTGNLDGDTAQDIIELLTTLNReqfmTLLMVTHD 200
Cdd:PRK10636 443 LIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEG----ALVVVSHD 486
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
30-94 |
1.64e-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: 38.15 E-value: 1.64e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 30 GQSCAIVGASGSGKSTLLNLIglldqpcHGSLVLDGSEVAQADADQRAVTRNRLL------GFV-----FQSFNLL 94
Cdd:cd01854 85 GKTSVLVGQSGVGKSTLLNAL-------LPELVLATGEISEKLGRGRHTTTHRELfplpggGLIidtpgFRELGLL 153
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-209 |
4.26e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1796960594 125 LEKVGLEPRAKYRPAD-LSGGQRQRVAIAR----ALVTEPRILlaDEPTGNLDGDTAQDIIELLTTLnREQFMTLLMVTH 199
Cdd:TIGR00630 472 LIDVGLDYLSLSRAAGtLSGGEAQRIRLATqigsGLTGVLYVL--DEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEH 548
|
90
....*....|
gi 1796960594 200 DPAMAQCMDR 209
Cdd:TIGR00630 549 DEDTIRAADY 558
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
141-168 |
4.79e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.46 E-value: 4.79e-03
10 20
....*....|....*....|....*...
gi 1796960594 141 LSGGQRQRVAIARALVTEPRILLADEPT 168
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
29-93 |
6.62e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 35.98 E-value: 6.62e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1796960594 29 TGQSCAIVGASGSGKSTLLNLIglldqpcHGSLVLDGSEVAQADADQRAVTRNRLL------GFV-----FQSFNL 93
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNAL-------LPELDLRTGEISEKLGRGRHTTTHVELfplpggGLLidtpgFRELGL 173
|
|
| |
