|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-223 |
2.09e-110 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 316.99 E-value: 2.09e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHSNIDASYAERVIFIKDGRLYHEI 223
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPELAARADRVIRLRDGRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-219 |
9.23e-103 |
|
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: 297.48 E-value: 9.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYR 82
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLE-QTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-227 |
1.14e-82 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 246.50 E-value: 1.14e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYR 82
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMvGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:COG2884 79 RRI-GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH-SNIDASYAERVIFIKDGRLYHEIYRGE 227
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHdLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
2.91e-77 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 234.21 E-value: 2.91e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskal 80
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 yrqqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTK 160
Cdd:COG1116 82 -----RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 161 PTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHsNID-ASY-AERVIFIKD--GRLYHEI 223
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELLRLWQETGkTVLFVTH-DVDeAVFlADRVVVLSArpGRIVEEI 223
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-212 |
2.40e-75 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 227.74 E-value: 2.40e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNmkneskalyR 82
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHsNID-ASY-AERVI 212
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTH-DIDeAVFlADRVV 203
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
2-219 |
2.14e-71 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 217.66 E-value: 2.14e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:NF038007 1 MLNMQNAEKCYITKTIKTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKIIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:NF038007 81 RRELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:NF038007 161 ALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDGKL 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-219 |
3.98e-71 |
|
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: 217.69 E-value: 3.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGakRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 162 TILLADEPTGALDSKTSKTLM-MLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIdLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRL 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-219 |
6.52e-70 |
|
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: 213.92 E-value: 6.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyr 82
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03259 74 ---IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQrELGITTIYVTHDQEEAlALADRIAVMNEGRI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2-225 |
4.10e-69 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 216.50 E-value: 4.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskaly 81
Cdd:COG3842 5 ALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 rQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:COG3842 76 -KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNIDA-SYAERVIFIKDGRLY-----HEIYR 225
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQReLGITFIYVTHDQEEAlALADRIAVMNDGRIEqvgtpEEIYE 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-200 |
6.05e-66 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 208.01 E-value: 6.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLNNMKNESKA 79
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCIN---LLerpTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYRQQmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLtvqLH---LEGFLNKYPSEISGGQKQRIAIARA 156
Cdd:COG1135 79 AARRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAEL---LElvgLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487401142 157 LVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTH 200
Cdd:COG1135 155 LANNPKVLLCDEATSALDPETTRSILDLLKDINReLGLTIVLITH 199
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-219 |
6.48e-65 |
|
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: 201.66 E-value: 6.48e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMvGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:cd03258 81 RRRI-GMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHS-NIDASYAERVIFIKDGRL 219
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINReLGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
3-225 |
1.70e-64 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 204.54 E-value: 1.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNeskalyR 82
Cdd:COG3839 4 LELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNIDA-SYAERVIFIKDGRLY-----HEIYR 225
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRrLGTTTIYVTHDQVEAmTLADRIAVMNDGRIQqvgtpEELYD 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-219 |
1.98e-64 |
|
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: 199.94 E-value: 1.98e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYR 82
Cdd:cd03292 1 IEFINVTKTYP---NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMvGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03292 78 RKI-GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH-SNIDASYAERVIFIKDGRL 219
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHaKELVDTTRHRVIALERGKL 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2-219 |
1.53e-62 |
|
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: 195.42 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMvGFVFQD----FNllPTMTNKENIMMPLILAGAKRKD--IEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQRIAIA 154
Cdd:cd03257 81 RKEI-QMVFQDpmssLN--PRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 155 RALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGlTLLFITH-DLGvvAKIADRVAVMYAGKI 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
2.84e-62 |
|
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: 203.21 E-value: 2.84e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYG-KGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAL 80
Cdd:COG1123 260 LLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQQmVGFVFQD----FNllPTMTNKENIMMPLILAG-AKRKDIEQRVHQL--TVQLHlEGFLNKYPSEISGGQKQRIAI 153
Cdd:COG1123 340 LRRR-VQMVFQDpyssLN--PRMTVGDIIAEPLRLHGlLSRAERRERVAELleRVGLP-PDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 154 ARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQReLGLTYLFISH-DLAvvRYIADRVAVMYDGRI 483
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
5-214 |
1.45e-60 |
|
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: 189.75 E-value: 1.45e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 5 VKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYRQQ 84
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 85 MVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTIL 164
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487401142 165 LADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFI 214
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-219 |
1.91e-60 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 193.82 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmknesKAL 80
Cdd:COG1118 1 MSIEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----------RDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 Y-----RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIAR 155
Cdd:COG1118 67 FtnlppRERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 156 ALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHsNIDASY--AERVIFIKDGRL 219
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDeLGGTTVFVTH-DQEEALelADRVVVMNQGRI 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-225 |
5.43e-60 |
|
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: 188.98 E-value: 5.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMkneskALYR 82
Cdd:cd03300 1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-----PPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03300 72 RP-VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNIDA-SYAERVIFIKDGRLYH-----EIYR 225
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKeLGITFVFVTHDQEEAlTMSDRIAVMNKGKIQQigtpeEIYE 220
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-230 |
1.27e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 188.73 E-value: 1.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAL 80
Cdd:COG3638 1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQQmVGFVFQDFNLLPTMTNKENIM------MPLILAGAK---RKDIeQRVHQLTVQLHLEGFLNKYPSEISGGQKQRI 151
Cdd:COG3638 78 LRRR-IGMIFQQFNLVPRLSVLTNVLagrlgrTSTWRSLLGlfpPEDR-ERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 152 AIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHS-NIDASYAERVIFIKDGRL---------- 219
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGiTVVVNLHQvDLARRYADRIIGLRDGRVvfdgppaelt 235
|
250
....*....|....
gi 487401142 220 ---YHEIYRGEESQ 230
Cdd:COG3638 236 davLREIYGGEAEE 249
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-227 |
1.77e-59 |
|
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: 188.47 E-value: 1.77e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnmKNESKALY 81
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT--RRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQqmVGFVFQD----FNllPTMTNKENIMMPLILAGakRKDIEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQRIAIARA 156
Cdd:COG1124 79 RR--VQMVFQDpyasLH--PRHTVDRILAEPLRIHG--LPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 157 LVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHsNID--ASYAERVIFIKDGRLYHEIYRGE 227
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGlTYLFVSH-DLAvvAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-219 |
3.91e-59 |
|
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: 186.77 E-value: 3.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGahlNNMKNESKA 79
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLN---GLlkpTSGEVLVDG---KDITKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYRQQmVGFVFQD-----FNllptMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIA 154
Cdd:COG1122 72 ELRRK-VGLVFQNpddqlFA----PTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 155 RALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTH-DLDlvAELADRVIVLDDGRI 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-218 |
2.39e-58 |
|
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: 183.16 E-value: 2.39e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYR 82
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QqmVGFVFQDFNLLPTMTNKENIMMPLilagakrkdieqrvhqltvqlhlegflnkypseiSGGQKQRIAIARALVTKPT 162
Cdd:cd03229 77 R--IGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHSNIDASY-AERVIFIKDGR 218
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-218 |
5.29e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.43 E-value: 5.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALy 81
Cdd:COG1126 1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQmVGFVFQDFNLLPTMTNKENIMMPLILA-GAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTK 160
Cdd:COG1126 76 RRK-VGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 161 PTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsniDASYAE----RVIFIKDGR 218
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH---EMGFARevadRVVFMDGGR 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-219 |
1.83e-57 |
|
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: 181.96 E-value: 1.83e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALyR 82
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL-R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDFNLLPTMTNKENIMMPLILA-GAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:cd03262 76 QK-VGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-218 |
3.36e-57 |
|
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: 182.38 E-value: 3.36e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYR 82
Cdd:cd03256 1 IEVENLSKTYP---NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMvGFVFQDFNLLPTMTNKENIMMPL---------ILAGAKRKDIEQRVHQLTvQLHLEGFLNKYPSEISGGQKQRIAI 153
Cdd:cd03256 78 RQI-GMIFQQFNLIERLSVLENVLSGRlgrrstwrsLFGLFPKEEKQRALAALE-RVGLLDKAYQRADQLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 154 ARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:cd03256 156 ARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGiTVIVSLHQvDLAREYADRIVGLKDGR 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
4-219 |
4.35e-57 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 185.39 E-value: 4.35e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYRQ 83
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 84 QmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTI 163
Cdd:PRK11153 83 Q-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 164 LLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSnIDA--SYAERVIFIKDGRL 219
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINReLGLTIVLITHE-MDVvkRICDRVAVIDAGRL 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-222 |
5.24e-57 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 181.72 E-value: 5.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLNNMKNESK 78
Cdd:COG1127 5 MIEVRNLTKSFGD----RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLII---GLlrpDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQQMvGFVFQDFNLLPTMTNKENIMMPLI-LAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARAL 157
Cdd:COG1127 78 YELRRRI-GMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 158 VTKPTILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHsNIDASY--AERVIFIKDGRLYHE 222
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRdELGLTSVVVTH-DLDSAFaiADRVAVLADGKIIAE 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-222 |
8.85e-57 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 181.44 E-value: 8.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNmKNESKALY 81
Cdd:PRK09493 1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQmVGFVFQDFNLLPTMTNKENIMM-PLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTK 160
Cdd:PRK09493 76 RQE-AGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 161 PTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsniDASYAERV----IFIKDGRLYHE 222
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH---EIGFAEKVasrlIFIDKGRIAED 217
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-219 |
1.39e-56 |
|
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: 179.76 E-value: 1.39e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyr 82
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03301 74 ---IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQrLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-218 |
2.35e-56 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 179.20 E-value: 2.35e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKGlnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnmKNESKALYRq 83
Cdd:cd03225 1 ELKNLSFSYPDG--ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT--KLSLKELRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 84 qMVGFVFQDFNL-LPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03225 76 -KVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNID--ASYAERVIFIKDGR 218
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTH-DLDllLELADRVIVLEDGK 211
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
3-219 |
2.89e-56 |
|
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: 179.44 E-value: 2.89e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYR 82
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDFNLLPTMTNKENIMMPL-ILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:TIGR02982 82 RR-IGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIhQLEQ--TILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKL-AKEQgcTILMVTHDNRILDVADRILQMEDGKL 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-223 |
1.23e-55 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 178.09 E-value: 1.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:PRK11629 85 RNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQLEQT-ILMVTHSNIDASYAERVIFIKDGRLYHEI 223
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTaFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-222 |
3.49e-55 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 176.89 E-value: 3.49e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:PRK10584 86 RAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 162 TILLADEPTGALDSKTSKTLM-MLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRLYHE 222
Cdd:PRK10584 166 DVLFADEPTGNLDRQTGDKIAdLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-219 |
1.80e-54 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 185.31 E-value: 1.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-219 |
1.21e-53 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.94 E-value: 1.21e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnNMKNESKALYR 82
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE---DVARDPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:COG1131 74 R--IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTH-YLEeaERLCDRVAIIDKGRI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-219 |
1.70e-52 |
|
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: 170.21 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmKNESKAL 80
Cdd:cd03296 1 MSIEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG------EDATDVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRK----DIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARA 156
Cdd:cd03296 71 VQERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 157 LVTKPTILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEAlEVADRVVVMNKGRI 215
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2-200 |
3.17e-52 |
|
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: 172.16 E-value: 3.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTL----LNLIASfDGLTEGDIIVDGAHLNNMKNES 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPP-PGITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KALYRQQMVGFVFQD----FNllPTMTNKENIMMPLIL-AGAKRKDIEQRVHQL--TVQLHL-EGFLNKYPSEISGGQKQ 149
Cdd:COG0444 80 LRKIRGREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIhGGLSKAEARERAIELleRVGLPDpERRLDRYPHELSGGMRQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 487401142 150 RIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTH 200
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITH 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-219 |
4.78e-52 |
|
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: 169.02 E-value: 4.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlNNMKNESKALYR 82
Cdd:cd03295 1 IEFENVTKRYGGG---KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE--DIREQDPVELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLE--GFLNKYPSEISGGQKQRIAIARALVTK 160
Cdd:cd03295 76 K--IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 161 PTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHsNIDASY--AERVIFIKDGRL 219
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQeLGKTIVFVTH-DIDEAFrlADRIAIMKNGEI 214
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
3-219 |
1.27e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.92 E-value: 1.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVkkvyGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalYR 82
Cdd:COG4619 1 LELEGL----SFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE---WR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDFNLLPtMTNKENIMMPLILAgaKRKDIEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:COG4619 74 RQ-VAYVPQEPALWG-GTVRDNLPFPFQLR--ERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHSNIDAS-YAERVIFIKDGRL 219
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGrAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
22-221 |
1.41e-51 |
|
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: 167.90 E-value: 1.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyrqqmVGFVFQDFNLLPTMTN 101
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD------ISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 KENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTL 181
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 487401142 182 MMLFQEIH-QLEQTILMVTHSNIDA-SYAERVIFIKDGRLYH 221
Cdd:cd03299 169 REELKKIRkEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQ 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
2-231 |
2.22e-51 |
|
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: 167.48 E-value: 2.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:TIGR02315 1 MLEVENLSKVYP---NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMvGFVFQDFNLLPTMTNKENIMMP---------LILAGAKRKDIEqRVHQLTVQLHLEGFLNKYPSEISGGQKQRIA 152
Cdd:TIGR02315 78 RRRI-GMIFQHYNLIERLTVLENVLHGrlgykptwrSLLGRFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 153 IARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNID--ASYAERVIFIKDGRLyheIYRGEESQ 230
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDlaKKYADRIVGLKAGEI---VFDGAPSE 232
|
.
gi 487401142 231 L 231
Cdd:TIGR02315 233 L 233
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
3-248 |
3.01e-51 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 170.60 E-value: 3.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALyr 82
Cdd:TIGR03265 5 LSIDNIRKRFG----AFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qqmvGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:TIGR03265 79 ----GIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 163 ILLADEPTGALDSKTSKTLMmlfQEIHQLEQ----TILMVTHSNIDA-SYAERVIFIKDGRLYH-----EIYR------- 225
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLR---TEIRQLQRrlgvTTIMVTHDQEEAlSMADRIVVMNHGVIEQvgtpqEIYRhpatpfv 231
|
250 260
....*....|....*....|....*..
gi 487401142 226 ----GEESQLAFqQRITDSLALVNGGS 248
Cdd:TIGR03265 232 adfvGEVNWLPG-TRGGGSRARVGGLT 257
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-201 |
1.08e-49 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 163.88 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnnmknESKAL 80
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-----TGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRqqmvGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTK 160
Cdd:COG4525 77 DR----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAAD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 487401142 161 PTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHS 201
Cdd:COG4525 153 PRFLLMDEPFGALDALTREQMQELLLDVWQRTGkGVFLITHS 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-219 |
2.85e-49 |
|
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: 168.93 E-value: 2.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGlnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIA---SFDGLTEGDIIVDGAHLNNMKNEsk 78
Cdd:COG1123 4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMgllPHGGRISGEVLLDGRDLLELSEA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 alYRQQMVGFVFQDF-NLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARAL 157
Cdd:COG1123 80 --LRGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 158 VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNID-ASYAERVIFIKDGRL 219
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVvAEIADRVVVMDDGRI 221
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-219 |
2.40e-48 |
|
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: 160.69 E-value: 2.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGL-NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLiasFDGL---TEGDIIVDGAHLNNMKNESK 78
Cdd:TIGR04521 1 IKLKNVSYIYQPGTpFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQH---LNGLlkpTSGTVTIDGRDITAKKKKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQQmVGFVFQdF--NLLPTMTNKENIMM-PLILaGAKRKDIEQRVHQL--TVQLHlEGFLNKYPSEISGGQKQRIAI 153
Cdd:TIGR04521 78 KDLRKK-VGLVFQ-FpeHQLFEETVYKDIAFgPKNL-GLSEEEAEERVKEAleLVGLD-EEYLERSPFELSGGQMRRVAI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 154 ARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHSNID-ASYAERVIFIKDGRL 219
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGlTVILVTHSMEDvAEYADRVIVMHKGKI 221
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-224 |
3.08e-48 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 163.19 E-value: 3.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskaly 81
Cdd:PRK09452 14 LVELRGISKSFD----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 rQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:PRK09452 85 -NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 162 TILLADEPTGALDSKTSKTLMMlfqEIHQLEQ----TILMVTHSNIDA-SYAERVIFIKDGRLYH-----EIY 224
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQN---ELKALQRklgiTFVFVTHDQEEAlTMSDRIVVMRDGRIEQdgtprEIY 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-220 |
3.85e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 158.76 E-value: 3.85e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglnaTTALNqMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmKNESKALYR 82
Cdd:COG3840 2 LRLDDLTYRYG-----DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG------QDLTALPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENI---MMP-LILAGAKRkdieQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALV 158
Cdd:COG3840 70 ERPVSMLFQENNLFPHLTVAQNIglgLRPgLKLTAEQR----AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 159 TKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHSNIDA-SYAERVIFIKDGRLY 220
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGlTVLMVTHDPEDAaRIADRVLLVADGRIA 209
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-219 |
3.87e-48 |
|
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: 158.82 E-value: 3.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLNNMKNESKA 79
Cdd:cd03261 1 IELRGLTKSFGG----RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIV---GLlrpDSGEVLIDGEDISGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYRQQMvGFVFQDFNLLPTMTNKENIMMPLILAGA-KRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALV 158
Cdd:cd03261 74 RLRRRM-GMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 159 TKPTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHsNIDASY--AERVIFIKDGRL 219
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTH-DLDTAFaiADRIAVLYDGKI 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
3-219 |
5.47e-48 |
|
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: 159.73 E-value: 5.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYG--------------------KGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGD 62
Cdd:cd03294 1 IKIKGLYKIFGknpqkafkllakgkskeeilKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 63 IIVDGAHLNNM-KNESKALYRQQMvGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPS 141
Cdd:cd03294 81 VLIDGQDIAAMsRKELRELRRKKI-SMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 142 EISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:cd03294 160 ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEAlRLGDRIAIMKDGRL 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-217 |
7.11e-47 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 159.09 E-value: 7.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmKNESKAL 80
Cdd:PRK10851 1 MSIEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG------TDVSRLH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQQMVGFVFQDFNLLPTMTNKENIMMPL-ILAGAKRKD---IEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARA 156
Cdd:PRK10851 71 ARDRKVGFVFQHYALFRHMTVFDNIAFGLtVLPRRERPNaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 157 LVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNIDA-SYAERVIFIKDG 217
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEeLKFTSVFVTHDQEEAmEVADRVVVMSQG 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2-227 |
1.76e-46 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 154.26 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYgkgLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALY 81
Cdd:PRK10908 1 MIRFEHVSKAY---LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVhqlTVQLHLEGFLNK---YPSEISGGQKQRIAIARALV 158
Cdd:PRK10908 78 RRQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRV---SAALDKVGLLDKaknFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 159 TKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGRLyHEIYRGE 227
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDiGLISRRSYRMLTLSDGHL-HGGVGGE 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
2.36e-46 |
|
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: 151.65 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNmknESKALYRQQmVGFVFQDFNLLPTMTN 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD---DERKSLRKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 102 KENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLN----KYPSEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
14-219 |
4.31e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 154.14 E-value: 4.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 14 KGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLL---NLIASFDG--LTEGDIIVDGA-HLNNMKNESKALyRQQmVG 87
Cdd:PRK11264 11 KKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLLEQPEAgtIRVGDITIDTArSLSQQKGLIRQL-RQH-VG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 88 FVFQDFNLLPTMTNKENIMM-PLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLA 166
Cdd:PRK11264 89 FVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 487401142 167 DEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:PRK11264 169 DEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRI 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-218 |
1.03e-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: 150.61 E-value: 1.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalYR 82
Cdd:cd03228 1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLES---LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDFNLLpTMTNKENImmplilagakrkdieqrvhqltvqlhlegflnkypseISGGQKQRIAIARALVTKPT 162
Cdd:cd03228 76 KN-IAYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGR 218
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
3-221 |
1.34e-45 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 151.68 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNATTALNqmnlsvgaGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYR 82
Cdd:cd03297 2 LCVDIEKRLPDFTLKIDFDLN--------EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMmpLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03297 74 QRKIGLVFQQYALFPHLNVRENLA--FGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNIDASY-AERVIFIKDGRLYH 221
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQIKKnLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQY 212
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-222 |
8.12e-45 |
|
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: 150.96 E-value: 8.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKneSKALY 81
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS--RRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQqmVGFVFQDFNLLPTMTNKENIMM---PLI--LAGAKRKDiEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARA 156
Cdd:COG1120 75 RR--IAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 157 LVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHS-NIDASYAERVIFIKDGRLYHE 222
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGrTVVMVLHDlNLAARYADRLVLLKDGRIVAQ 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-219 |
3.22e-44 |
|
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: 146.77 E-value: 3.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKalyr 82
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qQMVGFVFQDFNLLPTMTNKENIMMplilagakrkdieqrvhqltvqlhlegflnkypseiSGGQKQRIAIARALVTKPT 162
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-222 |
5.08e-44 |
|
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: 149.12 E-value: 5.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIasfDGL---TEGDIIVDGahlNNMKNESKA 79
Cdd:TIGR04520 1 IEVENVSFSYPES--EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLL---NGLllpTSGKVTVDG---LDTLDEENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYRQQMVGFVFQD---------------FNLlptmtnkENIMMPlilagakRKDIEQRVHQLTVQLHLEGFLNKYPSEIS 144
Cdd:TIGR04520 73 WEIRKKVGMVFQNpdnqfvgatveddvaFGL-------ENLGVP-------REEMRKRVDEALKLVGMEDFRDREPHLLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 145 GGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHsNID-ASYAERVIFIKDGRLYHE 222
Cdd:TIGR04520 139 GGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGiTVISITH-DMEeAVLADRVIVMNKGKIVAE 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-219 |
8.11e-44 |
|
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: 147.71 E-value: 8.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGL-----TEGDIIVDGAHLNNMKNES 77
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KALYRQqmVGFVFQDFNLLPtMTNKENIMMPLILAG-AKRKDIEQRVHQL--TVQLHLEGFLNKYPSEISGGQKQRIAIA 154
Cdd:cd03260 77 LELRRR--VGMVFQKPNPFP-GSIYDNVAYGLRLHGiKLKEELDERVEEAlrKAALWDEVKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 155 RALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKK-EYTIVIVTH-NMQqaARVADRTAFLLNGRL 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-237 |
1.52e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 147.54 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLNNMKNEs 77
Cdd:COG1121 5 PAIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAIL---GLlppTSGTVRLFGKPPRRARRR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 kalyrqqmVGFVFQDFNLLPT--MTNKENIMMPL-----ILAGAKRKDiEQRVHQLTVQLHLEGFLNKYPSEISGGQKQR 150
Cdd:COG1121 77 --------IGYVPQRAEVDWDfpITVRDVVLMGRygrrgLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 151 IAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDA--SYAERVIFIKDGRLYH----EIY 224
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTH-DLGAvrEYFDRVLLLNRGLVAHgppeEVL 226
|
250
....*....|...
gi 487401142 225 RGEESQLAFQQRI 237
Cdd:COG1121 227 TPENLSRAYGGPV 239
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-219 |
2.77e-43 |
|
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: 149.18 E-value: 2.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 37 IMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyrqqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKR 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH------INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 117 KDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTI 195
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeQLGITF 154
|
170 180
....*....|....*....|....*
gi 487401142 196 LMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGKI 179
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
24-222 |
3.66e-43 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 145.88 E-value: 3.66e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 24 QMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmKNESKALYRQQMVGFVFQDFNLLPTMTNKE 103
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPPSRRPVSMLFQENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 104 NImmPLILAGAKRKDIEQR--VHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTL 181
Cdd:PRK10771 91 NI--GLGLNPGLKLNAAQRekLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487401142 182 MMLFQEIHQLEQ-TILMVTHSNIDAS-YAERVIFIKDGRLYHE 222
Cdd:PRK10771 169 LTLVSQVCQERQlTLLMVSHSLEDAArIAPRSLVVADGRIAWD 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
27-219 |
9.76e-43 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 144.17 E-value: 9.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 27 LSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyrqqmVGFVFQDFNLLPTMTNKENIM 106
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 107 MPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQ 186
Cdd:cd03298 93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190
....*....|....*....|....*....|....*
gi 487401142 187 EIHQLEQ-TILMVTHSNIDASY-AERVIFIKDGRL 219
Cdd:cd03298 173 DLHAETKmTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
1.03e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 145.16 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAH--LNNMKNESK 78
Cdd:COG4161 1 MSIQLKNINCFYGS----HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPSEKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQQMVGFVFQDFNLLPTMTNKEN-IMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARAL 157
Cdd:COG4161 77 IRLLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 158 VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGRL 219
Cdd:COG4161 157 MMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEvEFARKVASQVVYMEKGRI 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-218 |
4.82e-42 |
|
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: 149.83 E-value: 4.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVY-------GKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTL----LNLIASfdgltEGDIIVDGAHL 70
Cdd:COG4172 275 LLEARDLKVWFpikrglfRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 71 NNMKneSKAL--YRQQM-VgfVFQD-FNLL-PTMTNKENIMMPLIL--AGAKRKDIEQRVHQLTVQLHL-EGFLNKYPSE 142
Cdd:COG4172 350 DGLS--RRALrpLRRRMqV--VFQDpFGSLsPRMTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 143 ISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEI---HQLeqTILMVTHsniD----ASYAERVIFIK 215
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLqreHGL--AYLFISH---DlavvRALAHRVMVMK 500
|
...
gi 487401142 216 DGR 218
Cdd:COG4172 501 DGK 503
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-219 |
1.26e-41 |
|
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: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMkneSKALYR 82
Cdd:COG2274 474 IELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI---DPASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDFNLLPTmTNKENIMMplilaGAKRKDIEqRVHQLTVQLHLEGFLNKYP-----------SEISGGQKQRI 151
Cdd:COG2274 549 RQ-IGVVLQDVFLFSG-TIRENITL-----GDPDATDE-EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 152 AIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRLADRIIVLDKGRI 687
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-219 |
1.53e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 142.08 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLN--NMKNESK 78
Cdd:PRK11124 1 MSIQLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfsKTPSDKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQQMVGFVFQDFNLLPTMTNKEN-IMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARAL 157
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 158 VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGRL 219
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEvEVARKTASRVVYMENGHI 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-241 |
1.61e-41 |
|
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: 141.92 E-value: 1.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGlnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskalY 81
Cdd:COG4555 1 MIEVENLSKKYGKV----PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE----A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMvGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:COG4555 73 RRQI-GVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNID-ASYAERVIFIKDGRLyheIYRGEESQLAfQQRITDS 240
Cdd:COG4555 152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEvEALCDRVVILHKGKV---VAQGSLDELR-EEIGEEN 227
|
.
gi 487401142 241 L 241
Cdd:COG4555 228 L 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-219 |
2.19e-41 |
|
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: 148.75 E-value: 2.19e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalyR 82
Cdd:COG4988 337 IELEDVSFSYPGG---RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPAS----W 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDfNLLPTMTNKENIMMplilagAKRKDIEQRVHQLTVQLHLEGFLNKYP-----------SEISGGQKQRI 151
Cdd:COG4988 410 RRQIAWVPQN-PYLFAGTIRENLRL------GRPDASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 152 AIARALVTKPTILLADEPTGALDSKTSKTLMmlfQEIHQL--EQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEIL---QALRRLakGRTVILITHRLALLAQADRILVLDDGRI 549
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-174 |
2.20e-41 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 144.10 E-value: 2.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVY--GKGLNATT-----ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMK 74
Cdd:COG4608 7 LLEVRDLKKHFpvRGGLFGRTvgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 75 NESKALYRQ--QMVgfvFQD----FNllPTMTNKENIMMPLILAG-AKRKDIEQRVHQL--TVQLHLEgFLNKYPSEISG 145
Cdd:COG4608 87 GRELRPLRRrmQMV---FQDpyasLN--PRMTVGDIIAEPLRIHGlASKAERRERVAELleLVGLRPE-HADRYPHEFSG 160
|
170 180
....*....|....*....|....*....
gi 487401142 146 GQKQRIAIARALVTKPTILLADEPTGALD 174
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-228 |
2.35e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 142.15 E-value: 2.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGL-NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKnESKaly 81
Cdd:COG1101 2 LELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDfNLL---PTMTNKENimmpLILA-----------GAKRKDIEQRVHQL-TVQLHLEGFLNKYPSEISGG 146
Cdd:COG1101 78 RAKYIGRVFQD-PMMgtaPSMTIEEN----LALAyrrgkrrglrrGLTKKRRELFRELLaTLGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 147 QKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEI---HQLeqTILMVTHSNIDA-SYAERVIFIKDGRLYHE 222
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveeNNL--TTLMVTHNMEQAlDYGNRLIMMHEGRIILD 230
|
....*.
gi 487401142 223 IyRGEE 228
Cdd:COG1101 231 V-SGEE 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
3-219 |
8.75e-41 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 140.58 E-value: 8.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKalyr 82
Cdd:PRK11247 13 LLLNAVSKRYG----ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qqmvgFVFQDFNLLPTMTNKENIMMPLilagakRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:PRK11247 85 -----LMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLfqeIHQLEQ----TILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:PRK11247 154 LLLLDEPLGALDALTRIEMQDL---IESLWQqhgfTVLLVTHDVSEAvAMADRVLLIEEGKI 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-221 |
1.80e-40 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 142.86 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 6 KHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyrqqm 85
Cdd:PRK11000 7 RNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 86 VGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILL 165
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 166 ADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNIDA-SYAERVIFIKDGR---------LYH 221
Cdd:PRK11000 157 LDEPLSNLDAALRVQMRIEISRLHKrLGRTMIYVTHDQVEAmTLADKIVVLDAGRvaqvgkpleLYH 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-217 |
6.65e-40 |
|
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: 137.60 E-value: 6.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskalyrqQMVgfVFQDFNLLPTMTN 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD-------RMV--VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 KENIMMPL--ILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSK 179
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487401142 180 TLM-MLFQEIHQLEQTILMVTHsNIDAS--YAERVIFIKDG 217
Cdd:TIGR01184 152 NLQeELMQIWEEHRVTVLMVTH-DVDEAllLSDRVVMLTNG 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-222 |
9.95e-40 |
|
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: 135.64 E-value: 9.95e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyrq 83
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 84 QMVGFVFQdfnllptmtnkenimmplILAgakrkdieqrvhqltvQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTI 163
Cdd:cd03214 73 RKIAYVPQ------------------ALE----------------LLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 164 LLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHS-NIDASYAERVIFIKDGRLYHE 222
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRLaRERGKTVVMVLHDlNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-221 |
1.82e-39 |
|
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: 136.10 E-value: 1.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlNNMKNESKALYr 82
Cdd:cd03263 1 LQIRNLTKTYKKGTK--PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING---YSIRTDRKAAR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03263 75 -QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIhQLEQTILMVTHSNIDASY-AERVIFIKDGRLYH 221
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRC 212
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-218 |
2.11e-39 |
|
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: 133.91 E-value: 2.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKGlnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskaLYRQ 83
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE---ELRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 84 QmVGFVFQdfnllptmtnkenimmplilagakrkdieqrvhqltvqlhlegflnkypseISGGQKQRIAIARALVTKPTI 163
Cdd:cd00267 74 R-IGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 164 LLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDAS-YAERVIFIKDGR 218
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAElAADRVIVLKDGK 157
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-219 |
2.17e-39 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 135.76 E-value: 2.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 26 NLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmKNESKALYRQQMVGFVFQDFNLLPTMTNKENI 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVND------QSHTGLAPYQRPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 106 MMPLiLAGAKRKDIEQ-RVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMML 184
Cdd:TIGR01277 92 GLGL-HPGLKLNAEQQeKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190
....*....|....*....|....*....|....*..
gi 487401142 185 FQEIHQLEQ-TILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:TIGR01277 171 VKQLCSERQrTLLMVTHHLSDArAIASQIAVVSQGKI 207
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2-224 |
2.83e-39 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 139.97 E-value: 2.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYgkglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNeskaly 81
Cdd:PRK11607 19 LLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIhqLEQ---TILMVTHSNIDA-SYAERVIFIKDGRLYH-----EIY 224
Cdd:PRK11607 169 KLLLLDEPMGALDKKLRDRMQLEVVDI--LERvgvTCVMVTHDQEEAmTMAGRIAIMNRGKFVQigepeEIY 238
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-225 |
3.57e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 139.08 E-value: 3.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmKNESKALYR 82
Cdd:PRK11432 7 VVLKNITKRFGS----NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG------EDVTHRSIQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:PRK11432 77 QRDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHSNIDA-SYAERVIFIKDGRLYH-----EIYR 225
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRELQQqFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMQigspqELYR 226
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2-200 |
6.87e-39 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 135.60 E-value: 6.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkaly 81
Cdd:PRK11248 1 MLQISHLYADYG----GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 rqqmvGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 487401142 162 TILLADEPTGALDSKTSKTLM-MLFQEIHQLEQTILMVTH 200
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQtLLLKLWQETGKQVLLITH 187
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-221 |
7.47e-39 |
|
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: 134.20 E-value: 7.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 15 GLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNeskalyrqqMVGFVFQDFN 94
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK---------RIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 95 LLPTM--TNKENIMMPL-----ILAGAKRKDiEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLAD 167
Cdd:cd03235 79 IDRDFpiSVRDVVLMGLyghkgLFRRLSKAD-KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 168 EPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDAS--YAERVIFIKDGRLYH 221
Cdd:cd03235 158 EPFAGVDPKTQEDIYELLRELRREGMTILVVTH-DLGLVleYFDRVLLLNRTVVAS 212
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-218 |
2.00e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 135.56 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKGLN-ATTALNQMNLSVGAGEFVAIMGESGSGKSTLlnlIASFDGL---TEGDIIVDGAHLNNMKNE 76
Cdd:PRK13637 1 MSIKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTL---IQHLNGLlkpTSGKIIIDGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SKALYRQqmVGFVFQ--DFNLLPTMTNKENIMMPLILaGAKRKDIEQRVHQL--TVQLHLEGFLNKYPSEISGGQKQRIA 152
Cdd:PRK13637 78 LSDIRKK--VGLVFQypEYQLFEETIEKDIAFGPINL-GLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 153 IARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHSNID-ASYAERVIFIKDGR 218
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHkEYNMTIILVSHSMEDvAKLADRIIVMNKGK 222
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-219 |
2.14e-38 |
|
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: 133.72 E-value: 2.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkGLnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyr 82
Cdd:cd03219 1 LEVRGLTKRFG-GL---VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAG----------AKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIA 152
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAAQARTgsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 153 IARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDA--SYAERVIFIKDGRL 219
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEH-DMDVvmSLADRVTVLDQGRV 221
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-218 |
5.42e-38 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 136.00 E-value: 5.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 24 QMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLT---EGDIIVDGAHL-NNMKNESKALYRQQmVGFVFQDFNLLPTM 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIA---GLErpdSGRIRLGGEVLqDSARGIFLPPHRRR-IGYVFQEARLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENImmpliLAGAKRKDIEQR---VHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSK 176
Cdd:COG4148 93 SVRGNL-----LYGRKRAPRAERrisFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487401142 177 TSKTLMMLFQEIHQ-LEQTILMVTHSnID--ASYAERVIFIKDGR 218
Cdd:COG4148 168 RKAEILPYLERLRDeLDIPILYVSHS-LDevARLADHVVLLEQGR 211
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
3-225 |
1.26e-37 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 138.76 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalYR 82
Cdd:COG1132 340 IEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLES---LR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDFNLLpTMTNKENIMMplilaGakRKDI-EQRVHQLTVQLHLEGFLNKYP-----------SEISGGQKQR 150
Cdd:COG1132 414 RQ-IGVVPQDTFLF-SGTIRENIRY-----G--RPDAtDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 151 IAIARALVTKPTILLADEPTGALDSKTSKtlmMLFQEIHQLEQ--TILMVTH--SNIDAsyAERVIFIKDGR-------- 218
Cdd:COG1132 485 IAIARALLKDPPILILDEATSALDTETEA---LIQEALERLMKgrTTIVIAHrlSTIRN--ADRILVLDDGRiveqgthe 559
|
250
....*....|....
gi 487401142 219 -------LYHEIYR 225
Cdd:COG1132 560 ellarggLYARLYR 573
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
16-212 |
4.97e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 129.52 E-value: 4.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 16 LNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASF--DGLT-EGDIIVDGAHLNNMKNESKAlyrqqmVGFVFQD 92
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTlsPAFSaSGEVLLNGRRLTALPAEQRR------IGILFQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 93 FNLLPTMTNKENIM--MPLILAGAKRKdieQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:COG4136 85 DLLFPHLSVGENLAfaLPPTIGRAQRR---ARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487401142 171 GALDSK-TSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVI 212
Cdd:COG4136 162 SKLDAAlRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
3-218 |
9.45e-37 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 132.66 E-value: 9.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNeskalyR 82
Cdd:PRK11650 4 LKLQAVRKSYD---GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:PRK11650 75 DRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 163 ILLADEPTGALDSKtsktL---MMLfqEIHQLEQ----TILMVTHSNIDA-SYAERVIFIKDGR 218
Cdd:PRK11650 155 VFLFDEPLSNLDAK----LrvqMRL--EIQRLHRrlktTSLYVTHDQVEAmTLADRVVVMNGGV 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-219 |
9.60e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 130.16 E-value: 9.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGkGLnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKneSKAL 80
Cdd:COG0411 3 PLLEVRGLTKRFG-GL---VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP--PHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQqmvGFV--FQDFNLLPTMTNKENIMM---------------PLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEI 143
Cdd:COG0411 77 ARL---GIArtFQNPRLFPELTVLENVLVaaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 144 SGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHsNIDA--SYAERVIFIKDGRL 219
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGiTILLIEH-DMDLvmGLADRIVVLDFGRV 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-219 |
3.15e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 134.51 E-value: 3.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalyR 82
Cdd:COG4987 334 LELEDVSFRYPGA--GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDD----L 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQD---FNllptMTNKENimmpLILAgakRKDI-EQRVHQLTVQLHLEGFLNKYP-----------SEISGGQ 147
Cdd:COG4987 408 RRRIAVVPQRphlFD----TTLREN----LRLA---RPDAtDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 148 KQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLERMDRILVLEDGRI 547
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-211 |
3.26e-36 |
|
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: 127.21 E-value: 3.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnmknESKAL 80
Cdd:COG4133 1 MMLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR----DARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQQMvGFVFQDFNLLPTMTNKENIMMpliLAGAKRKDI-EQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVT 159
Cdd:COG4133 73 YRRRL-AYLGHADGLKPELTVRENLRF---WAALYGLRAdREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 487401142 160 KPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERV 211
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVL 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
26-219 |
6.56e-36 |
|
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: 130.62 E-value: 6.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 26 NLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYRQQMVGFVFQDFNLLPTMTNKENI 105
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 106 mmpliLAGAKRKDIEQRV---HQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLM 182
Cdd:TIGR02142 97 -----RYGMKRARPSERRisfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 487401142 183 MLFQEIHQ-LEQTILMVTHSnID--ASYAERVIFIKDGRL 219
Cdd:TIGR02142 172 PYLERLHAeFGIPILYVSHS-LQevLRLADRVVVLEDGRV 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-222 |
1.19e-35 |
|
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: 126.15 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLnattALNQMNLSVGAGEFvAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskalYR 82
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QqMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03264 72 R-RIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTH--SNIDASyAERVIFIKDGRLYHE 222
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHivEDVESL-CNQVAVLNKGKLVFE 210
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-218 |
3.96e-35 |
|
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: 125.34 E-value: 3.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalYRQQMvGFVFQDFNLLPTmTN 101
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRW---LRSQI-GLVSQEPVLFDG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 KENIMmpLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEI-------SGGQKQRIAIARALVTKPTILLADEPTGALD 174
Cdd:cd03249 94 AENIR--YGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVgergsqlSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487401142 175 SKTSKtlmmLFQEihQLEQ-----TILMVTH--SNIdaSYAERVIFIKDGR 218
Cdd:cd03249 172 AESEK----LVQE--ALDRamkgrTTIVIAHrlSTI--RNADLIAVLQNGQ 214
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
3-218 |
9.15e-35 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 124.91 E-value: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYG-----KGLNattalnqmnLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNES 77
Cdd:COG4598 9 LEVRDLHKSFGdlevlKGVS---------LTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KALY---RQQM------VGFVFQDFNLLPTMTNKENIMM-PLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQ 147
Cdd:COG4598 80 GELVpadRRQLqrirtrLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 148 KQRIAIARALVTKPTILLADEPTGALDSKtsktlmmLFQE----IHQLEQ---TILMVTHsniDASYA----ERVIFIKD 216
Cdd:COG4598 160 QQRAAIARALAMEPEVMLFDEPTSALDPE-------LVGEvlkvMRDLAEegrTMLVVTH---EMGFArdvsSHVVFLHQ 229
|
..
gi 487401142 217 GR 218
Cdd:COG4598 230 GR 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-219 |
1.04e-34 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 124.76 E-value: 1.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLL---N----LIASFDglTEGDIIVDGAHLNNMKN 75
Cdd:COG1117 12 IEVRNLNVYYGD----KQALKDINLDIPENKVTALIGPSGCGKSTLLrclNrmndLIPGAR--VEGEILLDGEDIYDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 76 ESKALYRQqmVGFVFQDFNLLPtMTNKENIMMPLILAGAK-RKDIEQRVHQLTVQLHL----EGFLNKYPSEISGGQKQR 150
Cdd:COG1117 86 DVVELRRR--VGMVFQKPNPFP-KSIYDNVAYGLRLHGIKsKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 151 IAIARALVTKPTILLADEPTGALDSKTSKTLMMLfqeIHQLEQ--TILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:COG1117 163 LCIARALAVEPEVLLMDEPTSALDPISTAKIEEL---ILELKKdyTIVIVTH-NMQqaARVSDYTAFFYLGEL 231
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-219 |
1.15e-34 |
|
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: 129.80 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKS----TLLNLIASFDGLTEGDIIVDGAHLNNMKNES 77
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KALYRQQMVGFVFQD----FNllPTMTNKENIMMPLIL-AGAKRKDIEQRVHQLtvqLHLEGF------LNKYPSEISGG 146
Cdd:COG4172 86 LRRIRGNRIAMIFQEpmtsLN--PLHTIGKQIAEVLRLhRGLSGAAARARALEL---LERVGIpdperrLDAYPHQLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 147 QKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHS-NIDASYAERVIFIKDGRL 219
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
3-222 |
1.91e-34 |
|
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: 123.31 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyr 82
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPL-ILAGAKRKDIEQRVHQLTVQLHlEgFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:cd03224 74 RAGIGYVPEGRRIFPELTVEENLLLGAyARRRAKRKARLERVYELFPRLK-E-RRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDA--SYAERVIFIKDGRLYHE 222
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQ-NARFalEIADRAYVLERGRVVLE 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-226 |
2.10e-33 |
|
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: 119.58 E-value: 2.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAS--FDGLTEGDIIVDGahlnnmKNESKALYRQQMvGFVFQDFNLLPTM 99
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLING------RPLDKRSFRKII-GYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENIMMplilagakrkdieqrvhqltvQLHLEGflnkypseISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSK 179
Cdd:cd03213 98 TVRETLMF---------------------AAKLRG--------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 180 TLMMLFQEIHQLEQTILMVTH--SNIDASYAERVIFIKDGRLyheIYRG 226
Cdd:cd03213 149 QVMSLLRRLADTGRTIICSIHqpSSEIFELFDKLLLLSQGRV---IYFG 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-222 |
3.89e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 121.28 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIasfDGL---TEGDIIVDGAHLNnmknESK 78
Cdd:PRK13635 5 IIRVEHISFRYPD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLL---NGLllpEAGTITVGGMVLS----EET 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQQMVGFVFQD---------------FNLlptmtnkENIMMPlilagakRKDIEQRVHQLTVQLHLEGFLNKYPSEI 143
Cdd:PRK13635 76 VWDVRRQVGMVFQNpdnqfvgatvqddvaFGL-------ENIGVP-------REEMVERVDQALRQVGMEDFLNREPHRL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 144 SGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMmlfQEIHQLEQ----TILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:PRK13635 142 SGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVL---ETVRQLKEqkgiTVLSITHDLDEAAQADRVIVMNKGEI 218
|
...
gi 487401142 220 YHE 222
Cdd:PRK13635 219 LEE 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2-222 |
5.54e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 120.95 E-value: 5.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLnliASFDGL---TEGDIIVDGAHLnnmKNESK 78
Cdd:PRK13639 1 ILETRDLKYSYPDG---TEALKGINFKAEKGEMVALLGPNGAGKSTLF---LHFNGIlkpTSGEVLIKGEPI---KYDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYR-QQMVGFVFQ---DFNLLPTMtnKENIMM-PLILaGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAI 153
Cdd:PRK13639 72 SLLEvRKTVGIVFQnpdDQLFAPTV--EEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 154 ARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGRLYHE 222
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDvDLVPVYADKVYVMSDGKIIKE 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-226 |
9.77e-33 |
|
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: 118.62 E-value: 9.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKaly 81
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 rqQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:cd03266 78 --RRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNID--ASYAERVIFIKDGRLyheIYRG 226
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTH-IMQevERLCDRVVVLHRGRV---VYEG 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-222 |
1.02e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 120.96 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKGL-NATTALNQMNLSVGAGEFVAIMGESGSGKSTLlnlIASFDGL---TEGDIIVDGAHLNNMKNE 76
Cdd:PRK13651 1 MQIKVKNIVKIFNKKLpTELKALDNVSVEINQGEFIAIIGQTGSGKTTF---IEHLNALllpDTGTIEWIFKDEKNKKKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 S----------------------KALYRQqmVGFVFQ--DFNLLPTmTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHL 132
Cdd:PRK13651 78 KekekvleklviqktrfkkikkiKEIRRR--VGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 133 -EGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDA--SYAE 209
Cdd:PRK13651 155 dESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH-DLDNvlEWTK 233
|
250
....*....|...
gi 487401142 210 RVIFIKDGRLYHE 222
Cdd:PRK13651 234 RTIFFKDGKIIKD 246
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-219 |
1.83e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.59 E-value: 1.83e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnNMKNESKAl 80
Cdd:COG1129 3 PLLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 yRQQMVGFVFQDFNLLPTMTNKENIMMPLILAGA---KRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARAL 157
Cdd:COG1129 77 -QAAGIAIIHQELNLVPNLSVAENIFLGREPRRGgliDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 158 VTKPTILLADEPTGALDSKTSKtlmMLFQEIHQL-EQ--TILMVTH-----SNIdasyAERVIFIKDGRL 219
Cdd:COG1129 156 SRDARVLILDEPTASLTEREVE---RLFRIIRRLkAQgvAIIYISHrldevFEI----ADRVTVLRDGRL 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-218 |
4.20e-32 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 119.83 E-value: 4.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKS----TLLNLIASfDGLTEGDIIVDGAHLNNMKNES 77
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KALYRQQMVGFVFQD--FNLLPTMTNKENIMMPLIL--AGAKRKDIEQRVHQLTVQLHLEGF--LNKYPSEISGGQKQRI 151
Cdd:PRK09473 91 LNKLRAEQISMIFQDpmTSLNPYMRVGEQLMEVLMLhkGMSKAEAFEESVRMLDAVKMPEARkrMKMYPHEFSGGMRQRV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 152 AIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:PRK09473 171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDlGVVAGICDKVLVMYAGR 239
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
3-222 |
6.00e-32 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 117.76 E-value: 6.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNES---KA 79
Cdd:PRK10619 6 LNVIDLHKRYGE----HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYRQQM------VGFVFQDFNLLPTMTNKENIM-MPLILAGAKRKDIEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQRI 151
Cdd:PRK10619 82 ADKNQLrllrtrLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 152 AIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASY-AERVIFIKDGRLYHE 222
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEE 233
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-218 |
1.51e-31 |
|
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: 115.61 E-value: 1.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVY------GKGLnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDgaHLNNMKN 75
Cdd:COG4778 4 LLEVENLSKTFtlhlqgGKRL---PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR--HDGGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 76 ESKA-----LY-RQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHL-EGFLNKYPSEISGGQK 148
Cdd:COG4778 79 LAQAspreiLAlRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 149 QRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsniDASY----AERVIFIKDGR 218
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFH---DEEVreavADRVVDVTPFS 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
14-222 |
1.55e-31 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 116.65 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 14 KGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLTEGDIIVdGAH---LNNMKNESKALYR-----QQM 85
Cdd:PRK09984 12 KTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLS---GLITGDKSA-GSHielLGRTVQREGRLARdirksRAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 86 VGFVFQDFNLLPTMTNKENIMM------PLILAGAK--RKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARAL 157
Cdd:PRK09984 88 TGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 158 VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDAS--YAERVIFIKDGRLYHE 222
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYAlrYCERIVALRQGHVFYD 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-219 |
5.77e-31 |
|
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: 114.22 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnNMKNESKALYRQQmVGFVFQDFNLLpTMT 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT---DIRQLDPADLRRN-IGYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMM--PL-----ILAGAKRKDieqrVHQLtVQLHLEGF---LNKYPSEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:cd03245 94 LRDNITLgaPLadderILRAAELAG----VTDF-VNKHPNGLdlqIGERGRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487401142 171 GALDSKTSktlMMLFQEIHQL--EQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:cd03245 169 SAMDMNSE---ERLKERLRQLlgDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-231 |
6.73e-31 |
|
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: 114.25 E-value: 6.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNAttALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalYR 82
Cdd:cd03251 1 VEFKNVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS---LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMvGFVFQDFNLLPTmTNKENIMMPliLAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEI-------SGGQKQRIAIAR 155
Cdd:cd03251 76 RQI-GLVSQDVFLFND-TVAENIAYG--RPGATREEVEEAARAANAHEFIMELPEGYDTVIgergvklSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 156 ALVTKPTILLADEPTGALDSKTSktlmMLFQE-IHQLEQ--TILMVTH--SNIDAsyAERVIFIKDGRLyheIYRGEESQ 230
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESE----RLVQAaLERLMKnrTTFVIAHrlSTIEN--ADRIVVLEDGKI---VERGTHEE 222
|
.
gi 487401142 231 L 231
Cdd:cd03251 223 L 223
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-218 |
1.78e-30 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 115.74 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 24 QMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLT---EGDIIVDGAHLNNMKNESKALYRQQMVGFVFQDFNLLPTMT 100
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAIS---GLTrpqKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENImmpliLAGAKRKDIEQ--RVHQLtvqLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTS 178
Cdd:PRK11144 93 VRGNL-----RYGMAKSMVAQfdKIVAL---LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 487401142 179 KTLMMLFQEI-HQLEQTILMVTHSnIDA--SYAERVIFIKDGR 218
Cdd:PRK11144 165 RELLPYLERLaREINIPILYVSHS-LDEilRLADRVVVLEQGK 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-231 |
2.10e-30 |
|
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: 113.09 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalYR 82
Cdd:cd03253 1 IEFENVTFAYDPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQD---------FNLL---PTMTNKEnimmplILAGAKRKDIEQRVhqltvqlhlEGFLNKYPSE-------I 143
Cdd:cd03253 75 RA-IGVVPQDtvlfndtigYNIRygrPDATDEE------VIEAAKAAQIHDKI---------MRFPDGYDTIvgerglkL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 144 SGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRLyheI 223
Cdd:cd03253 139 SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVNADKIIVLKDGRI---V 214
|
....*...
gi 487401142 224 YRGEESQL 231
Cdd:cd03253 215 ERGTHEEL 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
3-219 |
2.94e-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: 112.58 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlNNMKNESKALYR 82
Cdd:cd03252 1 ITFEHVRFRYKP--DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG---HDLALADPAWLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDfNLLPTMTNKENIM-----MPL--ILAGAKRKDieqrVHQLTVQLHlEGF---LNKYPSEISGGQKQRIA 152
Cdd:cd03252 76 RQ-VGVVLQE-NVLFNRSIRDNIAladpgMSMerVIEAAKLAG----AHDFISELP-EGYdtiVGEQGAGLSGGQRQRIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 153 IARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:cd03252 149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRI 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-219 |
3.77e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 113.67 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTaLNQMNLSVGAGEFVAIMGESGSGKSTLLNLIasfDGLTE---GDIIVDGAHLNnmknESK 78
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI---DGLLEaesGQIIIDGDLLT----EEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQQMVGFVFQD-FNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARAL 157
Cdd:PRK13650 76 VWDIRHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 158 VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQmTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-239 |
3.77e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 113.69 E-value: 3.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNM-KNESKALYRQQmVGFVFQ--DFNLLP 97
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQIRKK-VGLVFQfpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 TMTNKENIMMPLILaGAKRKDIEQRVHQltvQLHL----EGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGAL 173
Cdd:PRK13649 101 ETVLKDVAFGPQNF-GVSQEEAEALARE---KLALvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 174 DSKTSKTLMMLFQEIHQLEQTILMVTHSNID-ASYAERVIFIKDGRL---------YHEIYRGEESQL------AFQQRI 237
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDvANYADFVYVLEKGKLvlsgkpkdiFQDVDFLEEKQLgvpkitKFAQRL 256
|
..
gi 487401142 238 TD 239
Cdd:PRK13649 257 AD 258
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-217 |
5.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.19 E-value: 5.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKGLN-ATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNliaSFDGL---TEGDIIVDGAHLNNMKNE 76
Cdd:PRK13634 1 MDITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQ---HLNGLlqpTSGTVTIGERVITAGKKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SKALYRQQMVGFVFQdF--NLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQRIAI 153
Cdd:PRK13634 78 KKLKPLRKKVGIVFQ-FpeHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 154 ARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHSNID-ASYAERVIFIKDG 217
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHSMEDaARYADQIVVMHKG 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
3-219 |
8.63e-30 |
|
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: 109.61 E-value: 8.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLNNMKnesKA 79
Cdd:cd03246 1 LEVENVSFRYPG--AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIL---GLlrpTSGRVRLDGADISQWD---PN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYRQQmVGFVFQDFNLLPTmTNKENIMmplilagakrkdieqrvhqltvqlhlegflnkypseiSGGQKQRIAIARALVT 159
Cdd:cd03246 73 ELGDH-VGYLPQDDELFSG-SIAENIL-------------------------------------SGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 160 KPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-212 |
1.05e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 116.23 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMknESKALYR 82
Cdd:TIGR02857 322 LEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA--DADSWRD 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QqmVGFVFQdfnlLPTMTN---KENIMmpLILAGAKRKDIEQRVHQLTVQ-------LHLEGFLNKYPSEISGGQKQRIA 152
Cdd:TIGR02857 397 Q--IAWVPQ----HPFLFAgtiAENIR--LARPDASDAEIREALERAGLDefvaalpQGLDTPIGEGGAGLSGGQAQRLA 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 153 IARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVI 212
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIV 527
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-200 |
1.05e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.89 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLnNMKNES 77
Cdd:COG3845 4 PALELRGITKRFG----GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILY---GLyqpDSGEILIDGKPV-RIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KAlyRQQMVGFVFQDFNLLPTMTNKENIMM---PLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIA 154
Cdd:COG3845 76 DA--IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEIL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 487401142 155 RALVTKPTILLADEPTGAL-----DSktsktlmmLFQEIHQL-EQ--TILMVTH 200
Cdd:COG3845 154 KALYRGARILILDEPTAVLtpqeaDE--------LFEILRRLaAEgkSIIFITH 199
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-217 |
1.26e-29 |
|
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: 110.04 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmkNESKALYRQ 83
Cdd:cd03226 1 RIENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG-------KPIKAKERR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 84 QMVGFVFQDFNL-LPTMTNKENIMMPLILAGAKRKDIEqrvHQLTvQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03226 71 KSIGYVMQDVDYqLFTDSVREELLLGLKELDAGNEQAE---TVLK-DLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH-SNIDASYAERVIFIKDG 217
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHdYEFLAKVCDRVLLLANG 202
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-217 |
1.38e-29 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 111.47 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKK--VYGKGL---NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNE 76
Cdd:COG4167 4 LLEVRNLSKtfKYRTGLfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 skalYRQQMVGFVFQDFN--LLPTMTNKENIMMPLILAgaKRKDIEQRVHQLTVQLHLEGFL----NKYPSEISGGQKQR 150
Cdd:COG4167 84 ----YRCKHIRMIFQDPNtsLNPRLNIGQILEEPLRLN--TDLTAEEREERIFATLRLVGLLpehaNFYPHMLSSGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 151 IAIARALVTKPTILLADEPTGALD-SKTSKT--LMMLFQEIHQLeqTILMVTHS-NIDASYAERVIFIKDG 217
Cdd:COG4167 158 VALARALILQPKIIIADEALAALDmSVRSQIinLMLELQEKLGI--SYIYVSQHlGIVKHISDKVLVMHQG 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
19-219 |
1.57e-29 |
|
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: 116.50 E-value: 1.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 19 TTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMkneSKALYRQQmVGFVFQDFNLLpT 98
Cdd:TIGR03375 478 TPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI---DPADLRRN-IGYVPQDPRLF-Y 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 99 MTNKENIMM--PL-----ILAGAKRKDieqrVHQLtVQLHLEGF---LNKYPSEISGGQKQRIAIARALVTKPTILLADE 168
Cdd:TIGR03375 553 GTLRDNIALgaPYaddeeILRAAELAG----VTEF-VRRHPDGLdmqIGERGRSLSGGQRQAVALARALLRDPPILLLDE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 169 PTGALDSKTSKTLmmlfqeIHQLEQ-----TILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:TIGR03375 628 PTSAMDNRSEERF------KDRLKRwlagkTLVLVTHRTSLLDLVDRIIVMDNGRI 677
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-219 |
1.80e-29 |
|
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: 110.39 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlNNMKNESKALYRqQMVGFVFQDFNLLPTmT 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDG---IDIRDISRKSLR-SMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMM--PLilagAKRKDIE---QRVHQLTVQLHLEGFLNKYPSE----ISGGQKQRIAIARALVTKPTILLADEPTG 171
Cdd:cd03254 93 IMENIRLgrPN----ATDEEVIeaaKEAGAHDFIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487401142 172 ALDSKTSKTLMMLFQEIHQlEQTILMVTH--SNIdaSYAERVIFIKDGRL 219
Cdd:cd03254 169 NIDTETEKLIQEALEKLMK-GRTSIIIAHrlSTI--KNADKILVLDDGKI 215
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-219 |
2.27e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 111.84 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKGLN-ATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNliaSFDGL---TEGDIIVDGAHLNnMKNE 76
Cdd:PRK13641 1 MSIKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQ---HFNALlkpSSGTITIAGYHIT-PETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SKALYR-QQMVGFVFQdF--NLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQRIA 152
Cdd:PRK13641 77 NKNLKKlRKKVSLVFQ-FpeAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 153 IARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:PRK13641 156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH-NMDdvAEYADDVLVLEHGKL 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-219 |
2.56e-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: 107.90 E-value: 2.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmkneskalyr 82
Cdd:cd03216 1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qQMVGFvfqdfnllptmtnkenimmpLILAGAKRKDIEqRVHQLtvqlhlegflnkypseiSGGQKQRIAIARALVTKPT 162
Cdd:cd03216 62 -KEVSF--------------------ASPRDARRAGIA-MVYQL-----------------SVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 163 ILLADEPTGALDSKTSKtlmMLFQEIHQLEQ---TILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:cd03216 103 LLILDEPTAALTPAEVE---RLFKVIRRLRAqgvAVIFISH-RLDevFEIADRVTVLRDGRV 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-219 |
3.33e-29 |
|
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: 109.38 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlNNMKNESKALYR 82
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPREVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03265 74 R--IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 163 ILLADEPTGALDSKTSktlMMLFQEIHQLEQ----TILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:cd03265 152 VLFLDEPTIGLDPQTR---AHVWEYIEKLKEefgmTILLTTHYMEEAeQLCDRVAIIDHGRI 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
22-200 |
4.12e-29 |
|
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: 109.28 E-value: 4.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIA---SFDGLTEGDIIVDGahlnnmknesKALYRQQM---VGFVFQDFNL 95
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNG----------QPRKPDQFqkcVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 LPTMTNKENIMMPLILAGAKRKDIEQRVHQLTV----QLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTG 171
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVEDvllrDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180
....*....|....*....|....*....
gi 487401142 172 ALDSKTSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
4-219 |
4.24e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 110.47 E-value: 4.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKGLNatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLN--NMKneskalY 81
Cdd:PRK13632 9 KVENVSFSYPNSEN--NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISkeNLK------E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQD---------------FNLlptmtnkENIMMPlilagakRKDIEQRVHQLTVQLHLEGFLNKYPSEISGG 146
Cdd:PRK13632 81 IRKKIGIIFQNpdnqfigatveddiaFGL-------ENKKVP-------PKKMKDIIDDLAKKVGMEDYLDKEPQNLSGG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 147 QKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAILADKVIVFSEGKL 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-212 |
1.02e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 108.26 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVkkvyGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkal 80
Cdd:PRK10247 6 PLLQLQNV----GYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQQmVGFVFQDfnllPTM---TNKENIMMPLILAGaKRKDiEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQRIAIARA 156
Cdd:PRK10247 79 YRQQ-VSYCAQT----PTLfgdTVYDNLIFPWQIRN-QQPD-PAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRN 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 157 LVTKPTILLADEPTGALDSKTSKTLMMLfqeIHQL--EQTI--LMVTHSNIDASYAERVI 212
Cdd:PRK10247 152 LQFMPKVLLLDEITSALDESNKHNVNEI---IHRYvrEQNIavLWVTHDKDEINHADKVI 208
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-222 |
1.41e-28 |
|
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: 108.15 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAl 80
Cdd:COG0410 2 PMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 yrQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAK---RKDIE----------QRVHQLTVQLhlegflnkypseiSGGQ 147
Cdd:COG0410 77 --RLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRaevRADLErvyelfprlkERRRQRAGTL-------------SGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 148 KQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDA--SYAERVIFIKDGRLYHE 222
Cdd:COG0410 142 QQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQ-NARFalEIADRAYVLERGRIVLE 217
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-227 |
1.52e-28 |
|
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: 109.12 E-value: 1.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGL-----NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNE 76
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGlfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SKALYRQQmVGFVFQD----FNllPTMTNKENIMMPLI-LAGAKRKDIEQRVHQLTVQLHLEG-FLNKYPSEISGGQKQR 150
Cdd:TIGR02769 82 QRRAFRRD-VQLVFQDspsaVN--PRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 151 IAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQT-ILMVTHS-NIDASYAERVIFIKDGRLYHEIYRGE 227
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTaYLFITHDlRLVQSFCQRVAVMDKGQIVEECDVAQ 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
3-219 |
2.40e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 110.89 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYG-----------KGLNATTALNQMNLSVGA---------GEFVAIMGESGSGKSTLLNLIASFDGLTEGD 62
Cdd:PRK10070 5 LEIKNLYKIFGehpqrafkyieQGLSKEQILEKTGLSLGVkdaslaieeGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 63 IIVDGAHLNNMKNESKALYRQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSE 142
Cdd:PRK10070 85 VLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 143 ISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTL---MMLFQEIHQleQTILMVTHSNIDA-SYAERVIFIKDGR 218
Cdd:PRK10070 165 LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMqdeLVKLQAKHQ--RTIVFISHDLDEAmRIGDRIAIMQNGE 242
|
.
gi 487401142 219 L 219
Cdd:PRK10070 243 V 243
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-230 |
2.63e-28 |
|
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: 107.23 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyr 82
Cdd:TIGR03410 1 LEVSNLNVYYG----QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHleGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:TIGR03410 74 RAGIAYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFPVLK--EMLGRRGGDLSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 163 ILLADEPT-GALDS---KTSKTLMMLFQEIhqlEQTILMVTHsNID--ASYAERVIFIKDGRLYHEIYRGEESQ 230
Cdd:TIGR03410 152 LLLLDEPTeGIQPSiikDIGRVIRRLRAEG---GMAILLVEQ-YLDfaRELADRYYVMERGRVVASGAGDELDE 221
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-219 |
8.86e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.78 E-value: 8.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGL-----TEGDIIVDGAHLNNMKNE 76
Cdd:PRK14239 5 ILQVSDLSVYYNK----KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLnpevtITGSIVYNGHNIYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SKALYRQqmVGFVFQDFNLLPtMTNKENIMMPLILAGAKRKDI-----EQRVHQLTVQLHLEGFLNKYPSEISGGQKQRI 151
Cdd:PRK14239 81 TVDLRKE--IGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVldeavEKSLKGASIWDEVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 152 AIARALVTKPTILLADEPTGALD----SKTSKTLMMLFQEIhqleqTILMVTHSNIDAS-YAERVIFIKDGRL 219
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDpisaGKIEETLLGLKDDY-----TMLLVTRSMQQASrISDRTGFFLDGDL 225
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-231 |
9.00e-28 |
|
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: 110.96 E-value: 9.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkaLY 81
Cdd:TIGR02203 330 DVEFRNVTFRYPG--RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS--LR 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQqmVGFVFQDFNLLPTmTNKENIMMplilaGAKRKDIEQRVHQLTVQLHLEGFLNKYP-----------SEISGGQKQR 150
Cdd:TIGR02203 406 RQ--VALVSQDVVLFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 151 IAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRLyheIYRGEESQ 230
Cdd:TIGR02203 478 LAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEKADRIVVMDDGRI---VERGTHNE 553
|
.
gi 487401142 231 L 231
Cdd:TIGR02203 554 L 554
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-200 |
1.10e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 106.15 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGL-----TEGDIIVDGAHLNNMkNES 77
Cdd:PRK14247 4 IEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKM-DVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KALYRQQMVgfvFQDFNLLPTMTNKENIMMPLIL--AGAKRKDIEQRVHQLTVQLHL----EGFLNKYPSEISGGQKQRI 151
Cdd:PRK14247 79 ELRRRVQMV---FQIPNPIPNLSIFENVALGLKLnrLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 152 AIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTH 200
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKK-DMTIVLVTH 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1-188 |
1.28e-27 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 107.87 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKkVY-----GKGL-----NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHL 70
Cdd:PRK15079 7 VLLEVADLK-VHfdikdGKQWfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 71 NNMKNESKALYRQ--QMVgfvFQD--FNLLPTMTNKENIMMPLILAGAK--RKDIEQRVHQ--LTVQLhLEGFLNKYPSE 142
Cdd:PRK15079 86 LGMKDDEWRAVRSdiQMI---FQDplASLNPRMTIGEIIAEPLRTYHPKlsRQEVKDRVKAmmLKVGL-LPNLINRYPHE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487401142 143 ISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEI 188
Cdd:PRK15079 162 FSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-226 |
2.04e-27 |
|
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: 104.61 E-value: 2.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlNNMKNESKALYR 82
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKdieqRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03268 74 ---IGALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH--SNIDaSYAERVIFIKDGRLyheIYRG 226
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHllSEIQ-KVADRIGIINKGKL---IEEG 208
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-219 |
3.08e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 105.31 E-value: 3.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 25 MNLSVGAGEFVAIMGESGSGKSTLLNLIASF-----DGLTEGDIIVDGAHLNNMKNESKALYRQqmVGFVFQDFNLLPTM 99
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIEVRRE--VGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENIMMPLILAG--AKRKDIEQRVH----QLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGAL 173
Cdd:PRK14267 101 TIYDNVAIGVKLNGlvKSKKELDERVEwalkKAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487401142 174 DSKTSKTLMMLFQEIHQlEQTILMVTHSNIDAS-YAERVIFIKDGRL 219
Cdd:PRK14267 181 DPVGTAKIEELLFELKK-EYTIVLVTHSPAQAArVSDYVAFLYLGKL 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-191 |
3.33e-27 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 109.02 E-value: 3.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 20 TALNQMNLSVGAGEFVAIMGESGSGKST----LLNLIASfdgltEGDIIVDGAHLNNMKNESKALYRQQMvGFVFQDFN- 94
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVRHRI-QVVFQDPNs 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 95 -LLPTMTNKENIMMPL-----ILAGAKRkdiEQRVHQLTVQLHLEGFL-NKYPSEISGGQKQRIAIARALVTKPTILLAD 167
Cdd:PRK15134 374 sLNPRLNVLQIIEEGLrvhqpTLSAAQR---EQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180
....*....|....*....|....*..
gi 487401142 168 EPTGALDSKTSK---TLMMLFQEIHQL 191
Cdd:PRK15134 451 EPTSSLDKTVQAqilALLKSLQQKHQL 477
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2-201 |
5.70e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.09 E-value: 5.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYG-KGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNliaSFDGL---TEGDI----IVDGAHLNNM 73
Cdd:PRK13631 21 ILRVKNLYCVFDeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVT---HFNGLiksKYGTIqvgdIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 74 KNESKALYRQ--------QMVGFVFQ--DFNLLPTMTNKEnIMMPLILAGAKRKDIEQRVHQLTVQLHL-EGFLNKYPSE 142
Cdd:PRK13631 98 ELITNPYSKKiknfkelrRRVSMVFQfpEYQLFKDTIEKD-IMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 143 ISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS 201
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-218 |
5.96e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.82 E-value: 5.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLnliASFDGL---TEGDIIVDGAHLNnmknESKA 79
Cdd:PRK13647 5 IEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLL---LHLNGIylpQRGRVKVMGREVN----AENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYRQQMVGFVFQD-FNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALV 158
Cdd:PRK13647 75 KWVRSKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 159 TKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDvDLAAEWADQVIVLKEGR 215
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
2-227 |
7.72e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 104.38 E-value: 7.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGK-GLNAT----TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNE 76
Cdd:PRK10419 3 LLNVSGLSHHYAHgGLSGKhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SKALYRQQmVGFVFQD----FNllPTMTNKENIMMPLI-LAGAKRKDIEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQR 150
Cdd:PRK10419 83 QRKAFRRD-IQMVFQDsisaVN--PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 151 IAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHsniDAS----YAERVIFIKDGRLYHEIYR 225
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITH---DLRlverFCQRVMVMDNGQIVETQPV 236
|
..
gi 487401142 226 GE 227
Cdd:PRK10419 237 GD 238
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
32-232 |
1.57e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.44 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 32 GEFVAIMGESGSGKSTLLNLIASFD--GLTEGDIIVdgahLNNMKNESKALyrQQMVGFVFQDFNLLPTMTNKENIM--- 106
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSpkGVKGSGSVL----LNGMPIDAKEM--RAISAYVQQDDLFIPTLTVREHLMfqa 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 107 ---MPLILAGAKRKdieQRVHQLTVQLHLE-------GFLNKYPSeISGGQKQRIAIARALVTKPTILLADEPTGALDSK 176
Cdd:TIGR00955 125 hlrMPRRVTKKEKR---ERVDEVLQALGLRkcantriGVPGRVKG-LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSF 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 177 TSKTLMMLFQEIHQLEQTILMVTH-------SNIDasyaeRVIFIKDGRLyheIYRGEESQLA 232
Cdd:TIGR00955 201 MAYSVVQVLKGLAQKGKTIICTIHqpsselfELFD-----KIILMAEGRV---AYLGSPDQAV 255
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-222 |
1.98e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.71 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKGLN-ATTALNQMNLSVGAGEFVAIMGESGSGKSTLlnlIASFDGL---TEGDIIVDGAHLNNMKNE 76
Cdd:PRK13646 1 MTIRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTL---IQNINALlkpTTGTVTVDDITITHKTKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SKALYRQQMVGFVFQdfnlLPTMTNKENIMMPLILAGAKR-----KDIEQRVHQLTVQLhleGF----LNKYPSEISGGQ 147
Cdd:PRK13646 78 KYIRPVRKRIGMVFQ----FPESQLFEDTVEREIIFGPKNfkmnlDEVKNYAHRLLMDL---GFsrdvMSQSPFQMSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 148 KQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIhQLEQ--TILMVTHSNID-ASYAERVIFIKDGRLYHE 222
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSL-QTDEnkTIILVSHDMNEvARYADEVIVMKEGSIVSQ 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-222 |
2.27e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 103.63 E-value: 2.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 17 NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyrQQMVGFVFQ--DFN 94
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDI---RNKAGMVFQnpDNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 95 LLPTMTNKENIMMPLILaGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALD 174
Cdd:PRK13633 98 IVATIVEEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 175 SKTSKTLMMLFQEIHQLEQ-TILMVTHSNIDASYAERVIFIKDGRLYHE 222
Cdd:PRK13633 177 PSGRREVVNTIKELNKKYGiTIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-219 |
2.80e-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: 100.47 E-value: 2.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskalyR 82
Cdd:cd03247 1 LSINNVSFSYPE--QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTmTNKENIMMPLilagakrkdieqrvhqltvqlhlegflnkypseiSGGQKQRIAIARALVTKPT 162
Cdd:cd03247 74 SSLISVLNQRPYLFDT-TLRNNLGRRF----------------------------------SGGERQRLALARILLQDAP 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEiHQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIFE-VLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-177 |
3.50e-26 |
|
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: 101.85 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyr 82
Cdd:cd03218 1 LRAENLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170
....*....|....*
gi 487401142 163 ILLADEPTGALDSKT 177
Cdd:cd03218 154 FLLLDEPFAGVDPIA 168
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-219 |
3.69e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 103.27 E-value: 3.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 18 ATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYRQQMVGFVFQ--DFNL 95
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 LPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDS 175
Cdd:PRK13643 98 FEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487401142 176 KTSKTLMMLFQEIHQLEQTILMVTHSNID-ASYAERVIFIKDGRL 219
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDvADYADYVYLLEKGHI 222
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-219 |
4.43e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 4.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNAttALNQMNLSVGAGEFVAIMGESGSGKST---LLNLIASFDGLTEGDIIVDGAHLNnmkneSKA 79
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLT-----AKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYR-QQMVGFVFQD-FNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARAL 157
Cdd:PRK13640 79 VWDiREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 158 VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:PRK13640 159 AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVLVLDDGKL 221
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-174 |
5.03e-26 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.51 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVY--GKGLNATT----ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKN 75
Cdd:PRK11308 5 LLQAIDLKKHYpvKRGLFKPErlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 76 ESKALYRQQmVGFVFQD--FNLLPTMTNKENIMMPLI----LAGAKRKdieQRVHQL--TVQLHLEgFLNKYPSEISGGQ 147
Cdd:PRK11308 85 EAQKLLRQK-IQIVFQNpyGSLNPRKKVGQILEEPLLintsLSAAERR---EKALAMmaKVGLRPE-HYDRYPHMFSGGQ 159
|
170 180
....*....|....*....|....*..
gi 487401142 148 KQRIAIARALVTKPTILLADEPTGALD 174
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALD 186
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-235 |
5.26e-26 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 106.08 E-value: 5.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 26 NLSVGAGEFVAIMGESGSGKSTLLNLIASFdgLT-EGDIIVDGAHLNNMkneSKALYRQQmVGFVFQDfNLLPTMTNKEN 104
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF--LPyQGSLKINGIELREL---DPESWRKH-LSWVGQN-PQLPHGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 105 IMMPLILAGakrkdiEQRVHQLTVQLHLEGFLNKYP-----------SEISGGQKQRIAIARALVTKPTILLADEPTGAL 173
Cdd:PRK11174 443 VLLGNPDAS------DEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 174 DSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRLyheIYRGEESQLAFQQ 235
Cdd:PRK11174 517 DAHSEQLVMQALNAASR-RQTTLMVTHQLEDLAQWDQIWVMQDGQI---VQQGDYAELSQAG 574
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-231 |
8.99e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 8.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 16 LNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKN--ESKALYRQQMVGFVFQDF 93
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDifQIDAIKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 94 NLLPTMTNKENIMMPLILAGAK-----RKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADE 168
Cdd:PRK14246 100 NPFPHLSIYDNIAYPLKSHGIKekreiKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 169 PTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDAS-YAERVIFIKDGRLY-----HEIYRGEESQL 231
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKN-EIAIVIVSHNPQQVArVADYVAFLYNGELVewgssNEIFTSPKNEL 247
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-218 |
9.55e-26 |
|
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: 100.05 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmknESKALYR 82
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQmELVEELCDRVLLLNKGR 205
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
18-219 |
2.29e-25 |
|
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: 103.97 E-value: 2.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 18 ATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskalYRQQMVGFVFQDFNLLP 97
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRE----TFGKHIGYLPQDVELFP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 TmTNKENIMM-------PLILAGAKRKDieqrVHQLTVqlhleGFLNKYPSEI-------SGGQKQRIAIARALVTKPTI 163
Cdd:TIGR01842 406 G-TVAENIARfgenadpEKIIEAAKLAG----VHELIL-----RLPDGYDTVIgpggatlSGGQRQRIALARALYGDPKL 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 164 LLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-219 |
2.31e-25 |
|
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: 99.47 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 18 ATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskalYRQQMVGFVFQDfnllp 97
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK----YLHSKVSLVGQE----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 tmtnkenimmPLILAGAKRKDIE--------QRVHQLTVQLHLEGFLNKYPSEI-----------SGGQKQRIAIARALV 158
Cdd:cd03248 97 ----------PVLFARSLQDNIAyglqscsfECVKEAAQKAHAHSFISELASGYdtevgekgsqlSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 159 TKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPE-RRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-169 |
3.21e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.33 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLNNMknes 77
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIV---GLvkpDSGRIFLDGEDITHL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 kALY-RQQM-VGF------VFQDfnllptMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQ 149
Cdd:COG1137 71 -PMHkRARLgIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERR 143
|
170 180
....*....|....*....|
gi 487401142 150 RIAIARALVTKPTILLADEP 169
Cdd:COG1137 144 RVEIARALATNPKFILLDEP 163
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-219 |
5.74e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 103.26 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnmKNESKALYRQqmVGFVFQDfNLLPTMTN 101
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV--QYDHHYLHRQ--VALVGQE-PVLFSGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 KENImmpliLAGAKRKDIEQrVHQLTVQLHLEGFLNKYP-----------SEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:TIGR00958 572 RENI-----AYGLTDTPDEE-IMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 171 GALDSKTSKTlmmLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:TIGR00958 646 SALDAECEQL---LQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-218 |
6.09e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.92 E-value: 6.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKnesKALY 81
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSR---KGLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 R-QQMVGFVFQD-FNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVT 159
Cdd:PRK13636 79 KlRESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 160 KPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:PRK13636 159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDiDIVPLYCDNVFVMKEGR 219
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
21-219 |
1.08e-24 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 102.09 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnNMKNESKALYRQQMvGFVFQDFNLLPTmT 100
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGV---DLRQLDPAELRARM-ALVPQDPVLFAA-S 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMMplilagaKRKDI-EQRVHQLTVQLHLEGFLNKYPS-----------EISGGQKQRIAIARALVTKPTILLADE 168
Cdd:TIGR02204 430 VMENIRY-------GRPDAtDEEVEAAARAAHAHEFISALPEgydtylgergvTLSGGQRQRIAIARAILKDAPILLLDE 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487401142 169 PTGALDSKtSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:TIGR02204 503 ATSALDAE-SEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRI 552
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
15-212 |
1.11e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 15 GLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnnmkneskalyrqQMVGFVFQDFN 94
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG---------------ARVAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 95 LLPTM--TNKENIMM----PLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADE 168
Cdd:NF040873 66 VPDSLplTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 487401142 169 PTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVI 212
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCV 189
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-231 |
1.74e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 101.63 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVY-GKglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkalY 81
Cdd:PRK11176 342 IEFRNVTFTYpGK---EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLAS---L 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQmVGFVFQDFNLL-PTMTNkeNImmplilAGAK-----RKDIEQRVHqltvQLHLEGFLNKYPS-----------EIS 144
Cdd:PRK11176 416 RNQ-VALVSQNVHLFnDTIAN--NI------AYARteqysREQIEEAAR----MAYAMDFINKMDNgldtvigengvLLS 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 145 GGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIhQLEQTILMVTH--SNIDAsyAERVIFIKDGRLyhe 222
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHrlSTIEK--ADEILVVEDGEI--- 556
|
....*....
gi 487401142 223 IYRGEESQL 231
Cdd:PRK11176 557 VERGTHAEL 565
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
20-222 |
1.87e-24 |
|
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: 97.22 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 20 TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmkneskalyrqQMVGFVfqDFN--LLP 97
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------------RVSSLL--GLGggFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 TMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKT 177
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 487401142 178 SKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGRLYHE 222
Cdd:cd03220 178 QEKCQRRLRELLKQGKTVILVSHDpSSIKRLCDRALVLEKGKIRFD 223
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-237 |
2.12e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 101.44 E-value: 2.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMkNESkALyRQQMVgFVFQDFNLLPTmT 100
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADY-SEA-AL-RQAIS-VVSQRVHLFSA-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENimmpLILAGAKRKDiEQRVHQLT-VQL--HLEGF--LNKYPSE----ISGGQKQRIAIARALVTKPTILLADEPTG 171
Cdd:PRK11160 430 LRDN----LLLAAPNASD-EALIEVLQqVGLekLLEDDkgLNAWLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTE 504
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 172 ALDSKTSKTLMMLFQEiHQLEQTILMVTHSNIDASYAERVIFIKDGRLyheIYRGEESQL--------AFQQRI 237
Cdd:PRK11160 505 GLDAETERQILELLAE-HAQNKTVLMITHRLTGLEQFDRICVMDNGQI---IEQGTHQELlaqqgryyQLKQRL 574
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2-222 |
2.63e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.75 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnNMKNESKALY 81
Cdd:PRK13644 1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGI---DTGDFSKLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQ-------------DFNLLPtmtnkENIMMPLIlagakrkDIEQRVHQLTVQLHLEGFLNKYPSEISGGQK 148
Cdd:PRK13644 75 IRKLVGIVFQnpetqfvgrtveeDLAFGP-----ENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 149 QRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDGRLYHE 222
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLE 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2-222 |
4.84e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.47 E-value: 4.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTaLNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnmknESKALY 81
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT----AENVWN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQD-FNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTK 160
Cdd:PRK13642 79 LRRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 161 PTILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTHSNIDASYAERVIFIKDGRLYHE 222
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
3-201 |
7.62e-24 |
|
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: 99.74 E-value: 7.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAlyr 82
Cdd:TIGR02868 335 LELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR--- 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qQMVGFVFQDFNLLPTmTNKENIM----------MPLILAGAKRKD-IEQRVHQLTVQLHLEGflnkypSEISGGQKQRI 151
Cdd:TIGR02868 409 -RRVSVCAQDAHLFDT-TVRENLRlarpdatdeeLWAALERVGLADwLRALPDGLDTVLGEGG------ARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487401142 152 AIARALVTKPTILLADEPTGALDSKTSKTLM-MLFQEIHqlEQTILMVTHS 201
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETADELLeDLLAALS--GRTVVLITHH 529
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-221 |
1.02e-23 |
|
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: 95.54 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEG-DIIV-----DGAHLNNMK 74
Cdd:COG1119 2 PLLELRNVTVRRGG----KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVWELR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 75 neskalyrqQMVGFVFQDF-NLLPTMTNKENImmplILAGA----------KRKDIEqRVHQLTVQLHLEGFLNKYPSEI 143
Cdd:COG1119 78 ---------KRIGLVSPALqLRFPRDETVLDV----VLSGFfdsiglyrepTDEQRE-RARELLELLGLAHLADRPFGTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 144 SGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHsnidasYAE-------RVIFIK 215
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTH------HVEeippgitHVLLLK 217
|
....*.
gi 487401142 216 DGRLYH 221
Cdd:COG1119 218 DGRVVA 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-218 |
1.72e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 94.07 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIasfdgltegdiivdgahLNNMKNESKALYRQQMVGFVFQdFNLLPTMT 100
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-----------------LGELEKLSGSVSVPGSIAYVSQ-EPWIQNGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIM--MPL--------ILAGAKRKDIEQRVHQLTVQLHlEGFLNkypseISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:cd03250 82 IRENILfgKPFdeeryekvIKACALEPDLEILPDGDLTEIG-EKGIN-----LSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487401142 171 GALDSKTSKTLM-MLFQEIHQLEQTILMVTHsNID-ASYAERVIFIKDGR 218
Cdd:cd03250 156 SAVDAHVGRHIFeNCILGLLLNNKTRILVTH-QLQlLPHADQIVVLDNGR 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
22-218 |
1.83e-23 |
|
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: 98.74 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkaLyrQQMVGFVFQD---FNllpt 98
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS--L--RAAIGIVPQDtvlFN---- 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 99 MTNKENImmplilA----GAKRKDIEQrvhqlTVQL-HLEGFLNKYPS-----------EISGGQKQRIAIARALVTKPT 162
Cdd:COG5265 446 DTIAYNI------AygrpDASEEEVEA-----AARAaQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTH--SNIdaSYAERVIFIKDGR 218
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHrlSTI--VDADEILVLEAGR 569
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
4-222 |
2.48e-23 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 94.76 E-value: 2.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKneSKALYRQ 83
Cdd:COG4604 3 EIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP--SRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 84 qmVGFVFQDFNLLPTMTNKEnimmpLILAG--------AKRKDiEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIAR 155
Cdd:COG4604 77 --LAILRQENHINSRLTVRE-----LVAFGrfpyskgrLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 156 ALVTKPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHS-NIDASYAERVIFIKDGRLYHE 222
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDiNFASCYADHIVAMKDGRVVAQ 217
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
22-219 |
2.90e-23 |
|
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: 98.28 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMknESKALYRQqmVGFVFQDfNLLPTMTN 101
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIA--DPAWLRRQ--MGVVLQE-NVLFSRSI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 KENIMM--PLI----------LAGAKRKDIEQRvhqltvqlhlEGF---LNKYPSEISGGQKQRIAIARALVTKPTILLA 166
Cdd:TIGR01846 548 RDNIALcnPGApfehvihaakLAGAHDFISELP----------QGYnteVGEKGANLSGGQRQRIAIARALVGNPRILIF 617
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487401142 167 DEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:TIGR01846 618 DEATSALDYESEALIMRNMREICR-GRTVIIIAHRLSTVRACDRIIVLEKGQI 669
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-220 |
4.08e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 4.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKAL 80
Cdd:PRK13548 1 AMLEARNLSVRLGG----RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YR----QQM-VGFVFqdfnllptmTNKENIMM---PLILAGAKRKDIEQRVHQLTVQLHLEGflNKYPsEISGGQKQRIA 152
Cdd:PRK13548 77 RRavlpQHSsLSFPF---------TVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAG--RDYP-QLSGGEQQRVQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 153 IARALV------TKPTILLADEPTGALDSKTSKTLMMLfqeIHQLEQ----TILMVTHS-NIDASYAERVIFIKDGRLY 220
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRL---ARQLAHerglAVIVVLHDlNLAARYADRIVLLHQGRLV 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-222 |
6.34e-23 |
|
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: 96.80 E-value: 6.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGL--TEGDII---------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFD----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 65 -------VDGAHLNNMK----NESKALYRQQM--VGFVFQ-DFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQL 130
Cdd:TIGR03269 77 kvgepcpVCGGTLEPEEvdfwNLSDKLRRRIRkrIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 131 HLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLM-MLFQEIHQLEQTILMVTH-SNIDASYA 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHnALEEAVKASGISMVLTSHwPEVIEDLS 236
|
250
....*....|....
gi 487401142 209 ERVIFIKDGRLYHE 222
Cdd:TIGR03269 237 DKAIWLENGEIKEE 250
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
6.36e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.05 E-value: 6.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNmKNESKAly 81
Cdd:PRK13648 7 IIVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DNFEKL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 rQQMVGFVFQD---------------FNLlptmtnkENIMMPlilagakRKDIEQRVHQLTVQLHLEGFLNKYPSEISGG 146
Cdd:PRK13648 82 -RKHIGIVFQNpdnqfvgsivkydvaFGL-------ENHAVP-------YDEMHRRVSEALKQVDMLERADYEPNALSGG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 147 QKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHSNIDASYAERVIFIKDGRLY----- 220
Cdd:PRK13648 147 QKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYkegtp 226
|
....*....
gi 487401142 221 HEIYRGEES 229
Cdd:PRK13648 227 TEIFDHAEE 235
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-219 |
8.17e-23 |
|
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: 96.74 E-value: 8.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLNNMKNESkalyRQQMVGFVFQDFNLLPT 98
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLV---GVwppTAGSVRLDGADLSQWDREE----LGRHIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 99 mTNKENI-MMP-----LILAGAKRKDieqrVHQLTVQLHlEGflnkYPSEI-------SGGQKQRIAIARALVTKPTILL 165
Cdd:COG4618 421 -TIAENIaRFGdadpeKVVAAAKLAG----VHEMILRLP-DG----YDTRIgeggarlSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 166 ADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH-SNIdASYAERVIFIKDGRL 219
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHrPSL-LAAVDKLLVLRDGRV 544
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-219 |
1.41e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 93.53 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIV-DGAHLNNMKN--ESKALYRQqmVGFVFQ--DFNL 95
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgDYAIPANLKKikEVKRLRKE--IGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 LPTMTNKENIMMPLILaGAKRKDIEQRVHQLTVQLHL-EGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALD 174
Cdd:PRK13645 104 FQETIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 487401142 175 SKTSKTLMMLFQEIHQ-LEQTILMVTHsNIDA--SYAERVIFIKDGRL 219
Cdd:PRK13645 183 PKGEEDFINLFERLNKeYKKRIIMVTH-NMDQvlRIADEVIVMHEGKV 229
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2-218 |
2.84e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.91 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLnattALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAH-----LNNM-KN 75
Cdd:PRK11701 6 LLSVRGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdLYALsEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 76 ESKALYRQQMvGFVFQDF--NLLPTMTNKENIMMPLILAGAKR-KDI-EQRVHQL-TVQLHLEGfLNKYPSEISGGQKQR 150
Cdd:PRK11701 82 ERRRLLRTEW-GFVHQHPrdGLRMQVSAGGNIGERLMAVGARHyGDIrATAGDWLeRVEIDAAR-IDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 151 IAIARALVTKPTILLADEPTGALD-SKTSKTLMMLFQEIHQLEQTILMVTHsniDASYA----ERVIFIKDGR 218
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDvSVQARLLDLLRGLVRELGLAVVIVTH---DLAVArllaHRLLVMKQGR 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-218 |
7.43e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.00 E-value: 7.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKS----TLLNLIASFDGL-TEGDIIVDGAHLNNMKNE 76
Cdd:PRK15134 5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SKALYRQQMVGFVFQD--FNLLPTMTNKENIMMPLIL-----AGAKRKDIEQRVHQLTVQlHLEGFLNKYPSEISGGQKQ 149
Cdd:PRK15134 85 TLRGVRGNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLhrgmrREAARGEILNCLDRVGIR-QAAKRLTDYPHQLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 150 RIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQeLNMGLLFITHNlSIVRKLADRVAVMQNGR 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-189 |
1.89e-21 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 90.23 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKV--YGKGL---NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNmkn 75
Cdd:PRK15112 3 TLLEVRNLSKTfrYRTGWfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 76 eSKALYRQQMVGFVFQD--FNLLPTMTNKENIMMPLIL-----AGAKRKDIEQRVHQLTVqlhLEGFLNKYPSEISGGQK 148
Cdd:PRK15112 80 -GDYSYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLntdlePEQREKQIIETLRQVGL---LPDHASYYPHMLAPGQK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 487401142 149 QRIAIARALVTKPTILLADEPTGALD-SKTSK--TLMMLFQEIH 189
Cdd:PRK15112 156 QRLGLARALILRPKVIIADEALASLDmSMRSQliNLMLELQEKQ 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-218 |
2.58e-21 |
|
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: 92.20 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASF--DGLTEGDIIVDGAHLnnmKNESKA 79
Cdd:TIGR02633 1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPL---KASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LYRQQMVGFVFQDFNLLPTMTNKENIMM--PLILAGAKRKDIE--QRVHQLTVQLHLEGFLNKYP-SEISGGQKQRIAIA 154
Cdd:TIGR02633 74 DTERAGIVIIHQELTLVPELSVAENIFLgnEITLPGGRMAYNAmyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 155 RALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKlNEVKAVCDTICVIRDGQ 218
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
2-225 |
2.96e-21 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 90.57 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKS----TLLNLIaSFDGLTEGD-IIVDGAHLNNMKNE 76
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLI-DYPGRVMAEkLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 77 SkalyRQQMVG----FVFQD--FNLLPTMTNKENIMMPL-ILAGAKRKDIEQRVHQLTVQLHL---EGFLNKYPSEISGG 146
Cdd:PRK11022 82 E----RRNLVGaevaMIFQDpmTSLNPCYTVGFQIMEAIkVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 147 QKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHS-NIDASYAERVIFIKDGRLY---- 220
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDlALVAEAAHKIIVMYAGQVVetgk 237
|
....*.
gi 487401142 221 -HEIYR 225
Cdd:PRK11022 238 aHDIFR 243
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-231 |
3.43e-21 |
|
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: 92.11 E-value: 3.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNAttaLNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlNNMKNESKALYR 82
Cdd:TIGR01193 474 IVINDVSYSYGYGSNI---LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG---FSLKDIDRHTLR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QqMVGFVFQD---F------NLLptMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEgfLNKYPSEISGGQKQRIAI 153
Cdd:TIGR01193 548 Q-FINYLPQEpyiFsgsileNLL--LGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTE--LSEEGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 154 ARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHqlEQTILMVTHSNIDASYAERVIFIKDGRLyheIYRGEESQL 231
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ--DKTIIFVAHRLSVAKQSDKIIVLDHGKI---IEQGSHDEL 695
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-236 |
7.69e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 7.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 5 VKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDgahlNNMKneskalyrqq 84
Cdd:COG0488 1 LENLSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----KGLR---------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 85 mVGFVFQDFNLLPTMTNKENIMMPLILAGAKRK--------------------------------DIEQRVHQLTVQLHL 132
Cdd:COG0488 63 -IGYLPQEPPLDDDLTVLDTVLDGDAELRALEAeleeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 133 -EGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTsktlmmlfqeIHQLEQ-------TILMVTHSN-- 202
Cdd:COG0488 142 pEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----------IEWLEEflknypgTVLVVSHDRyf 211
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 487401142 203 IDASyAERVIFIKDGRLYheIYRG------EESQLAFQQR 236
Cdd:COG0488 212 LDRV-ATRILELDRGKLT--LYPGnysaylEQRAERLEQE 248
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-200 |
1.01e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 89.12 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnnmknESKAL 80
Cdd:PRK13536 40 VAIDLAGVSKSYGD----KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-----PARAR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTK 160
Cdd:PRK13536 111 LARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 487401142 161 PTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTH 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-206 |
1.27e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.92 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLnattALNQMNLSVGAGEFVAIMGESGSGKSTLL-------NLIASFDglTEGDIIVDGAHLNNMK 74
Cdd:PRK14243 10 VLRTENLNVYYGSFL----AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKNLYAPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 75 NESKALYRQqmVGFVFQDFNLLPTmTNKENIMMPLILAGAK---RKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRI 151
Cdd:PRK14243 84 VDPVEVRRR--IGMVFQKPNPFPK-SIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 152 AIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDAS 206
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHNMQQAA 214
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-200 |
1.62e-20 |
|
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: 85.87 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 17 NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnnmkNESKALYRQQMVGFVFQDfNLL 96
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPL----AEQRDEPHENILYLGHLP-GLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 97 PTMTNKENI-MMPLILAGAKRKdieqrVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDS 175
Cdd:TIGR01189 86 PELSALENLhFWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
170 180
....*....|....*....|....*
gi 487401142 176 KTSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-222 |
1.80e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 1.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKneSKAL 80
Cdd:PRK11231 1 MTLRTENLTVGYGT----KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS--SRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQqmvgfvfqdFNLLPT-MTNKENIMM---------P-LILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQ 149
Cdd:PRK11231 75 ARR---------LALLPQhHLTPEGITVrelvaygrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 150 RIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDAS-YAERVIFIKDGRLYHE 222
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASrYCDHLVVLANGHVMAQ 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
20-219 |
2.44e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 86.67 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 20 TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDG--AHLNNMkneskalyrqqMVGFVfqdfn 94
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA---GIlepTSGRVEVNGrvSALLEL-----------GAGFH----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 95 llPTMTNKENIMMPLILAGAKRKDIEQRVHqltvqlHLEGFlnkypSEI-----------SGGQKQRIAIARALVTKPTI 163
Cdd:COG1134 101 --PELTGRENIYLNGRLLGLSRKEIDEKFD------EIVEF-----AELgdfidqpvktySSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 164 LLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSnIDA--SYAERVIFIKDGRL 219
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHS-MGAvrRLCDRAIWLEKGRL 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-219 |
2.65e-20 |
|
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: 89.48 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVY---GKGLnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLTE----------GDIIVDGA 68
Cdd:TIGR03269 279 IIKVRNVSKRYisvDRGV--VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIA---GVLEptsgevnvrvGDEWVDMT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 69 HLNNMkNESKAlyrQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTV----QLHLEGFLNKYPSEIS 144
Cdd:TIGR03269 354 KPGPD-GRGRA---KRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMvgfdEEKAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 145 GGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMmlfQEIH----QLEQTILMVTHsniDASYA----ERVIFIKD 216
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVT---HSILkareEMEQTFIIVSH---DMDFVldvcDRAALMRD 503
|
...
gi 487401142 217 GRL 219
Cdd:TIGR03269 504 GKI 506
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-218 |
3.64e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.17 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnnmknESKALYR 82
Cdd:PRK13537 8 IDFRNVEKRYG----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PSRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDAS-YAERVIFIKDGR 218
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAErLCDRLCVIEEGR 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-219 |
3.89e-20 |
|
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: 85.62 E-value: 3.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMkneSKALYR 82
Cdd:cd03244 3 IEFKNVSLRYRPNLP--PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMvGFVFQDfnllptmtnkenimmPLILAGAKRKDI-------EQRVHQLTVQLHLEGFLNKYP-----------SEIS 144
Cdd:cd03244 78 SRI-SIIPQD---------------PVLFSGTIRSNLdpfgeysDEELWQALERVGLKEFVESLPggldtvveeggENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 145 GGQKQRIAIARALVTKPTILLADEPTGALDSKTS----KTLMMLFQEIhqleqTILMVTH---SNIDasyAERVIFIKDG 217
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDaliqKTIREAFKDC-----TVLTIAHrldTIID---SDRILVLDKG 213
|
..
gi 487401142 218 RL 219
Cdd:cd03244 214 RV 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-200 |
4.04e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 86.20 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkGLnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKneSKALY 81
Cdd:PRK11300 5 LLSVSGLMMRFG-GL---LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP--GHQIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGfVFQDFNLLPTMTNKENIMMPL-------ILAG---------AKRKDIEQRVHQLTvQLHLEGFLNKYPSEISG 145
Cdd:PRK11300 79 RMGVVR-TFQHVRLFREMTVIENLLVAQhqqlktgLFSGllktpafrrAESEALDRAATWLE-RVGLLEHANRQAGNLAY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 146 GQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTH 200
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrNEHNVTVLLIEH 212
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-219 |
4.28e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 88.86 E-value: 4.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESkaLY 81
Cdd:PRK13657 334 AVEFDDVSFSYD---NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS--LR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQqmVGFVFQDFNLL------------PTMTNKEnimMPLILAGAKRKD-IEQRVHQLTVQLHLEGflnkypSEISGGQK 148
Cdd:PRK13657 409 RN--IAVVFQDAGLFnrsiednirvgrPDATDEE---MRAAAERAQAHDfIERKPDGYDTVVGERG------RQLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 149 QRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:PRK13657 478 QRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNADRILVFDNGRV 547
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
3-198 |
6.32e-20 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 88.24 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMkneSKALYR 82
Cdd:PRK10790 341 IDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL---SHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQmVGFVFQDfnllptmtnkenimmPLILAGAKRKDI-------EQRVHQL--TVQLH---------LEGFLNKYPSEIS 144
Cdd:PRK10790 415 QG-VAMVQQD---------------PVVLADTFLANVtlgrdisEEQVWQAleTVQLAelarslpdgLYTPLGEQGNNLS 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 487401142 145 GGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHqlEQTILMV 198
Cdd:PRK10790 479 VGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVR--EHTTLVV 530
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-200 |
1.23e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 86.11 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKStllnLIAS-FDGLTEGDIIV--DGAHLNNMK------NESKALYRQQMvGFVFQ 91
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKS----LIAKaICGITKDNWHVtaDRFRWNGIDllklspRERRKIIGREI-AMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 92 DFN--LLPTMTNKENIM--MPLI--------LAGAKRKDIEQRVHQLTVQLHlEGFLNKYPSEISGGQKQRIAIARALVT 159
Cdd:COG4170 97 EPSscLDPSAKIGDQLIeaIPSWtfkgkwwqRFKWRKKRAIELLHRVGIKDH-KDIMNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 487401142 160 KPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQT-ILMVTH 200
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTsILLISH 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-200 |
2.28e-19 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 84.43 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 24 QMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYRQQMvGFVFQDFNLLPTMTNKE 103
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRM-SMLFQSGALFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 104 NIMMPLilagAKRKDIEQRVHQLTVQLHLE-----GFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTS 178
Cdd:PRK11831 104 NVAYPL----REHTQLPAPLLHSTVMMKLEavglrGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180
....*....|....*....|...
gi 487401142 179 KTLMMLFQEI-HQLEQTILMVTH 200
Cdd:PRK11831 180 GVLVKLISELnSALGVTCVVVSH 202
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-218 |
2.51e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.96 E-value: 2.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVK--HVKkVYGKGLnattaLNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDG--LTEGDIIVDGAHLNNMKNESK 78
Cdd:COG0396 1 LEIKnlHVS-VEGKEI-----LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRqqmVGFVFQD---------FNLLPTMTNKenIMMPLILAGAKRKDIEqrvhQLTVQLHL-EGFLNKYPSE-ISGGQ 147
Cdd:COG0396 75 ARAG---IFLAFQYpveipgvsvSNFLRTALNA--RRGEELSAREFLKLLK----EKMKELGLdEDFLDRYVNEgFSGGE 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 148 KQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSN--IDASYAERVIFIKDGR 218
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQriLDYIKPDFVHVLVDGR 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-251 |
2.57e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 84.38 E-value: 2.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 15 GLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEG-----DIIVDGAHLNNMKNeskALYRQQMVGFV 89
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD---VLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 90 FQDFNLLPTMtnkeniMMPLILAGAK------RKDI----EQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVT 159
Cdd:PRK14271 107 FQRPNPFPMS------IMDNVLAGVRahklvpRKEFrgvaQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 160 KPTILLADEPTGALDSKTSKTLMMLFQEIHQlEQTILMVTHSNIDAS-YAERVIFIKDGRLYHEiyrGEESQLAFQQRIT 238
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLAD-RLTVIIVTHNLAQAArISDRAALFFDGRLVEE---GPTEQLFSSPKHA 256
|
250
....*....|...
gi 487401142 239 DSLALVNGGSVNI 251
Cdd:PRK14271 257 ETARYVAGLSGDV 269
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
3-228 |
4.18e-19 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 82.83 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHL--NNMKN----- 75
Cdd:TIGR03740 1 LETKNLSKRFGK----QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWtrKDLHKigsli 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 76 ESKALYRqqmvgfvfqdfNLlptmTNKENIMMPLILAGAKRKDIEQRVHqlTVQLHLEGflNKYPSEISGGQKQRIAIAR 155
Cdd:TIGR03740 77 ESPPLYE-----------NL----TARENLKVHTTLLGLPDSRIDEVLN--IVDLTNTG--KKKAKQFSLGMKQRLGIAI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 156 ALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH--SNIDAsYAERVIFIKDGRL-YHEIYRGEE 228
Cdd:TIGR03740 138 ALLNHPKLLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHilSEVQQ-LADHIGIISEGVLgYQGKINKSE 212
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2-218 |
8.15e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.98 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASF--DGLTEGDIIVDGAHL--NNMKNES 77
Cdd:PRK13549 5 LLEMKNITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqaSNIRDTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KAlyrqqMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIE---QRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIA 154
Cdd:PRK13549 81 RA-----GIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDamyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 155 RALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:PRK13549 156 KALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKlNEVKAISDTICVIRDGR 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2-222 |
1.78e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlNNMKNESKALY 81
Cdd:PRK11614 5 MLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG---KDITDWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLILagAKRKDIEQR---VHQLTVQLHLEgfLNKYPSEISGGQKQRIAIARALV 158
Cdd:PRK11614 78 MREAVAIVPEGRRVFSRMTVEENLAMGGFF--AERDQFQERikwVYELFPRLHER--RIQRAGTMSGGEQQMLAIGRALM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 159 TKPTILLADEPTGALdskTSKTLMMLFQEIHQLEQ---TILMV-THSNIDASYAERVIFIKDGRLYHE 222
Cdd:PRK11614 154 SQPRLLLLDEPSLGL---APIIIQQIFDTIEQLREqgmTIFLVeQNANQALKLADRGYVLENGHVVLE 218
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-219 |
2.41e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 81.43 E-value: 2.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 26 NLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLT--EGDIIVDGAHLNNMKNESKALYR-----QQMVGF---VFQDFNL 95
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMA---GLLpgQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFampVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 -LPtmtnkenimmplilAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALV-TKPTI------LLAD 167
Cdd:COG4138 93 hQP--------------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqVWPTInpegqlLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487401142 168 EPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGRL 219
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDlNHTLRHADRVWLLKQGKL 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-230 |
2.75e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 83.53 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKhvkkvygkGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnMKNESKALy 81
Cdd:COG1129 256 VLEVE--------GLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR-IRSPRDAI- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 rQQMVGFVFQD---FNLLPTMTNKENIMMP---------LILAGAKRKDIEQRVHQLTVqlhlegflnKYPS------EI 143
Cdd:COG1129 326 -RAGIAYVPEDrkgEGLVLDLSIRENITLAsldrlsrggLLDRRRERALAEEYIKRLRI---------KTPSpeqpvgNL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 144 SGGQKQRIAIARALVTKPTILLADEPT-----GAldsKtsktlmmlfQEIHQL-----EQ--TILMVThSNID--ASYAE 209
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEPTrgidvGA---K---------AEIYRLirelaAEgkAVIVIS-SELPelLGLSD 462
|
250 260
....*....|....*....|.
gi 487401142 210 RVIFIKDGRLYHEIYRGEESQ 230
Cdd:COG1129 463 RILVMREGRIVGELDREEATE 483
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-221 |
2.88e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 2.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVdGAHLNnmkneskaly 81
Cdd:COG0488 315 VLELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK---------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 rqqmVGFVFQDFNLL-PTMTNKENImmplilAGAKRKDIEQRVHQLtvqlhLEGFL------NKYPSEISGGQKQRIAIA 154
Cdd:COG0488 380 ----IGYFDQHQEELdPDKTVLDEL------RDGAPGGTEQEVRGY-----LGRFLfsgddaFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 155 RALVTKPTILLADEPTGALDSKTsktlmmlfqeIHQLEQ-------TILMVTH-----SNIdasyAERVIFIKDGRLYH 221
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIET----------LEALEEalddfpgTVLLVSHdryflDRV----ATRILEFEDGGVRE 509
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-200 |
2.91e-18 |
|
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: 79.98 E-value: 2.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAS--FDGLTEGDIIVDGAHLNnmknesKALYRQqmVGFVFQDFNLLPTM 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLD------KNFQRS--TGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENIMMPLILAGakrkdieqrvhqltvqlhlegflnkypseISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSK 179
Cdd:cd03232 95 TVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAY 145
|
170 180
....*....|....*....|.
gi 487401142 180 TLMMLFQEIHQLEQTILMVTH 200
Cdd:cd03232 146 NIVRFLKKLADSGQAILCTIH 166
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-218 |
3.06e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 83.37 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 19 TTALNQMNLSVGAGEFVAIMGESGSGKS----TLLNLIASFDGLTEGDIIV------DGAHLNNMKNESKALYRQQMVGF 88
Cdd:PRK10261 29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLlrrrsrQVIELSEQSAAQMRHVRGADMAM 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 89 VFQD--FNLLPTMTNKENIMMPLIL-AGAKRKDIEQRVHQLTVQLHL---EGFLNKYPSEISGGQKQRIAIARALVTKPT 162
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQ-LEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKeMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-174 |
4.86e-18 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 82.98 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKST----LLNLIASfdglTEGDIIVDGAHLNNMKNESKALYRQQMvGFVFQD--FN 94
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVES----QGGEIIFNGQRIDTLSPGKLQALRRDI-QFIFQDpyAS 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 95 LLPTMTNKENIMMPLILAGAKRKDIEQ-RVHQL--TVQLHLEGFLnKYPSEISGGQKQRIAIARALVTKPTILLADEPTG 171
Cdd:PRK10261 414 LDPRQTVGDSIMEPLRVHGLLPGKAAAaRVAWLleRVGLLPEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
|
...
gi 487401142 172 ALD 174
Cdd:PRK10261 493 ALD 495
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
3-226 |
5.17e-18 |
|
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: 80.07 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVY-----GKGLNAT------------TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIV 65
Cdd:cd03267 1 IEVSNLSKSYrvyskEPGLIGSlkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 66 DGahLNNMKNESKALYRqqmVGFVF-QDFNL---LPTMtnkENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPS 141
Cdd:cd03267 81 AG--LVPWKRRKKFLRR---IGVVFgQKTQLwwdLPVI---DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 142 EISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTHSNID-ASYAERVIFIKDGRL 219
Cdd:cd03267 153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGtTVLLTSHYMKDiEALARRVLVIDKGRL 232
|
....*..
gi 487401142 220 yheIYRG 226
Cdd:cd03267 233 ---LYDG 236
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-201 |
5.69e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.70 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 17 NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnmknesKALyRQQMVGFVFQDFNL- 95
Cdd:PRK15056 18 NGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR------QAL-QKNLVAYVPQSEEVd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 --LPTMTnKENIMMPL-----ILAGAKRKDiEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADE 168
Cdd:PRK15056 91 wsFPVLV-EDVVMMGRyghmgWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190
....*....|....*....|....*....|...
gi 487401142 169 PTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS 201
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-219 |
6.70e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 6.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 13 GKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnNMKNESKALyrQQMVGFVFQD 92
Cdd:PRK11288 11 GKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM-RFASTTAAL--AAGVAIIYQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 93 FNLLPTMTNKENIM---MPlilagAKRKDIEQRVHQLTVQLHLEGF-LNKYPS----EISGGQKQRIAIARALVTKPTIL 164
Cdd:PRK11288 88 LHLVPEMTVAENLYlgqLP-----HKGGIVNRRLLNYEAREQLEHLgVDIDPDtplkYLSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 165 LADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDASYA--ERVIFIKDGRL 219
Cdd:PRK11288 163 AFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH-RMEEIFAlcDAITVFKDGRY 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-201 |
1.16e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 79.70 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLtEGDIIVDG--AHLNNMKNESKA----LYRQqmVGFVFQDFNL 95
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVEGrvEFFNQNIYERRVnlnrLRRQ--VSMVHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 LPtMTNKENIMMPLILAGAKRK-----DIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:PRK14258 100 FP-MSVYDNVAYGVKIVGWRPKleiddIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190
....*....|....*....|....*....|..
gi 487401142 171 GALDSKTSKTLMMLFQEIH-QLEQTILMVTHS 201
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRlRSELTMVIVSHN 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-231 |
1.20e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 20 TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKneSKALYRQqmVGFVFQDFNLLPTM 99
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS--SKAFARK--VAYLPQQLPAAEGM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENIMM---PLILA-GAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDS 175
Cdd:PRK10575 101 TVRELVAIgryPWHGAlGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 176 KTSKTLMMLfqeIHQLEQ----TILMVTHS-NIDASYAERVIFIKDGRLyheIYRGEESQL 231
Cdd:PRK10575 181 AHQVDVLAL---VHRLSQerglTVIAVLHDiNMAARYCDYLVALRGGEM---IAQGTPAEL 235
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-219 |
1.27e-17 |
|
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: 77.86 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 14 KGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNmKNESKAlyRQQMVGFVFQD- 92
Cdd:cd03215 8 RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR-RSPRDA--IRAGIAYVPEDr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 93 --FNLLPTMTNKENIMMPLILagakrkdieqrvhqltvqlhlegflnkypseiSGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:cd03215 85 krEGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 171 GALDSKTSktlmmlfQEIHQL-----EQ--TILMVThSNID--ASYAERVIFIKDGRL 219
Cdd:cd03215 133 RGVDVGAK-------AEIYRLirelaDAgkAVLLIS-SELDelLGLCDRILVMYEGRI 182
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-218 |
1.75e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 81.46 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 20 TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLTEGDIIVDGAHLNNMKNESKALYRqqmVGFVFQDFNLLPTM 99
Cdd:PLN03211 82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALA---GRIQGNNFTGTILANNRKPTKQILKR---TGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENIMMP--LILAGAKRKDIEQRVHQLTV-QLHLEG-----FLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTG 171
Cdd:PLN03211 156 TVRETLVFCslLRLPKSLTKQEKILVAESVIsELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 172 ALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYA--ERVIFIKDGR 218
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-217 |
2.08e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 81.01 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIV-DGAHLnnmkneskalyrqqMvgFVFQDfNLLP 97
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIA---GLwpyGSGRIARpAGARV--------------L--FLPQR-PYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 TMTNKENIMMPLILAGAKRKDIEQRVHQltVQL-HLEGFLNK---YPSEISGGQKQRIAIARALVTKPTILLADEPTGAL 173
Cdd:COG4178 439 LGTLREALLYPATAEAFSDAELREALEA--VGLgHLAERLDEeadWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487401142 174 DSKTSKTLMMLFQEihQLEQ-TILMVTHSNIDASYAERVIFIKDG 217
Cdd:COG4178 517 DEENEAALYQLLRE--ELPGtTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-219 |
2.35e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 2.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMknESKAL 80
Cdd:PRK09536 2 PMIDVSDLSVEFG----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAL--SARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 YRQqmVGFVFQDFNLLPTMTNKENIMM---PLI--LAGAKRKDiEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIAR 155
Cdd:PRK09536 76 SRR--VASVPQDTSLSFEFDVRQVVEMgrtPHRsrFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 156 ALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGRL 219
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDlDLAARYCDELVLLADGRV 217
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-218 |
2.43e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTL----LNLIASfdglTEGDIIVDGAHLNnmknesK 78
Cdd:COG4152 2 LELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTiriiLGILAP----DSGEVLWDGEPLD------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQqmVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALV 158
Cdd:COG4152 68 EDRRR--IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 159 TKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDasYAER----VIFIKDGR 218
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSH-QME--LVEElcdrIVIINKGR 206
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
3-225 |
4.26e-17 |
|
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: 76.80 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVK-KVYGKglnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDG--LTEGDIIVDGAHLNNMKNESKA 79
Cdd:cd03217 1 LEIKDLHvSVGGK-----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 lyrQQMVGFVFQdfnllptmtnkenimMPLILAGAKRKDIEQRVHqltvqlhlEGFlnkypseiSGGQKQRIAIARALVT 159
Cdd:cd03217 76 ---RLGIFLAFQ---------------YPPEIPGVKNADFLRYVN--------EGF--------SGGEKKRNEILQLLLL 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 160 KPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSN--IDASYAERVIFIKDGR--------LYHEIYR 225
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQrlLDYIKPDRVHVLYDGRivksgdkeLALEIEK 197
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
13-226 |
7.23e-17 |
|
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: 76.15 E-value: 7.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 13 GKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLTEGDIIVDGA-HLNNMKNESKALYRQQMVGFVFQ 91
Cdd:cd03233 14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEGDiHYNGIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 92 DFNLLPTMTNKENIMMPLILAGakrkdieqrvhqltvqlhlegflNKYPSEISGGQKQRIAIARALVTKPTILLADEPTG 171
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 172 ALDSKTSKTLMMLFQEI-HQLEQTILMVTHSNIDASYA--ERVIFIKDGRlyhEIYRG 226
Cdd:cd03233 148 GLDSSTALEILKCIRTMaDVLKTTTFVSLYQASDEIYDlfDKVLVLYEGR---QIYYG 202
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-211 |
8.55e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 77.08 E-value: 8.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLT---EGDIIVDGAHLNNMKNESKAlyrQQMVGFVFQDFNLLP 97
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVIT---GKTrpdSGSVLFGGTDLTGLDEHEIA---RLGIGRKFQKPTVFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 TMTNKENIMmpLILAGAKR----------KDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLAD 167
Cdd:COG4674 99 ELTVFENLE--LALKGDRGvfaslfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 168 EPT-GALDSKTSKTlMMLFQEIHQlEQTILMVTHsniD----ASYAERV 211
Cdd:COG4674 177 EPVaGMTDAETERT-AELLKSLAG-KHSVVVVEH---DmefvRQIARKV 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-200 |
1.01e-16 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 79.30 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 25 MNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIV-DGAHLNNMKNESKALY-RQQMVGF-------------- 88
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfKNEHTNDMTNEQDYQGdEEQNVGMknvnefsltkeggs 1266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 89 -----VFQ-------------DFNL-----LPTMTNKENIMMPLIL--------AGAKRKDIEQRVHQLTVQLHLEGFLN 137
Cdd:PTZ00265 1267 gedstVFKnsgkilldgvdicDYNLkdlrnLFSIVSQEPMLFNMSIyenikfgkEDATREDVKRACKFAAIDEFIESLPN 1346
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 138 KYPSEI-------SGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIH-QLEQTILMVTH 200
Cdd:PTZ00265 1347 KYDTNVgpygkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAH 1417
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-216 |
1.05e-16 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 74.88 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 17 NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIvdgahlnnmkneskalyrqqmvgfvfqdf 93
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA---GLwpwGSGRIG----------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 94 nllptMTNKENIMM----PLILAGAKRkdiEQRVhqltvqlhlegflnkYP--SEISGGQKQRIAIARALVTKPTILLAD 167
Cdd:cd03223 60 -----MPEGEDLLFlpqrPYLPLGTLR---EQLI---------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 168 EPTGALDSKTSKTLMMLFQEihqLEQTILMVTHSNIDASYAERVIFIKD 216
Cdd:cd03223 117 EATSALDEESEDRLYQLLKE---LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
12-222 |
1.12e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.95 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 12 YGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKneSKALYRQqmVGFVFQ 91
Cdd:PRK10253 17 YGK----YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYA--SKEVARR--IGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 92 DFNLLPTMTNKENIM------MPLILAGakRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILL 165
Cdd:PRK10253 89 NATTPGDITVQELVArgryphQPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 166 ADEPTGALDSKTSKTLMMLFQEIHQLE-QTILMVTHS-NIDASYAERVIFIKDGRLYHE 222
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKgYTLAAVLHDlNQACRYASHLIALREGKIVAQ 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-234 |
1.13e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 78.99 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 17 NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMK-NESKAlyRQQMVG---FVFQD 92
Cdd:PRK10789 326 TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRS--RLAVVSqtpFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 93 fnllpTMTNkeNImmPLILAGAKRKDIEQ-----RVHQLTVQLHlEGflnkYPSEI-------SGGQKQRIAIARALVTK 160
Cdd:PRK10789 404 -----TVAN--NI--ALGRPDATQQEIEHvarlaSVHDDILRLP-QG----YDTEVgergvmlSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 161 PTILLADEPTGALDSKTSktlmmlFQEIHQLEQ-----TILMVTHSNIDASYAERVIFIKDGrlyHEIYRGEESQLAFQ 234
Cdd:PRK10789 470 AEILILDDALSAVDGRTE------HQILHNLRQwgegrTVIISAHRLSALTEASEILVMQHG---HIAQRGNHDQLAQQ 539
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-226 |
2.24e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.05 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVY-----GKGLNAT------------TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDI 63
Cdd:COG4586 3 EVENLSKTYrvyekEPGLKGAlkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLT---GIlvpTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 64 IVDGahLNNMKNESKALYRqqmVGFVF------------QD-FNLLPTMTNkenimMPlilagakRKDIEQRVHQLTVQL 130
Cdd:COG4586 80 RVLG--YVPFKRRKEFARR---IGVVFgqrsqlwwdlpaIDsFRLLKAIYR-----IP-------DAEYKKRLDELVELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 131 HLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTH--SNIDAsY 207
Cdd:COG4586 143 DLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGtTILLTSHdmDDIEA-L 221
|
250
....*....|....*....
gi 487401142 208 AERVIFIKDGRLyheIYRG 226
Cdd:COG4586 222 CDRVIVIDHGRI---IYDG 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-200 |
2.35e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMkneSKALY 81
Cdd:PRK15439 11 LLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL---TPAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMMPLilagAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPNLSVKENILFGL----PKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 487401142 162 TILLADEPTGALdskTSKTLMMLFQEIHQLEQT---ILMVTH 200
Cdd:PRK15439 160 RILILDEPTASL---TPAETERLFSRIRELLAQgvgIVFISH 198
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-218 |
3.30e-16 |
|
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: 72.87 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLnattALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnnmkneSKALYr 82
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------VKIGY- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 qqmvgfvfqdfnllptmtnkenimmplilagakrkdieqrVHQLtvqlhlegflnkypseiSGGQKQRIAIARALVTKPT 162
Cdd:cd03221 68 ----------------------------------------FEQL-----------------SGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDsktSKTLMMLFQEIHQLEQTILMVTHSN--IDAsYAERVIFIKDGR 218
Cdd:cd03221 91 LLLLDEPTNHLD---LESIEALEEALKEYPGTVILVSHDRyfLDQ-VATKIIELEDGK 144
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
14-220 |
6.57e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 14 KGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGLT--EGDIIVDGAHLNNMKNESKALYR-----QQMV 86
Cdd:PRK03695 4 NDVAVSTRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMA---GLLpgSGSIQFAGQPLEAWSAAELARHRaylsqQQTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 87 GF---VFQDFNL-LPtmtnkenimmplilAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARA-LVTKP 161
Cdd:PRK03695 81 PFampVFQYLTLhQP--------------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWP 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 162 TI------LLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGRLY 220
Cdd:PRK03695 147 DInpagqlLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-217 |
8.18e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 8.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMkneSKALY 81
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL---DHKLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKENIMM-----------PLIlagaKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQR 150
Cdd:PRK09700 78 AQLGIGIIYQELSVIDELTVLENLYIgrhltkkvcgvNII----DWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 151 IAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDG 217
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDG 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-219 |
8.73e-16 |
|
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: 73.60 E-value: 8.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskALYR 82
Cdd:cd03369 7 IEVENLSVRYAPDL--PPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE--DLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QqmVGFVFQDfnllptmtnkenimmPLILAGAKRKDIEQRVHQLTVQLH-----LEGFLNkypseISGGQKQRIAIARAL 157
Cdd:cd03369 83 S--LTIIPQD---------------PTLFSGTIRSNLDPFDEYSDEEIYgalrvSEGGLN-----LSQGQRQLLCLARAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 487401142 158 VTKPTILLADEPTGALDSKT----SKTLMMLFQEIhqleqTILMVTH---SNIDasyAERVIFIKDGRL 219
Cdd:cd03369 141 LKRPRVLVLDEATASIDYATdaliQKTIREEFTNS-----TILTIAHrlrTIID---YDKILVMDAGEV 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-218 |
1.62e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.84 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 25 MNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAH------------------------LNNMKNESK-A 79
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHnlkdinlkwwrskigvvsqdpllfSNSIKNNIKyS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 LY-------------------------RQQMVGFVFQDFNLL-PTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLE 133
Cdd:PTZ00265 484 LYslkdlealsnyynedgndsqenknkRNSCRAKCAGDLNDMsNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHDFVS 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 134 GFLNKY-------PSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTI-LMVTHSNIDA 205
Cdd:PTZ00265 564 ALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTI 643
|
250
....*....|...
gi 487401142 206 SYAErVIFIKDGR 218
Cdd:PTZ00265 644 RYAN-TIFVLSNR 655
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-219 |
4.10e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.91 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNliaSFDGL---TEGDIIVDGAHLN--NMKNESKalyrqqMVGFVFQ---D 92
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFR---HFNGIlkpTSGSVLIRGEPITkeNIREVRK------FVGLVFQnpdD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 93 FNLLPTMtnKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGA 172
Cdd:PRK13652 90 QIFSPTV--EQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487401142 173 LDSKTSKTLMMLFQEI-HQLEQTILMVTHsNID--ASYAERVIFIKDGRL 219
Cdd:PRK13652 168 LDPQGVKELIDFLNDLpETYGMTVIFSTH-QLDlvPEMADYIYVMDKGRI 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-200 |
7.81e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKvygkGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDG--LTEGDIIVDGAHLNNMKNESKA 79
Cdd:CHL00131 7 ILEIKNLHA----SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 80 lyrQQMVGFVFQDFNLLPTMTNKENIMMPLilaGAKRK-------DIEQRVHQLTVQLHLEG----FLNKYPSE-ISGGQ 147
Cdd:CHL00131 83 ---HLGIFLAFQYPIEIPGVSNADFLRLAY---NSKRKfqglpelDPLEFLEIINEKLKLVGmdpsFLSRNVNEgFSGGE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487401142 148 KQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
26-201 |
7.97e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 7.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 26 NLS--VGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDG---------------AHLNNMKneskalyrqqmvgf 88
Cdd:PRK13539 20 GLSftLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdiddpdvaeachylGHRNAMK-------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 89 vfqdfnllPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQlHLEGFLNKYpseISGGQKQRIAIARALVTKPTILLADE 168
Cdd:PRK13539 86 --------PALTVAENLEFWAAFLGGEELDIAAALEAVGLA-PLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 487401142 169 PTGALDSKTSKTLMMLFQEiHqLEQ--TILMVTHS 201
Cdd:PRK13539 154 PTAALDAAAVALFAELIRA-H-LAQggIVIAATHI 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-200 |
8.24e-15 |
|
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: 70.60 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 20 TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskalYRQQMVGFVFQDfNLLPTM 99
Cdd:cd03231 14 ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS----IARGLLYLGHAP-GIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENimmpliLAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSK 179
Cdd:cd03231 89 SVLEN------LRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
170 180
....*....|....*....|.
gi 487401142 180 TLMMLFQEIHQLEQTILMVTH 200
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTH 183
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-207 |
1.26e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALyRQQmVGFVFQDFNLLPTMTN 101
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAL-RQQ-VATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 -KENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKT 180
Cdd:PRK13638 95 iDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180
....*....|....*....|....*..
gi 487401142 181 LMMLFQEIHQLEQTILMVTHsNIDASY 207
Cdd:PRK13638 175 MIAIIRRIVAQGNHVIISSH-DIDLIY 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-201 |
1.47e-14 |
|
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: 73.12 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKglNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnnMKNESKAly 81
Cdd:TIGR01257 1937 ILRLNELTKVYSG--TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDV-- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 rQQMVGFVFQDFNLLPTMTNKENIMMPLILAGAKRKDIEqRVHQLTVQ-LHLEGFLNKYPSEISGGQKQRIAIARALVTK 160
Cdd:TIGR01257 2011 -HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIE-KVANWSIQsLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487401142 161 PTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS 201
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHS 2129
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
4-225 |
2.43e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKGLNA--TTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdgltegdiivdgahlnnmknesKALY 81
Cdd:COG2401 26 RVAIVLEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA------------------------GALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTnkenimmPLILAGAKRKDIEQRVHQLT------VQLhlegFLNKYpSEISGGQKQRIAIAR 155
Cdd:COG2401 82 GTPVAGCVDVPDNQFGREA-------SLIDAIGRKGDFKDAVELLNavglsdAVL----WLRRF-KELSTGQKFRFRLAL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 156 ALVTKPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHSN--IDASYAERVIFIKDGRLYHEIYR 225
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLaRRAGITLVVATHHYdvIDDLQPDLLIFVGYGGVPEEKRR 222
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
22-223 |
2.72e-14 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 69.98 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDG--LTEGDIIVDGAHLNNMKNESKAlyRQQMvgFV-FQDFNLLPT 98
Cdd:TIGR01978 16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKGQDLLELEPDERA--RAGL--FLaFQYPEEIPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 99 MTNKENIMMPLilaGAKRK-------DIEQRVHQLTVQLHL----EGFLNKYPSE-ISGGQKQRIAIARALVTKPTILLA 166
Cdd:TIGR01978 92 VSNLEFLRSAL---NARRSargeeplDLLDFEKLLKEKLALldmdEEFLNRSVNEgFSGGEKKRNEILQMALLEPKLAIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 167 DEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSN--IDASYAERVIFIKDGR--------LYHEI 223
Cdd:TIGR01978 169 DEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQrlLNYIKPDYVHVLLDGRivksgdveLAKEL 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
14-219 |
3.09e-14 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 14 KGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALyrqQMVGFVFQDF 93
Cdd:PRK10895 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 94 NLLPTMTNKENIMMPLILagakRKDI-----EQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADE 168
Cdd:PRK10895 88 SIFRRLSVYDNLMAVLQI----RDDLsaeqrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487401142 169 PTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNIDASYA--ERVIFIKDGRL 219
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDH-NVRETLAvcERAYIVSQGHL 215
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
22-209 |
5.87e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnmknESKALYRQQMVgFVFQDFNLLPTMTN 101
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQLC-FVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 KENIMMPLILAGAKRKdieqrVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTL 181
Cdd:PRK13540 92 RENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|....*...
gi 487401142 182 MMLFQEIHQLEQTILMVTHSNIDASYAE 209
Cdd:PRK13540 167 ITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
26-200 |
6.31e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.29 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 26 NLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNEskalYRQqmvgfvfqdfNLL--------- 96
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQ----------DLLylghqpgik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 97 PTMTNKENIMMPLILAGAKRkdiEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSK 176
Cdd:PRK13538 87 TELTALENLRFYQRLHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170 180
....*....|....*....|....*.
gi 487401142 177 TSKTLMMLFQEiHqLEQ--TILMVTH 200
Cdd:PRK13538 164 GVARLEALLAQ-H-AEQggMVILTTH 187
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
21-220 |
7.56e-14 |
|
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: 70.81 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnnmknESKALYRQQMVGFVFQDFNLLPTMT 100
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKT 180
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487401142 181 LMMLFQEiHQLEQTILMVTHSNIDAS-YAERVIFIKDGRLY 220
Cdd:TIGR01257 1100 IWDLLLK-YRSGRTIIMSTHHMDEADlLGDRIAIISQGRLY 1139
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
27-219 |
2.12e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 67.80 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 27 LSVGAGEFVAIMGESGSGKStlLNLIASFDGL------TEGDIIVDGAHLnnmkneSKALYRQQMVGFVFQD----FNLL 96
Cdd:PRK10418 24 LTLQRGRVLALVGGSGSGKS--LTCAAALGILpagvrqTAGRVLLDGKPV------APCALRGRKIATIMQNprsaFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 97 PTMTN--KENImmpliLAGAKRKDIEQRVHQLT-VQL-HLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGA 172
Cdd:PRK10418 96 HTMHThaRETC-----LALGKPADDATLTAALEaVGLeNAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 173 LDSKTSKTLMMLFQEIHQLEQT-ILMVTHS-NIDASYAERVIFIKDGRL 219
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKRALgMLLVTHDmGVVARLADDVAVMSHGRI 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2-218 |
2.67e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.66 E-value: 2.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGkglnATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASF--DGLTEGDIIVDG--AHLNNMKnES 77
Cdd:NF040905 1 ILEMRGITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGevCRFKDIR-DS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 78 KALyrqqmvGFVF--QDFNLLPTMTNKENIMMplilaG---AKRKDIE-QRVHQLTVQLHLEGFLNKYP----SEISGGQ 147
Cdd:NF040905 76 EAL------GIVIihQELALIPYLSIAENIFL-----GnerAKRGVIDwNETNRRARELLAKVGLDESPdtlvTDIGVGK 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 148 KQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHS-NIDASYAERVIFIKDGR 218
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIRRVADSITVLRDGR 216
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
22-200 |
4.73e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.68 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmkneskalyrQQMVGFVFQDFNLLPTMTN 101
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---------------KLRIGYVPQKLYLDTTLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 KENIMMPLiLAGAKRKDIEQRVHQLTVQLHLEGFLNKypseISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTL 181
Cdd:PRK09544 85 TVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK----LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|
gi 487401142 182 MMLFQEI-HQLEQTILMVTH 200
Cdd:PRK09544 160 YDLIDQLrRELDCAVLMVSH 179
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
12-217 |
4.79e-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: 66.20 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 12 YGKGLnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYRQQMVGFVFQ 91
Cdd:cd03290 10 WGSGL---ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 92 DFNLLpTMTNKENIMM----------PLILAGAKRKDIEQRVHQLTVQLHLEGFlnkypsEISGGQKQRIAIARALVTKP 161
Cdd:cd03290 87 KPWLL-NATVEENITFgspfnkqrykAVTDACSLQPDIDLLPFGDQTEIGERGI------NLSGGQRQRICVARALYQNT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 162 TILLADEPTGALDSKTSKTLMM--LFQEIHQLEQTILMVTHSNIDASYAERVIFIKDG 217
Cdd:cd03290 160 NIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-200 |
5.33e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAS-FDG--LTEGDIIVDGAHLNNMKNESKAlYRQQmvgfvfQDFNLlPT 98
Cdd:TIGR00956 779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErVTTgvITGGDRLVNGRPLDSSFQRSIG-YVQQ------QDLHL-PT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 99 MTNKENIMMPLILAGAKRKDIEQR---VHQLTVQLHLEgflnKYPSEISG--------GQKQRIAIARALVTKPTILL-A 166
Cdd:TIGR00956 851 STVRESLRFSAYLRQPKSVSKSEKmeyVEEVIKLLEME----SYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLLLfL 926
|
170 180 190
....*....|....*....|....*....|....
gi 487401142 167 DEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:TIGR00956 927 DEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
3-240 |
5.97e-13 |
|
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: 66.80 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLNATtaLNQMNLSVGAGEFVAIMGESGSGKSTLLNliaSFDGL--TEGDIIVDGAHLNNMKNES--K 78
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLS---AFLRLlnTEGDIQIDGVSWNSVPLQKwrK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQQMVGFVFQD---FNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLnkypseISGGQKQRIAIAR 155
Cdd:cd03289 78 AFGVIPQKVFIFSGtfrKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCV------LSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 156 ALVTKPTILLADEPTGALDSKTS----KTLMMLFQEIhqleqTILMVTHSNIDASYAERVIFIKDG--RLYHEIYRGEES 229
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYqvirKTLKQAFADC-----TVILSEHRIEAMLECQRFLVIEENkvRQYDSIQKLLNE 226
|
250
....*....|.
gi 487401142 230 QLAFQQRITDS 240
Cdd:cd03289 227 KSHFKQAISPS 237
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-203 |
6.02e-13 |
|
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: 68.01 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKKVYGKG----LNATTA---------LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGlTEGDIIVDG 67
Cdd:TIGR01271 1201 LVIENPHAQKCWPSGgqmdVQGLTAkyteagravLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG 1279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 68 AHLNNMKNESkalYRQQmvgfvfqdFNLLPTMTnkenimmpLILAGAKRKDIE-------QRVHQLTVQLHLEGFLNKYP 140
Cdd:TIGR01271 1280 VSWNSVTLQT---WRKA--------FGVIPQKV--------FIFSGTFRKNLDpyeqwsdEEIWKVAEEVGLKSVIEQFP 1340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 141 SEI-----------SGGQKQRIAIARALVTKPTILLADEPTGALDSKT----SKTLMMLFQEI------HQLE-----QT 194
Cdd:TIGR01271 1341 DKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTlqiiRKTLKQSFSNCtvilseHRVEallecQQ 1420
|
....*....
gi 487401142 195 ILMVTHSNI 203
Cdd:TIGR01271 1421 FLVIEGSSV 1429
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-170 |
7.42e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.84 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 4 EVKHVKKVYGKglnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnNMkneSKALYRQ 83
Cdd:NF033858 3 RLEGVSHRYGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGG---DM---ADARHRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 84 QM---VGFVFQDF--NLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALV 158
Cdd:NF033858 73 AVcprIAYMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170
....*....|..
gi 487401142 159 TKPTILLADEPT 170
Cdd:NF033858 153 HDPDLLILDEPT 164
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-200 |
1.01e-12 |
|
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: 67.27 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 6 KHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDgahlNNMKneskalyrqqm 85
Cdd:TIGR03719 8 NRVSKVVPPK---KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 86 VGFVFQDFNLLPTMTNKENIMM---------------------------PLILAGAKRKDIEQRV--HQLTVQLHLEGFL 136
Cdd:TIGR03719 70 VGYLPQEPQLDPTKTVRENVEEgvaeikdaldrfneisakyaepdadfdKLAAEQAELQEIIDAAdaWDLDSQLEIAMDA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 137 NKYP------SEISGGQKQRIAIARALVTKPTILLADEPTGALDsktSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:TIGR03719 150 LRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESVAWLERHLQEYPGTVVAVTH 216
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-232 |
4.06e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNnmkNESKALYR 82
Cdd:PRK10522 323 LELRNVTFAYQDN---GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGfVFQDFNLLPTMTNKENimmplilAGAKRKDIEQRVHQLTVQ--LHLEG--FLNkypSEISGGQKQRIAIARALV 158
Cdd:PRK10522 397 KLFSA-VFTDFHLFDQLLGPEG-------KPANPALVEKWLERLKMAhkLELEDgrISN---LKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 159 TKPTILLADEPTGALDSKTSKTL-MMLFQEIHQLEQTILMVTHsniDASY---AERVIFIKDGRLYhEIyRGEESQLA 232
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISH---DDHYfihADRLLEMRNGQLS-EL-TGEERDAA 538
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-191 |
5.59e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDG--AHLNNMKNESKAlyrqqMVGFVFQDFNLLPT 98
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGkeVTFNGPKSSQEA-----GIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 99 MTNKENIMM----PLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGAL- 173
Cdd:PRK10762 94 LTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
|
170
....*....|....*...
gi 487401142 174 DSKTSKtlmmLFQEIHQL 191
Cdd:PRK10762 174 DTETES----LFRVIREL 187
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-217 |
6.71e-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: 64.97 E-value: 6.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAH-----LNNMKNESKALYRQQMVGFVFQDFNLL 96
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakigLHDLRFKITIIPQDPVLFSGSLRMNLD 1381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 97 P-TMTNKENIMMPLILAgakrkdieqrvhqltvqlHLEGFLNKYPSEI-----------SGGQKQRIAIARALVTKPTIL 164
Cdd:TIGR00957 1382 PfSQYSDEEVWWALELA------------------HLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 165 LADEPTGALDSKTSKTLMMLFQEihQLEQ-TILMVTHS-NIDASYAeRVIFIKDG 217
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTIRT--QFEDcTVLTIAHRlNTIMDYT-RVIVLDKG 1495
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
2-200 |
8.67e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.05 E-value: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVKKVYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKStllnLIA-SFDGLTEGD--IIVDGAHLNN---MKN 75
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKS----LIAkAICGVTKDNwrVTADRMRFDDidlLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 76 ESKAlyRQQMVG----FVFQDFN--LLPTmtnkENIMMPLILA---------------GAKRKDIEQrVHQLTVQLHlEG 134
Cdd:PRK15093 79 SPRE--RRKLVGhnvsMIFQEPQscLDPS----ERVGRQLMQNipgwtykgrwwqrfgWRKRRAIEL-LHRVGIKDH-KD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 135 FLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ-TILMVTH 200
Cdd:PRK15093 151 AMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNtTILLISH 217
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-200 |
1.04e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.15 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 32 GEFVAIMGESGSGKSTLLNLIAS--------FDGLTEGDIIVD---GAHLNN----MKNES-KALYRQQMVgfvfqdfNL 95
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDefrGSELQNyftkLLEGDvKVIVKPQYV-------DL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 LPTmTNKENIMMPLilagaKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDS 175
Cdd:cd03236 99 IPK-AVKGKVGELL-----KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*
gi 487401142 176 KTSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-232 |
2.00e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 63.11 E-value: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdgltegdiivdGAHLNNMKNESKALYRQ-----------QMVGFV- 89
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT-------------GDHPQGYSNDLTLFGRRrgsgetiwdikKHIGYVs 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 90 ---FQDFNLLPTMTNkenimmpLILAG-----AKRKDIEQRVHQLTVQ----LHLEGFLNKYP-SEISGGQkQRIA-IAR 155
Cdd:PRK10938 343 sslHLDYRVSTSVRN-------VILSGffdsiGIYQAVSDRQQKLAQQwldiLGIDKRTADAPfHSLSWGQ-QRLAlIVR 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 156 ALVTKPTILLADEPTGALDSkTSKTLMMLFQE--IHQLEQTILMVTHSNIDA--SYAERVIFIKDGrlyhEIYRGEESQL 231
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDP-LNRQLVRRFVDvlISEGETQLLFVSHHAEDApaCITHRLEFVPDG----DIYRYVQTKL 489
|
.
gi 487401142 232 A 232
Cdd:PRK10938 490 N 490
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-219 |
2.80e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 62.99 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGlnatTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdglteGDIIVDGAHLNNMKNESKALYR 82
Cdd:PRK15064 320 LEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVKWSENANIGYYA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFNLLPTMTNkenimmplilaGAKRKDIEQRVHQ-LTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKP 161
Cdd:PRK15064 389 QDHAYDFENDLTLFDWMSQ-----------WRQEGDDEQAVRGtLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 162 TILLADEPTGALDSKTSKTLMMLFQeihQLEQTILMVTHsniD----ASYAERVIFIKDGRL 219
Cdd:PRK15064 458 NVLVMDEPTNHMDMESIESLNMALE---KYEGTLIFVSH---DrefvSSLATRIIEITPDGV 513
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-212 |
3.82e-11 |
|
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: 61.27 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEF-----VAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYR---QQMVGFVFQDF 93
Cdd:cd03237 10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEgtvRDLLSSITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 94 NLLPTMtnKENIMMPlilagakrkdieqrvhqltvqLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGAL 173
Cdd:cd03237 90 YTHPYF--KTEIAKP---------------------LQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 487401142 174 DSK----TSKTLMMLfqeIHQLEQTILMVTHSNIDASY-AERVI 212
Cdd:cd03237 147 DVEqrlmASKVIRRF---AENNEKTAFVVEHDIIMIDYlADRLI 187
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-219 |
1.14e-10 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLN-LIASFDGLTEGDIIVDGAHLNnMKNESKALyrQQMVGFVFQD---FNLLP 97
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVD-IRNPAQAI--RAGIAMVPEDrkrHGIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 TMTNKENIMMPLILAGAKRKDIEQRVHQLTV-----QLHLEGFLNKYP-SEISGGQKQRIAIARALVTKPTILLADEPTG 171
Cdd:TIGR02633 353 ILGVGKNITLSVLKSFCFKMRIDAAAELQIIgsaiqRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 487401142 172 ALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVlGLSDRVLVIGEGKL 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-168 |
1.84e-10 |
|
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: 60.58 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 26 NLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAHLNnmkNESKALYRQQmvgF--VFQDFNLLPTmt 100
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLT---GLyrpESGEILLDGQPVT---ADNREAYRQL---FsaVFSDFHLFDR-- 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 101 nkenimmpliLAGAKRKDIEQRVHQLTVQLHLEG--------FLNKypsEISGGQKQRIAIARALVTKPTILLADE 168
Cdd:COG4615 421 ----------LLGLDGEADPARARELLERLELDHkvsvedgrFSTT---DLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-200 |
2.37e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnNMKNESKALyrQQMVGFVFQDFNLLptmt 100
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEAL--ENGISMVHQELNLV---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMMPLILAGAKRKDI---EQRVHQLTVQLHLEGFLNKYPSE----ISGGQKQRIAIARALVTKPTILLADEPTGAL 173
Cdd:PRK10982 86 LQRSVMDNMWLGRYPTKGMfvdQDKMYRDTKAIFDELDIDIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190
....*....|....*....|....*....|
gi 487401142 174 dskTSKTLMMLFQEIHQLEQT---ILMVTH 200
Cdd:PRK10982 166 ---TEKEVNHLFTIIRKLKERgcgIVYISH 192
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-177 |
2.51e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdglteGDIIVDGAHLNNMKNESKALYRQ----QMVGFVFqDF---- 93
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILN-------GEVLLDDGRIIYEQDLIVARLQQdpprNVEGTVY-DFvaeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 94 ---------------NLLPTMTNKENI--MMPL--ILAGAKRKDIEQRVHQLTVQLHLEGflNKYPSEISGGQKQRIAIA 154
Cdd:PRK11147 91 ieeqaeylkryhdisHLVETDPSEKNLneLAKLqeQLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALG 168
|
170 180
....*....|....*....|...
gi 487401142 155 RALVTKPTILLADEPTGALDSKT 177
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIET 191
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-201 |
2.56e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 2.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmkneSKALyrqqmvgfVFQDFNLLPTMT 100
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---------SAAL--------IAISSGLNGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKT 180
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180
....*....|....*....|.
gi 487401142 181 LMMLFQEIHQLEQTILMVTHS 201
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHS 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-214 |
2.84e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.34 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLN-LIASFDGLtEGDIIVDG--------AHLNNMKNESKALYRQQM----VGF 88
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVHMKGsvayvpqqAWIQNDSLRENILFGKALnekyYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 89 VFQDFNLLPTMTnkenimmplILAGAKRKDIEQRVHQLtvqlhlegflnkypseiSGGQKQRIAIARALVTKPTILLADE 168
Cdd:TIGR00957 733 VLEACALLPDLE---------ILPSGDRTEIGEKGVNL-----------------SGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487401142 169 PTGALDSKTSKtlmMLFQEIHQLE-----QTILMVTHSnidASYAERVIFI 214
Cdd:TIGR00957 787 PLSAVDAHVGK---HIFEHVIGPEgvlknKTRILVTHG---ISYLPQVDVI 831
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-174 |
4.96e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 58.88 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 2 LLEVKHVkkvYGKGLNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDIIVDGAhlnNMKNESK 78
Cdd:COG3845 257 VLEVENL---SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALA---GLrppASGSIRLDGE---DITGLSP 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 79 ALYRQQMVGFVFQD---FNLLPTMTNKENIMM-----------PLILAGAKRKDIEQRVHQLTVqlhlegflnKYPSE-- 142
Cdd:COG3845 328 RERRRLGVAYIPEDrlgRGLVPDMSVAENLILgryrrppfsrgGFLDRKAIRAFAEELIEEFDV---------RTPGPdt 398
|
170 180 190
....*....|....*....|....*....|....*.
gi 487401142 143 ----ISGGQKQRIAIARALVTKPTILLADEPTGALD 174
Cdd:COG3845 399 parsLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-226 |
8.98e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.58 E-value: 8.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAS----FDGLTEGDIIVDGAHLNNMKNEskalYRQQMVgFVFQDFNLLP 97
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKKH----YRGDVV-YNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 TMTNKENimmpLILAgAKRKDIEQRVHQLTVQLHLEGFL------------------NKYPSEISGGQKQRIAIARALVT 159
Cdd:TIGR00956 152 HLTVGET----LDFA-ARCKTPQNRPDGVSREEYAKHIAdvymatyglshtrntkvgNDFVRGVSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 160 KPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHSNIDASYA--ERVIFIKDGRlyhEIYRG 226
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKTSaNILDTTPLVAIYQCSQDAYElfDKVIVLYEGY---QIYFG 293
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-219 |
1.06e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 57.13 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnnmkneskalyrqqmVGFVFQDFNLLPTMT 100
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAISAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKT 180
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 487401142 181 LMMLFQEIHQLEQTILMVTHsNIDA--SYAERVIFIKDGRL 219
Cdd:PRK13546 182 CLDKIYEFKEQNKTIFFVSH-NLGQvrQFCTKIAWIEGGKL 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-218 |
1.79e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 32 GEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDgahlnnmkneskalyrqqmvgfvfqdfnllptmtnkenimmplil 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 112 agakrkDIEQRVHQLTVQLHLEGFLNKYPSeISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLM------MLF 185
Cdd:smart00382 37 ------DGEDILEEVLDQLLLIIVGGKKAS-GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLLL 109
|
170 180 190
....*....|....*....|....*....|....*....
gi 487401142 186 QEIHQLEQTILMVTH------SNIDASYAERVIFIKDGR 218
Cdd:smart00382 110 LLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLIL 148
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
16-198 |
2.76e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 16 LNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKalyrQQMVGFVFQDFN- 94
Cdd:PRK10938 13 LSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL----QKLVSDEWQRNNt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 95 --LLPTMTNKENIMMPLILAGAKRkdiEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGA 172
Cdd:PRK10938 89 dmLSPGEDDTGRTTAEIIQDEVKD---PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180
....*....|....*....|....*.
gi 487401142 173 LDSKTSKTLMMLFQEIHQLEQTILMV 198
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLV 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
23-174 |
4.81e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 4.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 23 NQMNLSVGAGEFVAIMGESGSGKSTLLN-LIASFDGLTEGDIIVDGAHLNnMKNESKALyrQQMVGFVFQD---FNLLPT 98
Cdd:PRK13549 279 DDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVK-IRNPQQAI--AQGIAMVPEDrkrDGIVPV 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 99 MTNKENIMMP---------LILAGAKRKDIEQRVHQLTVqlhlegflnKYPS------EISGGQKQRIAIARALVTKPTI 163
Cdd:PRK13549 356 MGVGKNITLAaldrftggsRIDDAAELKTILESIQRLKV---------KTASpelaiaRLSGGNQQKAVLAKCLLLNPKI 426
|
170
....*....|.
gi 487401142 164 LLADEPTGALD 174
Cdd:PRK13549 427 LILDEPTRGID 437
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-182 |
6.60e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.01 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 32 GEFVAIMGESGSGKSTLLNLIA--SFDGLTEGDIIVDGAhlnNMKNESKAlyrqQMVGFVFQDFNLLPTMTNKENIMMPL 109
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGF---PKKQETFA----RISGYCEQNDIHSPQVTVRESLIYSA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 110 ILAGAKRKDIEQR---VHQLTVQLHLEGFLNK---YP--SEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTL 181
Cdd:PLN03140 979 FLRLPKEVSKEEKmmfVDEVMELVELDNLKDAivgLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIV 1058
|
.
gi 487401142 182 M 182
Cdd:PLN03140 1059 M 1059
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-200 |
1.65e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 6 KHVKKVYGKGlnaTTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIV-DGAHlnnmkneskalyrqq 84
Cdd:PRK11819 10 NRVSKVVPPK---KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGIK--------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 85 mVGFVFQDFNLLPTMTNKENIMMPL------------------------------------ILAGAKRKDIEQRVHQLTV 128
Cdd:PRK11819 72 -VGYLPQEPQLDPEKTVRENVEEGVaevkaaldrfneiyaayaepdadfdalaaeqgelqeIIDAADAWDLDSQLEIAMD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 129 QLHLegflnkyP------SEISGGQKQRIAIARALVTKPTILLADEPTGALDsktSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:PRK11819 151 ALRC-------PpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD---AESVAWLEQFLHDYPGTVVAVTH 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-174 |
1.66e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 17 NATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKNESKALYRQQMVGfvfqdfnLL 96
Cdd:PRK13543 22 NEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPG-------LK 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 97 PTMTNKENIMMPLILAGAKRKDIEQrvHQLTVqLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALD 174
Cdd:PRK13543 95 ADLSTLENLHFLCGLHGRRAKQMPG--SALAI-VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
3-230 |
1.75e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKkvyGKGLNattalnQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNmKNESKALyr 82
Cdd:PRK10762 258 LKVDNLS---GPGVN------DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT-RSPQDGL-- 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 83 QQMVGFVFQDFN---LLPTMTNKENimMPLI-------LAGAKRKDIEQrvhqLTVQLHLEGFLNKYPS------EISGG 146
Cdd:PRK10762 326 ANGIVYISEDRKrdgLVLGMSVKEN--MSLTalryfsrAGGSLKHADEQ----QAVSDFIRLFNIKTPSmeqaigLLSGG 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 147 QKQRIAIARALVTKPTILLADEPTGALDSKTSKTlmmLFQEIHQLEQ---TILMVTHSNIDA-SYAERVIFIKDGRLYHE 222
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKE---IYQLINQFKAeglSIILVSSEMPEVlGMSDRILVMHEGRISGE 476
|
....*...
gi 487401142 223 IYRGEESQ 230
Cdd:PRK10762 477 FTREQATQ 484
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-228 |
1.83e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 23 NQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAhlnNMKNESKALYRQQMVGFVFQ---DFNLLPTM 99
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK---DISPRSPLDAVKKGMAYITEsrrDNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENI-------------MMPLILAGAKRKDIEQRVHQLTVQLHLegfLNKYPSEISGGQKQRIAIARALVTKPTILLA 166
Cdd:PRK09700 357 SIAQNMaisrslkdggykgAMGLFHEVDEQRTAENQRELLALKCHS---VNQNITELSGGNQQKVLISKWLCCCPEVIIF 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487401142 167 DEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNID-ASYAERVIFIKDGRLYHEIYRGEE 228
Cdd:PRK09700 434 DEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEiITVCDRIAVFCEGRLTQILTNRDD 496
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-170 |
1.92e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 20 TALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIAsfdGL---TEGDiivdgAHL-------NNMKNeskalyRQQmVGFV 89
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLT---GLlpaSEGE-----AWLfgqpvdaGDIAT------RRR-VGYM 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 90 FQDFNLLPTMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEP 169
Cdd:NF033858 345 SQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
.
gi 487401142 170 T 170
Cdd:NF033858 425 T 425
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-214 |
2.72e-08 |
|
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: 51.94 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 21 ALNQMNLSVGAGEFVAIMGESGSGKSTLLnliasFDGLTegdiivdgAHLNNMKNESKALYRQQMVGFVFQdfnlLPTMT 100
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLV-----NEGLY--------ASGKARLISFLPKFSRNKLIFIDQ----LQFLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMMPLilagakrkdieqrvhqltvqlhlegflNKYPSEISGGQKQRIAIARALV--TKPTILLADEPTGALDSKTS 178
Cdd:cd03238 73 DVGLGYLTL---------------------------GQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDI 125
|
170 180 190
....*....|....*....|....*....|....*.
gi 487401142 179 KTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFI 214
Cdd:cd03238 126 NQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-219 |
3.05e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.29 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASfdGLTE----------GDIIVDGAHLNNMKNESKALYR-----QQMV 86
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAPRLARLRavlpqAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 87 GFVF--QDFNLL-----------PTMTNKENIMMPLILAGAK---RKDIeqrvhqltvqlhlegflnkypSEISGGQKQR 150
Cdd:PRK13547 95 AFAFsaREIVLLgrypharragaLTHRDGEIAWQALALAGATalvGRDV---------------------TTLSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 151 IAIARAL---------VTKPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILMVTHS-NIDASYAERVIFIKDGRL 219
Cdd:PRK13547 154 VQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDpNLAARHADRIAMLADGAI 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-222 |
4.46e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.59 E-value: 4.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLN-LIASFDGLTEGDIIVDGahlnnmknesKALYRQQmVGFVFQdfnllptMT 100
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG----------TVAYVPQ-VSWIFN-------AT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMMPLILAGAKrkdIEQRVHQLTVQLHLEGFLNKYPSEI-------SGGQKQRIAIARALVTKPTILLADEPTGAL 173
Cdd:PLN03130 695 VRDNILFGSPFDPER---YERAIDVTALQHDLDLLPGGDLTEIgergvniSGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 487401142 174 DSKTSKTLM--MLFQEIHQleQTILMVTHSNIDASYAERVIFIKDGRLYHE 222
Cdd:PLN03130 772 DAHVGRQVFdkCIKDELRG--KTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-179 |
5.26e-08 |
|
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: 52.55 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 16 LNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGahlnnmkneskalyrqqMVGFVFQDFNL 95
Cdd:cd03291 47 LVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----------------RISFSSQFSWI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 LPTmTNKENIMMPLILAgakrkdiEQRVHQLTVQLHLEGFLNKYPSE-----------ISGGQKQRIAIARALVTKPTIL 164
Cdd:cd03291 110 MPG-TIKENIIFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLY 181
|
170
....*....|....*
gi 487401142 165 LADEPTGALDSKTSK 179
Cdd:cd03291 182 LLDSPFGYLDVFTEK 196
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-179 |
8.54e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 16 LNATTALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIivdgahlnnmKNESKALYRQQmvgfvfqdFNL 95
Cdd:TIGR01271 436 LYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------KHSGRISFSPQ--------TSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 LPTMTNKENIMMPLILAgakrkdiEQRVHQLTVQLHLEGFLNKYPSE-----------ISGGQKQRIAIARALVTKPTIL 164
Cdd:TIGR01271 498 IMPGTIKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLY 570
|
170
....*....|....*
gi 487401142 165 LADEPTGALDSKTSK 179
Cdd:TIGR01271 571 LLDSPFTHLDVVTEK 585
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-222 |
1.58e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLN-LIASFDGLTEGDIIVDGAhlnnmkneskALYRQQmVGFVFQdfnllptMT 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS----------VAYVPQ-VSWIFN-------AT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENImmpliLAGAKRKDIE--QRVHQLTVQLHLEGFLNKYPSEI-------SGGQKQRIAIARALVTKPTILLADEPTG 171
Cdd:PLN03232 695 VRENI-----LFGSDFESERywRAIDVTALQHDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLS 769
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 487401142 172 ALDSKTSKtlmMLFQEI--HQLE-QTILMVTHSNIDASYAERVIFIKDGRLYHE 222
Cdd:PLN03232 770 ALDAHVAH---QVFDSCmkDELKgKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-219 |
1.67e-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: 50.68 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 17 NATTALNQMNLSVGAGEFVAIMGESGSGKSTL----LNLIASFDGltegDIIVDGAHLNNMKneskalyrqqmvgfvfqd 92
Cdd:cd03288 32 NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFDG----KIVIDGIDISKLP------------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 93 fnlLPTMTNKENIMM--PLILAGAKRKDIEQR-------------VHQLTVQLH-LEGFLNKYPSE----ISGGQKQRIA 152
Cdd:cd03288 90 ---LHTLRSRLSIILqdPILFSGSIRFNLDPEckctddrlwealeIAQLKNMVKsLPGGLDAVVTEggenFSVGQRQLFC 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 487401142 153 IARALVTKPTILLADEPTGALDSKT----SKTLMMLFQeihqlEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATenilQKVVMTAFA-----DRTVVTIAHRVSTILDADLVLVLSRGIL 232
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-219 |
3.77e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 3.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLL-NLIASFDgLTEGDIIVDgahlnnmknESKALYRQQMvgfvfqdfnLLPTMT 100
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFE-ISEGRVWAE---------RSIAYVPQQA---------WIMNAT 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 101 NKENIMM-----PLILAGAKR-KDIEQRVHQLTVQLHLEgfLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALD 174
Cdd:PTZ00243 737 VRGNILFfdeedAARLADAVRvSQLEADLAQLGGGLETE--IGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 487401142 175 SKTSKTLMmlfQEI---HQLEQTILMVTHSNIDASYAERVIFIKDGRL 219
Cdd:PTZ00243 815 AHVGERVV---EECflgALAGKTRVLATHQVHVVPRADYVVALGDGRV 859
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
98-219 |
3.94e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 98 TMTNKENIMMPLILAGAKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKT 177
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 487401142 178 SKTLMMLFQEIHQLEQTILMVTHSNIDA-SYAERVIFIKDGRL 219
Cdd:NF000106 180 RNEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVIDRGRV 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-199 |
8.52e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVkkvygkglnatTALNQ-----MNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMK- 74
Cdd:PRK10982 249 VILEVRNL-----------TSLRQpsirdVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNa 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 75 ----NESKALYRQQ-----MVGFVFQDFNLLptMTNKENIMMPLILAGAKR--KDIEQRVHQLTVqlhlegflnKYPSE- 142
Cdd:PRK10982 318 neaiNHGFALVTEErrstgIYAYLDIGFNSL--ISNIRNYKNKVGLLDNSRmkSDTQWVIDSMRV---------KTPGHr 386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487401142 143 -----ISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVT 199
Cdd:PRK10982 387 tqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
22-200 |
1.26e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 48.25 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDG--LTEGDIIVDGAHLNNMKNESKAlyrQQMVGFVFQDFNLLPTM 99
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELSPEDRA---GEGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 100 TNKENIMMPLILAGAKRKD-----------IEQRVHQLTVQLHL------EGFlnkypseiSGGQKQRIAIARALVTKPT 162
Cdd:PRK09580 94 SNQFFLQTALNAVRSYRGQepldrfdfqdlMEEKIALLKMPEDLltrsvnVGF--------SGGEKKRNDILQMAVLEPE 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 487401142 163 ILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-200 |
2.59e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 35 VAIMGESGSGKSTLLNLIAsfdglteGDIIVDGAHLNNMKNESKALYRQQMVGFVfqDFNLLPTMtnkeniMMPLILAGA 114
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLIS-------GELQPSSGTVFRSAKVRMAVFSQHHVDGL--DLSSNPLL------YMMRCFPGV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 115 KrkdiEQRVHQLTVQLHLEGFLNKYPS-EISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTL---MMLFQeihq 190
Cdd:PLN03073 603 P----EQKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALiqgLVLFQ---- 674
|
170
....*....|
gi 487401142 191 leQTILMVTH 200
Cdd:PLN03073 675 --GGVLMVSH 682
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-200 |
2.82e-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: 47.86 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 32 GEFVAIMGESGSGKSTLLNLIA--------SFDGLTEGDIIVD-------GAHLNNMKN-ESKALYRQQMVGFVFQDFN- 94
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSgelkpnlgDYDEEPSWDEVLKrfrgtelQDYFKKLANgEIKVAHKPQYVDLIPKVFKg 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 95 ----LLptmtnkenimmplilagaKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:COG1245 179 tvreLL------------------EKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|
gi 487401142 171 GALDSKTSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-181 |
3.27e-06 |
|
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: 47.62 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 3 LEVKHVKKVYGKGLnattALNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIV-DGAHLNNMKNESKALY 81
Cdd:TIGR03719 323 IEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQSRDALD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 82 RQQMVGFVFQDFNLLPTMTNKEniMMPLILAGA---KRKDIEQRVHQLtvqlhlegflnkypseiSGGQKQRIAIARALV 158
Cdd:TIGR03719 399 PNKTVWEEISGGLDIIKLGKRE--IPSRAYVGRfnfKGSDQQKKVGQL-----------------SGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|...
gi 487401142 159 TKPTILLADEPTGALDSKTSKTL 181
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRAL 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-175 |
8.88e-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: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAG-----EFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDgahlnnmkneSKALYRQQmvgFVFQDFNll 96
Cdd:COG1245 351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED----------LKISYKPQ---YISPDYD-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 97 ptMTNKENImmplilagakRKDIEQRV------HQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:COG1245 416 --GTVEEFL----------RSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
....*
gi 487401142 171 GALDS 175
Cdd:COG1245 484 AHLDV 488
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
22-173 |
1.03e-05 |
|
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: 46.28 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDgahlnnmkNESKALYRQQMvgfvfqdfnllPTMTN 101
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP--------AKGKLFYVPQR-----------PYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 ---KENIMMPLILAGAKRKDI-EQRVHQLTVQLHLEGFLNK---------YPSEISGGQKQRIAIARALVTKPTILLADE 168
Cdd:TIGR00954 529 gtlRDQIIYPDSSEDMKRRGLsDKDLEQILDNVQLTHILEReggwsavqdWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
....*
gi 487401142 169 PTGAL 173
Cdd:TIGR00954 609 CTSAV 613
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-233 |
2.23e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 25 MNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKN----ESKALY----RQQmvGFVFQD---- 92
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlARGLVYlpedRQS--SGLYLDapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 93 FNLLPTMTNKenimMPLILAGAKRKDIEQRVH-QLTVQL-HLEgflnKYPSEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:PRK15439 360 WNVCALTHNR----RGFWIKPARENAVLERYRrALNIKFnHAE----QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 171 GALDSKTSKTLMMLFQEIHQLEQTILMVThSNID--ASYAERVIFIKDGRLYHEIYRGEES-----QLAF 233
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIAAQNVAVLFIS-SDLEeiEQMADRVLVMHQGEISGALTGAAINvdtimRLAF 500
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
143-197 |
2.67e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.22 E-value: 2.67e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 143 ISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTLMMLFQEI-HQLEQTILM 197
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIvHLTEATVLM 392
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-243 |
3.32e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 44.52 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 1 MLLEVKHVKkvyGKGLNATtalnqMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLnNMKNESKAL 80
Cdd:PRK11288 256 VRLRLDGLK---GPGLREP-----ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-DIRSPRDAI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 81 yRQQMV---------GFVfqdfnllPTMTNKENIMMP----------LILAGAKRKDIEQRVHQLTVqlhlegflnKYPS 141
Cdd:PRK11288 327 -RAGIMlcpedrkaeGII-------PVHSVADNINISarrhhlragcLINNRWEAENADRFIRSLNI---------KTPS 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 142 ------EISGGQKQRIAIARALVTKPTILLADEPTGALD--SKTSktlmmLFQEIHQLEQ---TILMVThSNIDA--SYA 208
Cdd:PRK11288 390 reqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE-----IYNVIYELAAqgvAVLFVS-SDLPEvlGVA 463
|
250 260 270
....*....|....*....|....*....|....*
gi 487401142 209 ERVIFIKDGRLYHEIYRGEesqlAFQQRITdSLAL 243
Cdd:PRK11288 464 DRIVVMREGRIAGELAREQ----ATERQAL-SLAL 493
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
144-201 |
3.76e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 3.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 144 SGGQKQRIAIARALVTKPTILLADEPTGALDSKTsktlmMLFQEIHQLE--QTILMVTHS 201
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA-----VLWLETYLLKwpKTFIVVSHA 400
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-212 |
4.75e-05 |
|
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: 42.94 E-value: 4.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487401142 142 EISGGQKQRIAIARALVTKPTILLADEPTGALDSK----TSKTLMMLFQEIhqlEQTILMVTHSNIDASY-AERVI 212
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEG---KKTALVVEHDLAVLDYlSDRIH 143
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
22-202 |
5.99e-05 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 42.74 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIvdgahlnNMKNESKALYRQQMVgfvfqdfnlLPTMTN 101
Cdd:PRK15177 3 LDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDFI-------GLRGDALPLGANSFI---------LPGLTG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 102 KENIMMPLILAGAKRKDIEQRVHQLTvqlHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSktL 181
Cdd:PRK15177 67 EENARMMASLYGLDGDEFSHFCYQLT---QLEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADGKLYTGDNATQ--L 141
|
170 180
....*....|....*....|.
gi 487401142 182 MMLFQEIHQLEQTILMVTHSN 202
Cdd:PRK15177 142 RMQAALACQLQQKGLIVLTHN 162
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-177 |
8.49e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 43.57 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNM--KNESKALyrqqmvGFVFQD------- 92
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFglMDLRKVL------GIIPQApvlfsgt 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 93 --FNLLPTMTNKENIMMPlILAGAKRKDIEQRVhqltvQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPT 170
Cdd:PLN03130 1329 vrFNLDPFNEHNDADLWE-SLERAHLKDVIRRN-----SLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
....*..
gi 487401142 171 GALDSKT 177
Cdd:PLN03130 1403 AAVDVRT 1409
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
37-181 |
1.09e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 37 IMGESGSGKSTLLNLIASFDGLTEGDIIVDGAHLNNMKneskalyrQQMVGFVFQDFNLLPTMTNKENIMMplilaGAKR 116
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--------KPYCTYIGHNLGLKLEMTVFENLKF-----WSEI 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 117 KDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALDSKTSKTL 181
Cdd:PRK13541 98 YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-174 |
1.18e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 32 GEFVAIMGESGSGKSTLLNLIA--------SFDGLTEGDIIVD---GAHLNN-----MKNESKALYRQQMVgfvfqdfNL 95
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSgelipnlgDYEEEPSWDEVLKrfrGTELQNyfkklYNGEIKVVHKPQYV-------DL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 96 LPTM---TNKEnimmplILagaKRKDIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGA 172
Cdd:PRK13409 172 IPKVfkgKVRE------LL---KKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
..
gi 487401142 173 LD 174
Cdd:PRK13409 243 LD 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
143-236 |
1.98e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.24 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 143 ISGGQKQRIAIARaLVTKPTILLA-DEPTGALDsktSKTLMMLFQEIHQLEQTILMVTHSN--IDASYAERVIFIKDGRL 219
Cdd:PRK11147 441 LSGGERNRLLLAR-LFLKPSNLLIlDEPTNDLD---VETLELLEELLDSYQGTVLLVSHDRqfVDNTVTECWIFEGNGKI 516
|
90 100
....*....|....*....|...
gi 487401142 220 ------YHEiyrgeesqlAFQQR 236
Cdd:PRK11147 517 gryvggYHD---------ARQQQ 530
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-174 |
2.37e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.10 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 32 GEFVAIMGESGSGKSTLLNLIASFDGLTEGDIIVDgahlnnmkneSKALYRQQmvgFVFQDFNllptMTNKEnimmplIL 111
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE----------LKISYKPQ---YIKPDYD----GTVED------LL 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487401142 112 AGAKRK-DIEQRVHQLTVQLHLEGFLNKYPSEISGGQKQRIAIARALVTKPTILLADEPTGALD 174
Cdd:PRK13409 422 RSITDDlGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
141-200 |
2.60e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 2.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 141 SEISGGQKQRIAIARALVTKPTILLADEPTGALDsktSKTLMMLFQEIHQLEQTILMVTH 200
Cdd:PRK15064 154 SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD---INTIRWLEDVLNERNSTMIIISH 210
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
119-201 |
3.14e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 119 IEQRVHQL-TVQL-HLEgfLNKYPSEISGGQKQRIAIARAL---VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQ 193
Cdd:PRK00635 786 IHEKIHALcSLGLdYLP--LGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH 863
|
....*...
gi 487401142 194 TILMVTHS 201
Cdd:PRK00635 864 TVVIIEHN 871
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
143-217 |
4.34e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487401142 143 ISGGQKQRIAIARAL---VTKPTILLaDEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAERVIFIKDG 217
Cdd:PRK00635 477 LSGGEQERTALAKHLgaeLIGITYIL-DEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPG 553
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-174 |
4.71e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 17 NATTALNqmnlsvgAGEFVAIMGESGSGKSTLLNLIasfdgltEGDIIVDGAHLNNMKNESKALYRQQM-------VGFV 89
Cdd:PRK10636 19 NATATIN-------PGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQLAWVNQETpalpqpaLEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 90 ------FQDFNLLPTMTNKENIMMPLILAGAKRKDIeqrvHQLTVQ------LHLEGF----LNKYPSEISGGQKQRIAI 153
Cdd:PRK10636 85 idgdreYRQLEAQLHDANERNDGHAIATIHGKLDAI----DAWTIRsraaslLHGLGFsneqLERPVSDFSGGWRMRLNL 160
|
170 180
....*....|....*....|.
gi 487401142 154 ARALVTKPTILLADEPTGALD 174
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLD 181
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
21-65 |
7.19e-04 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 40.40 E-value: 7.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 487401142 21 ALNQMnLSVGAGEFVAIMGESGSGKSTLLNLIASFdglTEGDIIV 65
Cdd:COG1157 147 AIDGL-LTVGRGQRIGIFAGSGVGKSTLLGMIARN---TEADVNV 187
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
143-204 |
8.15e-04 |
|
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: 40.38 E-value: 8.15e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 487401142 143 ISGGQKQRIAIARAL---VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNID 204
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH-NLD 893
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
27-65 |
1.54e-03 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 39.08 E-value: 1.54e-03
10 20 30
....*....|....*....|....*....|....*....
gi 487401142 27 LSVGAGEFVAIMGESGSGKSTLLNLIASFdglTEGDIIV 65
Cdd:cd01136 62 LTCGEGQRIGIFAGSGVGKSTLLGMIARN---TDADVNV 97
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
141-204 |
2.07e-03 |
|
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: 38.36 E-value: 2.07e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 487401142 141 SEISGGQKQRIAIARAL---VTKPTILLADEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHsNID 204
Cdd:cd03271 168 TTLSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEH-NLD 233
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
32-50 |
3.28e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 38.52 E-value: 3.28e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
22-50 |
3.50e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.50e-03
10 20
....*....|....*....|....*....
gi 487401142 22 LNQMNLSVGAGEFVAIMGESGSGKSTLLN 50
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
31-63 |
5.07e-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: 36.99 E-value: 5.07e-03
10 20 30
....*....|....*....|....*....|...
gi 487401142 31 AGEFVAIMGESGSGKSTLLNLIASFDGLTEGDI 63
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLATGEI 116
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
64-215 |
7.13e-03 |
|
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: 36.18 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 64 IVDGAHLNNMkneskalyRQQMVGFVFQDFNLL--PTMTNKENIM--MPLILAGA-----KRKDIEQRVHQLTVQLHLEG 134
Cdd:cd03227 2 IVLGRFPSYF--------VPNDVTFGEGSLTIItgPNGSGKSTILdaIGLALGGAqsatrRRSGVKAGCIVAAVSAELIF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487401142 135 FLnkypSEISGGQKQRIAIARALV---TKPTILLA-DEPTGALDSKTSKTLMMLFQEIHQLEQTILMVTHSNIDASYAER 210
Cdd:cd03227 74 TR----LQLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADK 149
|
....*
gi 487401142 211 VIFIK 215
Cdd:cd03227 150 LIHIK 154
|
|
| |
