|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-204 |
8.50e-100 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 288.82 E-value: 8.50e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNL---LG 77
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLrrkVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 158 DEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVV 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-204 |
6.83e-88 |
|
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: 257.84 E-value: 6.83e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNL---LGF 78
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELrqkVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 159 EPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-204 |
6.59e-83 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 250.02 E-value: 6.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHL--ENRNlLGF 78
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD--VTGLppEKRN-VGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRM-RGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 159 EPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG3842 161 EPLSALDAKLREEMREELRRlQRELGITFIYVTHDQEEALALADRIA 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-206 |
5.60e-80 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 238.02 E-value: 5.60e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQK----TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG------IDHL 70
Cdd:COG1136 4 LLELRNLTKSYGTGegevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslsereLARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 ENRNLlGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:COG1136 84 RRRHI-GFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAeAISDRIIRV 206
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVTHDPELA-ARADRVIRL 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-205 |
3.02e-79 |
|
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: 235.85 E-value: 3.02e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQ----KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV------GIDHLE 71
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 72 NRNLlGFVFQDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMID 151
Cdd:cd03255 81 RRHI-GFVFQSFNLLPDLTALENVELPLLLA-GVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 152 PQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEaISDRIIR 205
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDPELAE-YADRIIE 212
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-207 |
8.30e-79 |
|
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: 233.23 E-value: 8.30e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV---GIDHLENRNLLGF 78
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTlsptitmgkqkadakekaldllarlglkehaqvypYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:cd03229 81 VFQDFALFPHLTVLENIA-----------------------------------LGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 159 EPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd03229 126 EPTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-204 |
2.77e-77 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 231.91 E-value: 2.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNL---LG 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 158 DEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLI 207
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-204 |
1.25e-76 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 230.75 E-value: 1.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF----GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEnrnlL 76
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----R 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:COG1116 83 GVVFQEPALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 157 YDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLvfAEAI--SDRII 204
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRlWQETGKTVLFVTHDV--DEAVflADRVV 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-204 |
2.58e-76 |
|
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: 228.17 E-value: 2.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNlLGFVFQ 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN-IGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553319313 162 SALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03259 159 SALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIA 202
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-204 |
8.69e-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: 224.66 E-value: 8.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFG----QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidhlENRNLLG 77
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 158 DEPTSALDPELRQTVEALIVQN-REMGITQIVVTHDLvfAEAI--SDRII 204
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDI--DEAVflADRVV 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-204 |
2.80e-72 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 222.64 E-value: 2.80e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgiDHLE--NRNlLGF 78
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV--TDLPpkDRN-IAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKL-RKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 159 EPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG3839 159 EPLSNLDAKLRVEMRAEIKRlHRRLGTTTIYVTHDQVEAMTLADRIA 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-204 |
5.53e-72 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 221.94 E-value: 5.53e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGID-HLENRNlLGFVF 80
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlPPRERR-VGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553319313 161 TSALDPELRQTVEALIVQN-REMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVV 205
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-204 |
6.23e-72 |
|
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: 218.31 E-value: 6.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNL---L 76
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553319313 157 YDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRElRDELGLTSVVVTHDLDSAFAIADRVA 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-204 |
2.95e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 208.76 E-value: 2.95e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQ 81
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:COG1131 81 EPALYPDLTVRENLRFFARL-YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 162 SALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-204 |
4.99e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 206.06 E-value: 4.99e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidHLENRNL---- 75
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVT--ALRGRALrrlr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 --LGFVFQDFQLFPHLTVLDN-----LTLSPTI--TMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALAR 146
Cdd:COG3638 80 rrIGMIFQQFNLVPRLSVLTNvlagrLGRTSTWrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 147 AMMIDPQIIGYDEPTSALDPEL-RQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG3638 160 ALVQEPKLILADEPVASLDPKTaRQVMDLLRRIAREDGITVVVNLHQVDLARRYADRII 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-205 |
7.43e-67 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 204.52 E-value: 7.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQ-KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidHLENRNL---- 75
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLS--RLKRREIpylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 --LGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:COG2884 79 rrIGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553319313 154 IIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIR 205
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLE 209
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-204 |
2.54e-66 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 204.09 E-value: 2.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV----GIDHLENRNL-- 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSEKAIRLLrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 -LGFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:COG4161 83 kVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 155 IGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVV 212
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-208 |
8.90e-65 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 198.89 E-value: 8.90e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFVF 80
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLsAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHlTVLDNLTLSPTItmgKQKADAKEKALDLLARLGLKEHAQVYPYS-LSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:COG4619 81 QEPALWGG-TVRDNLPFPFQL---RERKFDRERALELLERLGLPPDILDKPVErLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 160 PTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVNP 208
Cdd:COG4619 157 PTSALDPENTRRVEELLREyLAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-204 |
3.72e-64 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 198.87 E-value: 3.72e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNL----- 75
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 ---------LGFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALAR 146
Cdd:COG4598 88 rqlqrirtrLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 147 AMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVV 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-204 |
8.96e-64 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 197.54 E-value: 8.96e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFG-QKTIFDgFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQV--------FYNGEDVGiDHLEN 72
Cdd:PRK11124 3 IQLNGINCFYGaHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSKTPSDK-AIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 RNLLGFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDP 152
Cdd:PRK11124 81 RRNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553319313 153 QIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVV 212
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-204 |
1.75e-63 |
|
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: 196.57 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG----IDHLENRNLLG 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLDNLTLsPTITMGK-QKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553319313 157 YDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-203 |
2.68e-63 |
|
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: 195.17 E-value: 2.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNlLGFVFQ 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSptITMGKQKADA-KEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:cd03301 80 NYALYPHMTVYDNIAFG--LKLRKVPKDEiDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553319313 161 TSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRlQQRLGTTTIYVTHDQVEAMTMADRI 201
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-207 |
3.14e-63 |
|
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: 195.92 E-value: 3.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgIDHLENRNLLGFVFQ 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 162 SALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd03300 159 GALDLKLRKDMQLELKRlQKELGITFVFVTHDQEEALTMSDRIAVMN 205
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-204 |
3.42e-63 |
|
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: 203.98 E-value: 3.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQK-----TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL 75
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD--LTKLSRRSL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 ------LGFVFQD--FQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGL-KEHAQVYPYSLSGGQKQRVALAR 146
Cdd:COG1123 338 relrrrVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIAR 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 147 AMMIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1123 418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADRVA 476
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-206 |
1.06e-62 |
|
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: 193.60 E-value: 1.06e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-----RNLLGF 78
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKaskfrREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:TIGR03608 81 LFQNFALIENETVEENLDL-GLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 159 EPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEaISDRIIRV 206
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-207 |
2.99e-62 |
|
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: 193.71 E-value: 2.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNlLGFVFQ 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTITMGKQ---KADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSErppEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 159 EPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRlHDELHVTTVFVTHDQEEALEVADRVVVMN 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-204 |
1.12e-61 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 192.66 E-value: 1.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNgeDVGIDHLEN-------- 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSlsqqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 ---RNLLGFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMM 149
Cdd:PRK11264 81 rqlRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-205 |
1.23e-61 |
|
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: 191.88 E-value: 1.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF----GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHL-EN--- 72
Cdd:COG4181 8 IIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD--LFALdEDara 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 ---RNLLGFVFQDFQLFPHLTVLDNLTLsPTITMGKqkADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMM 149
Cdd:COG4181 86 rlrARHVGFVFQSFQLLPTLTALENVML-PLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAiSDRIIR 205
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFElNRERGTTLVLVTHDPALAAR-CDRVLR 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-192 |
1.39e-61 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 194.91 E-value: 1.39e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQK----TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidHLENRNL- 75
Cdd:COG1135 1 MIELENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT--ALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 -----LGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:COG1135 79 aarrkIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALAN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHD 192
Cdd:COG1135 158 NPKVLLCDEATSALDPETTRSILDLLKDiNRELGLTIVLITHE 200
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-204 |
1.75e-61 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 195.94 E-value: 1.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgiDHL--ENRNlLGFV 79
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI--THVpaENRH-VNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHLTVLDNLTLSptITMGK-QKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:PRK09452 92 FQSYALFPHMTVFENVAFG--LRMQKtPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 159 EPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK09452 170 ESLSALDYKLRKQMQNELKAlQRKLGITFVFVTHDQEEALTMSDRIV 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-204 |
3.93e-61 |
|
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: 190.24 E-value: 3.93e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLLGFV 79
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQ--DFQLFpHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:COG1122 81 FQnpDDQLF-APTVEEDVAFGPEN-LGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 158 DEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI 205
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-203 |
4.24e-60 |
|
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: 187.79 E-value: 4.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQK----TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL- 75
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTD--LTLLSGKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 -----LGFVFQDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:cd03258 79 karrrIGMIFQHFNLLSSRTVFENVALPLEIA-GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALAN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:cd03258 158 NPKVLLCDEATSALDPETTQSILALLRDiNRELGLTIVLITHEMEVVKRICDRV 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-207 |
2.34e-59 |
|
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: 183.75 E-value: 2.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQ 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLtlsptitmgkqkadakekaldllarlglkehaqvypySLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03230 81 EPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 162 SALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILN 169
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-204 |
9.38e-59 |
|
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: 184.68 E-value: 9.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVF 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAEL-YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553319313 161 TSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVV 203
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-207 |
9.72e-59 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 188.37 E-value: 9.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNlLGFVFQ 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTITMGKQKADA---KEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTVLPRRERPNAaaiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 159 EPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQlHEELKFTSVFVTHDQEEAMEVADRVVVMS 211
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-207 |
4.83e-58 |
|
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: 181.90 E-value: 4.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQF--GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL-ENRNLLGFV 79
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLkELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDF--QLFpHLTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:cd03225 81 FQNPddQFF-GPTVEEEVAFGL-ENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 158 DEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLE 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-206 |
6.08e-58 |
|
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: 181.52 E-value: 6.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVF 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSptiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:COG4133 82 HADGLKPELTVRENLRFW---AALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 161 TSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAisDRIIRV 206
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAA--ARVLDL 202
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-203 |
7.20e-58 |
|
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: 182.50 E-value: 7.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFV 79
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIrEQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGL--KEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 158 DEPTSALDPELRQTV-EALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:cd03295 160 DEPFGALDPITRDQLqEEFKRLQQELGKTIVFVTHDIDEAFRLADRI 206
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-204 |
2.54e-57 |
|
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: 180.96 E-value: 2.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFG-QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV----GIDHLENRNL 75
Cdd:TIGR02315 1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 LGFVFQDFQLFPHLTVLDN-----LTLSPTITMGKQ---KADaKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARA 147
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENvlhgrLGYKPTWRSLLGrfsEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 148 MMIDPQIIGYDEPTSALDPEL-RQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR02315 160 LAQQPDLILADEPIASLDPKTsKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIV 217
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-204 |
4.70e-57 |
|
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: 180.38 E-value: 4.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQK----TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNL 75
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTrRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 LGFVFQDFQ--LFPHLTVLDnlTLS-PTITMGKqkADAKEKALDLLARLGL-KEHAQVYPYSLSGGQKQRVALARAMMID 151
Cdd:COG1124 81 VQMVFQDPYasLHPRHTVDR--ILAePLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 152 PQIIGYDEPTSALDPELR-QTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1124 157 PELLLLDEPTSALDVSVQaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVA 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-204 |
5.03e-57 |
|
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: 179.62 E-value: 5.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF----GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV----GIDHLEN 72
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 RNLLGFVFQDFQ--LFPHLTVLDNLTLSPTI-TMGKQKADAKEKALDLLARLGL-KEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:cd03257 81 RKEIQMVFQDPMssLNPRMTIGEQIAEPLRIhGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKlQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-204 |
2.48e-56 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 178.53 E-value: 2.48e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQ-KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGID-HLENRNL---L 76
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkGKALRQLrrqI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPHLTVLDN-----LTLSPTI--TMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMM 149
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvlsgrLGRRSTWrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADRIV 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-204 |
4.12e-55 |
|
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: 175.32 E-value: 4.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLE--NRNLLGFV 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGED--ITGLPphEIARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 --FQDFQLFPHLTVLDNLTLSPTITMG---------KQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:cd03219 79 rtFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-207 |
6.18e-55 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 174.56 E-value: 6.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIfdGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRnLLGFVF 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER-PVSMLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDN--LTLSPTitmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:COG3840 78 QENNLFPHLTVAQNigLGLRPG---LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 159 EPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDElCRERGLTVLMVTHDPEDAARIADRVLLVA 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-207 |
2.21e-54 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 176.83 E-value: 2.21e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLgFVFQ 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDIC-MVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSptITM-GKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:PRK11432 86 SYALFPHMSLGENVGYG--LKMlGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553319313 161 TSALDPELRQTVEALI--VQNReMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK11432 164 LSNLDANLRRSMREKIreLQQQ-FNITSLYVTHDQSEAFAVSDTVIVMN 211
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-204 |
1.78e-52 |
|
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: 168.13 E-value: 1.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESI-----DSGQVFYNGEDV---GIDHLENR 73
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydlDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 74 NLLGFVFQDFQLFPhLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKE--HAQVYPYSLSGGQKQRVALARAMMID 151
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 152 PQIIGYDEPTSALDPELRQTVEALIVQ-NREMGItqIVVTHDLVFAEAISDRII 204
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAElKKEYTI--VIVTHNMQQAARVADRTA 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
7-203 |
5.30e-52 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 168.21 E-value: 5.30e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 7 ISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNL----LGFVFQ 81
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaAMSRKELRELrrkkISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQ-GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 162 SALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:cd03294 189 SALDPLIRREMQDELLRlQAELQKTIVFITHDLDEALRLGDRI 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-204 |
7.63e-52 |
|
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: 167.53 E-value: 7.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL---LG 77
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD--LASLSRRELarrIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLDnltlspTITMG---------KQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:COG1120 79 YVPQEPPAPFGLTVRE------LVALGryphlglfgRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 149 MIDPQIIGYDEPTSALDP----ELRQTVEALivqNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLahqlEVLELLRRL---ARERGRTVVMVLHDLNLAARYADRLV 209
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-204 |
5.05e-51 |
|
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: 167.15 E-value: 5.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIF----DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLES---IDSGQVFYNGEDV-GIDHLEN 72
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLlKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 RNLLG----FVFQDfqlfPhLTVLDnltlsPTITMGKQ------------KADAKEKALDLLARLGL---KEHAQVYPYS 133
Cdd:COG0444 81 RKIRGreiqMIFQD----P-MTSLN-----PVMTVGDQiaeplrihgglsKAEARERAIELLERVGLpdpERRLDRYPHE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 134 LSGGQKQRVALARAMMIDPQIIGYDEPTSALDPelrqTVEALIVQ-----NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQAQILNllkdlQRELGLAILFITHDLGVVAEIADRVA 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-207 |
8.57e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 164.49 E-value: 8.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidhlENRNLLGFVF 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR----RARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQL---FPhLTVLDnltlspTITMGKQ---------KADAKEKALDLLARLGLKEHAQVyPYS-LSGGQKQRVALARA 147
Cdd:COG1121 82 QRAEVdwdFP-ITVRD------VVLMGRYgrrglfrrpSRADREAVDEALERVGLEDLADR-PIGeLSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-208 |
1.44e-50 |
|
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: 163.37 E-value: 1.44e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF-----GQKTI--FDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGID--HLE 71
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDlaQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 72 NRNLL-------GFVFQDFQLFPHLTVLDnLTLSPTITMGKQKADAKEKALDLLARLGLKEH-AQVYPYSLSGGQKQRVA 143
Cdd:COG4778 84 PREILalrrrtiGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 144 LARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVNP 208
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-205 |
2.94e-50 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 162.03 E-value: 2.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgiDHLENRNL---- 75
Cdd:TIGR02673 1 MIEFHNVSKAYPGGVaALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDV--NRLRGRQLpllr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 --LGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:TIGR02673 79 rrIGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553319313 154 IIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIR 205
Cdd:TIGR02673 158 LLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVII 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-202 |
5.32e-50 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 165.36 E-value: 5.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQK----TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL- 75
Cdd:PRK11153 1 MIELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQD--LTALSEKELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 -----LGFVFQDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:PRK11153 79 karrqIGMIFQHFNLLSSRTVFDNVALPLELA-GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDR 202
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDiNRELGLTIVLITHEMDVVKRICDR 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-205 |
6.96e-50 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 161.11 E-value: 6.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESID---SGQVFYNGEDvgIDHL--ENRNL 75
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRR--LTALpaEQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 lGFVFQDFQLFPHLTVLDNLT--LSPTITmgkqKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:COG4136 79 -GILFQDDLLFPHLSVGENLAfaLPPTIG----RAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 154 IIGYDEPTSALDPELRQTVEALIV-QNREMGITQIVVTHDLVFAEAISdRIIR 205
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFeQIRQRGIPALLVTHDEEDAPAAG-RVLD 205
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
2-204 |
2.06e-49 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 163.36 E-value: 2.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIF-----------DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHL 70
Cdd:COG4608 8 LEVRDLKKHFPVRGGLfgrtvgvvkavDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD--ITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 ENRNLLGF------VFQDFQ--LFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLK-EHAQVYPYSLSGGQKQR 141
Cdd:COG4608 86 SGRELRPLrrrmqmVFQDPYasLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 142 VALARAMMIDPQIIGYDEPTSALDpelrQTVEALIVqN------REMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALD----VSIQAQVL-NlledlqDELGLTYLFISHDLSVVRHISDRVA 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-204 |
6.34e-49 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 160.13 E-value: 6.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN--------- 72
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 -----RNLLGFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQV-YPYSLSGGQKQRVALAR 146
Cdd:PRK10619 86 qlrllRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 147 AMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-203 |
6.13e-48 |
|
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: 156.51 E-value: 6.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFG--QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFV 79
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLK-GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 160 PTSALDPELRQTVEALI---VQNREMgitqIVVTHDLVFAEAISDRI 203
Cdd:cd03263 160 PTSGLDPASRRAIWDLIlevRKGRSI----ILTTHSMDEAEALCDRI 202
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-207 |
2.44e-47 |
|
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: 152.78 E-value: 2.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLLGFVFQ 81
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAkLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 dfqlfphltvldnltlsptitmgkqkadakekaldllarlglkehaqvypysLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 162 SALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-207 |
2.84e-47 |
|
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: 154.61 E-value: 2.84e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDhlenRNLLGFVFQD 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 83 FQL---FPhLTVLDNLTLSPTITMG---KQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:cd03235 77 RSIdrdFP-ISVRDVVLMGLYGHKGlfrRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 157 YDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-204 |
3.32e-47 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 154.49 E-value: 3.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTI----FDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLEN--- 72
Cdd:NF038007 1 MLNMQNAEKCYITKTIktkvLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVtNLSYSQKiil 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 -RNLLGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMID 151
Cdd:NF038007 81 rRELIGYIFQSFNLIPHLSIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSN 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 152 PQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDlVFAEAISDRII 204
Cdd:NF038007 160 PALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRII 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-204 |
3.47e-47 |
|
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: 161.99 E-value: 3.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF--GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL---ESIDSGQVFYNGEDV-GIDHLENRN 74
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLlELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 75 LLGFVFQDF--QLFPhLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDP 152
Cdd:COG1123 84 RIGMVFQDPmtQLNP-VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 153 QIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVV 214
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-204 |
4.37e-47 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 155.22 E-value: 4.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFyngedVGIDHLEN-RNLLGFVF 80
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEaREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSptitmgkQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLG-------LKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553319313 161 TSALDPELRQTVEALIVQN-REMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVL 205
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-204 |
8.49e-47 |
|
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: 153.33 E-value: 8.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTI-FDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidHLENRNL----- 75
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVS--DLRGRAIpylrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 -LGFVFQDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:cd03292 79 kIGVVFQDFRLLPDRNVYENVAFALEVT-GVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 155 IGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVI 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-203 |
1.68e-46 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 153.26 E-value: 1.68e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIfDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLlGFVFQ 81
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDI-SYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSptitMGKQKADAKE---KALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:cd03299 79 NYALFPHMTVYKNIAYG----LKKRKVDKKEierKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 159 EPTSALDPELRQTV-EALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:cd03299 155 EPFSALDVRTKEKLrEELKKIRKEFGVTVLHVTHDFEEAWALADKV 200
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-203 |
6.48e-46 |
|
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: 154.19 E-value: 6.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 32 LVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLlGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAK 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHI-NMVFQSYALFPHMTVEENVAF-GLKMRKVPRAEIK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 112 EKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELR-QTVEALIVQNREMGITQIVVT 190
Cdd:TIGR01187 79 PRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRdQMQLELKTIQEQLGITFVFVT 158
|
170
....*....|...
gi 553319313 191 HDLVFAEAISDRI 203
Cdd:TIGR01187 159 HDQEEAMTMSDRI 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-202 |
9.02e-46 |
|
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: 150.66 E-value: 9.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLE----NRNLLG 77
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRD--ITGLPpherARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYpySLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAG--TLSGGEQQMLAIARALMSRPKLLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553319313 158 DEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDR 202
Cdd:cd03224 157 DEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADR 201
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
9-204 |
2.73e-45 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 153.85 E-value: 2.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 9 KQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLE----NRNLLGFVFQDF 83
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENImKQSPVElrevRRKKIGMVFQQF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 84 QLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSA 163
Cdd:TIGR01186 81 ALFPHMTILQNTSLGPEL-LGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553319313 164 LDPELRQTV-EALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR01186 160 LDPLIRDSMqDELKKLQATLQKTIVFITHDLDEAIRIGDRIV 201
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-207 |
3.18e-45 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 147.91 E-value: 3.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFG--QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGF 78
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLrDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFpHLTVLDNLtlsptitmgkqkadakekaldllarlglkehaqvypysLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:cd03228 81 VPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553319313 159 EPTSALDPELRQTVEALIvQNREMGITQIVVTHDLVfAEAISDRIIRVN 207
Cdd:cd03228 122 EATSALDPETEALILEAL-RALAKGKTVIVIAHRLS-TIRDADRIIVLD 168
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-204 |
3.30e-45 |
|
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: 159.23 E-value: 3.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQ--KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGF 78
Cdd:COG2274 474 IELENVSFRYPGdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLrQIDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFpHLTVLDNLTLS-PTITMGKQKADAKE-KALDLLARLGLKEHAQVYP--YSLSGGQKQRVALARAMMIDPQI 154
Cdd:COG2274 554 VLQDVFLF-SGTIRENITLGdPDATDEEIIEAARLaGLHDFIEALPMGYDTVVGEggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 155 IGYDEPTSALDPELRQTVEALIvQNREMGITQIVVTHDLVFAeAISDRII 204
Cdd:COG2274 633 LILDEATSALDAETEAIILENL-RRLLKGRTVIIIAHRLSTI-RLADRII 680
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-205 |
5.56e-45 |
|
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: 149.01 E-value: 5.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFG----QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL-- 75
Cdd:TIGR02982 2 ISIRNLNHYYGhgslRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQE--LHGASKKQLvq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 ----LGFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMID 151
Cdd:TIGR02982 80 lrrrIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 152 PQIIGYDEPTSALDPEL-RQTVEALIVQNREMGITQIVVTHDLVFAEaISDRIIR 205
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSgRDVVELMQKLAKEQGCTILMVTHDNRILD-VADRILQ 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-207 |
7.51e-45 |
|
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: 148.11 E-value: 7.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGeVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQ 81
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 162 SALDPELRQTVEALIVqnrEMGITQIVV--THDLVFAEAISDRIIRVN 207
Cdd:cd03264 159 AGLDPEERIRFRNLLS---ELGEDRIVIlsTHIVEDVESLCNQVAVLN 203
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-162 |
1.11e-44 |
|
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: 145.87 E-value: 1.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 17 FDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFVFQDFQLFPHLTVLDNL 95
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 96 TLSPTItMGKQKADAKEKALDLLARLGL----KEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTS 162
Cdd:pfam00005 81 RLGLLL-KGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-205 |
1.32e-44 |
|
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: 147.40 E-value: 1.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNLLGFVFQ 81
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKP--IKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 D--FQLFPHlTVLDNLTLSptitmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:cd03226 79 DvdYQLFTD-SVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 160 PTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIR 205
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLL 198
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-192 |
1.52e-44 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 148.86 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFG----QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV---GIDHlenr 73
Cdd:COG4525 3 MLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 74 nllGFVFQDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:COG4525 79 ---GVVFQKDALLPWLNVLDNVAFGLRLR-GVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553319313 154 IIGYDEPTSALDPELRQTVEALIVQN-REMGITQIVVTHD 192
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHS 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-207 |
1.90e-44 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 151.15 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgiDHLE--NRNlLG 77
Cdd:PRK11650 3 GLKLQAVRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV--NELEpaDRD-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLDNLTLSPTIT-MGKQKADAK-EKAldllAR-LGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRgMPKAEIEERvAEA----ARiLELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 155 IGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRlHRRLKTTSLYVTHDQVEAMTLADRVVVMN 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
17-204 |
3.15e-44 |
|
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: 146.67 E-value: 3.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 17 FDGFNLTVQ---DGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEdVGIDHLENRNL------LGFVFQDFQLFP 87
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKINLppqqrkIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 88 HLTVLDNLTLSptiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPE 167
Cdd:cd03297 89 HLNVRENLAFG---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 553319313 168 LRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03297 166 LRLQLLPELKQiKKNLNIPVIFVTHDLSEAEYLADRIV 203
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-204 |
4.23e-44 |
|
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: 145.27 E-value: 4.23e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLLGFVFQ 81
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAsLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 dfqlfphltvldnltlsptitmgkqkadakekaldLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03214 81 -----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 162 SALDP----ELRQTVEALivqNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03214 126 SHLDIahqiELLELLRRL---ARERGKTVVMVLHDLNLAARYADRVI 169
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-207 |
4.77e-44 |
|
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: 146.27 E-value: 4.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHlenRNLLGFVFQ 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA---RNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 162 SALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLN 202
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-206 |
1.11e-43 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 154.50 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF----GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgiDHLEN---- 72
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDV--ATLDAdala 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 ---RNLLGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMM 149
Cdd:PRK10535 82 qlrREHFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHD-LVFAEAisDRIIRV 206
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDpQVAAQA--ERVIEI 216
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-204 |
1.39e-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: 144.94 E-value: 1.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 20 FNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLlGFVFQDFQLFPHLTVLDN--LTL 97
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPV-SMLFQENNLFAHLTVEQNvgLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 98 SPTITMGKQKADAKEKALdllARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIV 177
Cdd:cd03298 96 SPGLKLTAEDRQAIEVAL---ARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180
....*....|....*....|....*...
gi 553319313 178 Q-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03298 173 DlHAETKMTVLMVTHQPEDAKRLAQRVV 200
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-204 |
1.59e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 1.59e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHlenRNLLGFVF 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLT----LSptitmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:COG4152 78 EERGLYPKMKVGEQLVylarLK-----GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 157 YDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIV 200
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-204 |
4.17e-43 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 148.25 E-value: 4.17e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNlLGFVFQDF 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG-VGMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 84 QLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSA 163
Cdd:PRK11000 85 ALYPHLSVAENMSFGLKLA-GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553319313 164 LDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK11000 164 LDAALRVQMRIEISRlHKRLGRTMIYVTHDQVEAMTLADKIV 205
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-206 |
6.71e-43 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 143.77 E-value: 6.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQK----TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLL 76
Cdd:PRK10584 6 IVEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 -----GFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMID 151
Cdd:PRK10584 86 rakhvGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 152 PQIIGYDEPTSALDpelRQT----VEALIVQNREMGITQIVVTHDLVFAeAISDRIIRV 206
Cdd:PRK10584 165 PDVLFADEPTGNLD---RQTgdkiADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRL 219
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-203 |
1.08e-42 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 147.56 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNL----LGFVFQDFQLFPHLTVLDN- 94
Cdd:COG4175 47 SFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDItKLSKKELRELrrkkMSMVFQHFALLPHRTVLENv 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 95 ---LTLSptitmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPelrqt 171
Cdd:COG4175 127 afgLEIQ-----GVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDP----- 196
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 172 veaLI---VQN------REMGITQIVVTHDLvfAEA--ISDRI 203
Cdd:COG4175 197 ---LIrreMQDellelqAKLKKTIVFITHDL--DEAlrLGDRI 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-207 |
2.91e-42 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 146.13 E-value: 2.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNlLGFVF 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-INMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNltlsptITMG-KQ----KADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQII 155
Cdd:PRK11607 98 QSYALFPHMTVEQN------IAFGlKQdklpKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 156 GYDEPTSALDPELRQTVEALIVQNRE-MGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK11607 172 LLDEPMGALDKKLRDRMQLEVVDILErVGVTCVMVTHDQEEAMTMAGRIAIMN 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-203 |
2.93e-42 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 148.24 E-value: 2.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDH-LENRNL-LGF 78
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAgIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTL------SPTITMGKQKADAKEkaldLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDP 152
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLgreprrGGLIDWRAMRRRARE----LLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 153 QIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDL--VFaeAISDRI 203
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLdeVF--EIADRV 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-204 |
7.01e-42 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 144.47 E-value: 7.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELkNISKQFGqktifdGFNLTVQ----DGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEdVGIDHLENRNL- 75
Cdd:COG4148 2 MLEV-DFRLRRG------GFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARGIFLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 -----LGFVFQDFQLFPHLTVLDNLTLsptitmGKQKADAKEKALDL---LARLGLKEHAQVYPYSLSGGQKQRVALARA 147
Cdd:COG4148 74 phrrrIGYVFQEARLFPHLSVRGNLLY------GRKRAPRAERRISFdevVELLGIGHLLDRRPATLSGGERQRVAIGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTV----EALivqNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4148 148 LLSSPRLLLMDEPLAALDLARKAEIlpylERL---RDELDIPILYVSHSLDEVARLADHVV 205
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-204 |
2.08e-41 |
|
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: 141.43 E-value: 2.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIF-----DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLL 76
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFekkalDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 ----GFVFQ--DFQLFpHLTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLKEH-AQVYPYSLSGGQKQRVALARAMM 149
Cdd:TIGR04521 81 rkkvGLVFQfpEHQLF-EETVYKDIAFGP-KNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRlHKEKGLTVILVTHSMEDVAEYADRVI 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-204 |
3.46e-41 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 146.85 E-value: 3.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISkqF---GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLG 77
Cdd:COG1132 340 IEFENVS--FsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrDLTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFpHLTVLDNltlsptITMGKQKADAKE--------KALDLLARLGLKEHAQVYP--YSLSGGQKQRVALARA 147
Cdd:COG1132 418 VVPQDTFLF-SGTIREN------IRYGRPDATDEEveeaakaaQAHEFIEALPDGYDTVVGErgVNLSGGQRQRIAIARA 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 148 MMIDPQIIGYDEPTSALDPElrqtVEALIVQN--REM-GITQIVVTHDLVFAEAiSDRII 204
Cdd:COG1132 491 LLKDPPILILDEATSALDTE----TEALIQEAleRLMkGRTTIVIAHRLSTIRN-ADRIL 545
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-201 |
3.86e-41 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 142.03 E-value: 3.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNL---LGFVFQD--FQLFPHLTV 91
Cdd:PRK11308 32 DGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlKADPEAQKLLrqkIQIVFQNpyGSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNLTLSPTITMGKQKADAKEKALDLLARLGLK-EHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQ 170
Cdd:PRK11308 112 GQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQA 191
|
170 180 190
....*....|....*....|....*....|..
gi 553319313 171 TVEALIVQ-NREMGITQIVVTHDLVFAEAISD 201
Cdd:PRK11308 192 QVLNLMMDlQQELGLSYVFISHDLSVVEHIAD 223
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-207 |
9.41e-41 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 140.22 E-value: 9.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 9 KQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQDFQLFPH 88
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 89 LTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPEL 168
Cdd:TIGR01188 81 LTGRENLEMMGRL-YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 553319313 169 RQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:TIGR01188 160 RRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIID 198
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-203 |
2.10e-40 |
|
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: 137.12 E-value: 2.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQ 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03265 81 DLSVDDELTGWENLYIHARL-YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 162 SALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKlKEEFGMTILLTTHYMEEAEQLCDRV 202
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-202 |
3.06e-40 |
|
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: 137.04 E-value: 3.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLE----NRNLL 76
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED--ITGLPphriARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADA-KEKALDLLARLglKEHAQVYPYSLSGGQKQRVALARAMMIDPQII 155
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRAdLERVYELFPRL--KERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 156 GYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDR 202
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADR 205
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-207 |
8.46e-40 |
|
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: 135.04 E-value: 8.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHlENRNLLGFVFQ 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTItMGKQKADAKEkaldLLARLGLKEHA--QVYPYSLsgGQKQRVALARAMMIDPQIIGYDE 159
Cdd:cd03268 80 APGFYPNLTARENLRLLARL-LGIRKKRIDE----VLDVVGLKDSAkkKVKGFSL--GMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553319313 160 PTSALDP----ELRQtveaLIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:cd03268 153 PTNGLDPdgikELRE----LILSLRDQGITVLISSHLLSEIQKVADRIGIIN 200
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-204 |
2.64e-39 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 135.64 E-value: 2.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF--GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDH--LENRNLLG 77
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQ--DFQlFPHLTV-------LDNLTLsPTITMGKQKADAkekaldlLARLGLKEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:TIGR04520 81 MVFQnpDNQ-FVGATVeddvafgLENLGV-PREEMRKRVDEA-------LKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLvfAEAI-SDRII 204
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKlNKEEGITVISITHDM--EEAVlADRVI 207
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-204 |
3.62e-39 |
|
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: 134.03 E-value: 3.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKT----IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLL 76
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPHLTVLDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGL-YGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 157 YDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVV 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-204 |
3.98e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 134.83 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFG-----QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENR-N 74
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 75 LLGFVFQDFQL--FPHLTVLDNLTL------SPTITMGKQKADaKEKALDLLARLGL----KEHAQVypYSLSGGQKQRV 142
Cdd:COG1101 81 YIGRVFQDPMMgtAPSMTIEENLALayrrgkRRGLRRGLTKKR-RELFRELLATLGLglenRLDTKV--GLLSGGQRQAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 143 ALARAMMIDPQIIGYDEPTSALDPELRQTVEAL---IVqnREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDPKTAALVLELtekIV--EENNLTTLMVTHNMEQALDYGNRLI 220
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-184 |
4.87e-39 |
|
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: 133.82 E-value: 4.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVF- 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 -QDFQLFPHLTVLDNLtLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:cd03218 81 pQEASIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180
....*....|....*....|....*
gi 553319313 160 PTSALDPELRQTVEALIVQNREMGI 184
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGI 184
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
20-206 |
6.80e-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: 133.06 E-value: 6.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 20 FNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgIDHLENRNLLGFVFQDFQLFPHLTVLDN--LTL 97
Cdd:TIGR01277 17 FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSH-TGLAPYQRPVSMLFQENNLFAHLTVRQNigLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 98 SPTItmgKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIV 177
Cdd:TIGR01277 96 HPGL---KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172
|
170 180 190
....*....|....*....|....*....|
gi 553319313 178 QN-REMGITQIVVTHDLVFAEAISDRIIRV 206
Cdd:TIGR01277 173 QLcSERQRTLLMVTHHLSDARAIASQIAVV 202
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-203 |
9.16e-39 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 139.01 E-value: 9.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDH-LENRNL-LGF 78
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTLS--PTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 157 YDEPTSALDPelrQTVEALIVQNREM---GITQIVVTHDLVFAEAISDRI 203
Cdd:COG3845 165 LDEPTAVLTP---QEADELFEILRRLaaeGKSIIFITHKLREVMAIADRV 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-204 |
3.42e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 132.65 E-value: 3.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF---------GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEdvgidHLEN 72
Cdd:COG4167 5 LEVRNLSKTFkyrtglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH-----KLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 RN------LLGFVFQDfqlfPhltvldNLTLSPTITMGKQ------------KADAKEKALDLLARLGL-KEHAQVYPYS 133
Cdd:COG4167 80 GDykyrckHIRMIFQD----P------NTSLNPRLNIGQIleeplrlntdltAEEREERIFATLRLVGLlPEHANFYPHM 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553319313 134 LSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELR-QTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRsQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVL 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
20-206 |
4.07e-38 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 131.63 E-value: 4.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 20 FNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgidHLEN---RNLLGFVFQDFQLFPHLTVLDN-- 94
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----HTTTppsRRPVSMLFQENNLFSHLTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 95 LTLSPTItmgKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEA 174
Cdd:PRK10771 94 LGLNPGL---KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190
....*....|....*....|....*....|...
gi 553319313 175 LIVQ-NREMGITQIVVTHDLVFAEAISDRIIRV 206
Cdd:PRK10771 171 LVSQvCQERQLTLLMVSHSLEDAARIAPRSLVV 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-200 |
4.41e-38 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 131.48 E-value: 4.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFG----QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGI------DHL 70
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 ENRNLlGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:PRK11629 85 RNQKL-GFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAIS 200
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGElNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-184 |
9.05e-38 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 130.92 E-value: 9.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGID--HLENRNLLGF 78
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTLsptI--TMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:COG1137 83 LPQEASIFRKLTVEDNILA---VleLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190
....*....|....*....|....*....|..
gi 553319313 157 YDEPTSALDP----ELRQTVEALivQNREMGI 184
Cdd:COG1137 160 LDEPFAGVDPiavaDIQKIIRHL--KERGIGV 189
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-193 |
1.82e-37 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 130.59 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENrnllGFVF 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER----GVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:PRK11248 77 QNEGLLPWRNVQDNVAFGLQLA-GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190
....*....|....*....|....*....|....
gi 553319313 161 TSALDPELRQTVEALIVQN-REMGITQIVVTHDL 193
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDI 189
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-205 |
2.46e-37 |
|
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: 136.05 E-value: 2.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF--GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLLGF 78
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDlRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFpHLTVLDNLTLsptitmGKQKADaKEKALDLLARLGLKEHAQVYPY-----------SLSGGQKQRVALARA 147
Cdd:COG4987 414 VPQRPHLF-DTTLRENLRL------ARPDAT-DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARA 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALI---VQNRemgiTQIVVTHDLVFAEAIsDRIIR 205
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLleaLAGR----TVLLITHRLAGLERM-DRILV 541
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-207 |
4.62e-37 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 135.27 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQ-KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFV 79
Cdd:COG4988 337 IELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLsDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFpHLTVLDNLTL-SPTITMgKQKADAKEKA--LDLLARL--GLK----EHAQvypySLSGGQKQRVALARAMMI 150
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLgRPDASD-EELEAALEAAglDEFVAALpdGLDtplgEGGR----GLSGGQAQRLALARALLR 490
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDLVFAeAISDRIIRVN 207
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLD 545
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-202 |
5.24e-37 |
|
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: 134.54 E-value: 5.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF-----GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNL 75
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 --------LGFVFQDFQLFPHLTVLDNLTLSPTITMGKQKAdaKEKALDLLARLGLKEHAQV-----YPYSLSGGQKQRV 142
Cdd:TIGR03269 359 grgrakryIGILHQEYDLYPHRTVLDNLTEAIGLELPDELA--RMKAVITLKMVGFDEEKAEeildkYPDELSEGERHRV 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 143 ALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNR-EMGITQIVVTHDLVFAEAISDR 202
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAReEMEQTFIIVSHDMDFVLDVCDR 497
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-204 |
1.10e-36 |
|
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: 127.97 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV---GIDHLenrnllgFVFQDFQLFPHLTVLDN 94
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItepGPDRM-------VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 95 LTLSPTITMGKQKADAKEKALD-LLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTV- 172
Cdd:TIGR01184 75 IALAVDRVLPDLSKSERRAIVEeHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLq 154
|
170 180 190
....*....|....*....|....*....|..
gi 553319313 173 EALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDEALLLSDRVV 186
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-202 |
2.20e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 127.85 E-value: 2.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL-ESID----SGQVFYNGEDV---GIDHLENR 73
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDGEDIydpDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 74 NLLGFVFQDFQLFPHlTVLDNLTLSPTITMGKQKADAKEKALDLLARLGL----KEHAQVYPYSLSGGQKQRVALARAMM 149
Cdd:COG1117 92 RRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDLvfAEA--ISDR 202
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIVTHNM--QQAarVSDY 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-204 |
4.87e-36 |
|
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: 132.12 E-value: 4.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF-GQKTIF----------DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESiDSGQVFYNGEDvgIDHL 70
Cdd:COG4172 276 LEARDLKVWFpIKRGLFrrtvghvkavDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQD--LDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 ENRNLLGF------VFQD-FQ-LFPHLTVLDnltlspTIT-------MGKQKADAKEKALDLLARLGLK-EHAQVYPYSL 134
Cdd:COG4172 353 SRRALRPLrrrmqvVFQDpFGsLSPRMTVGQ------IIAeglrvhgPGLSAAERRARVAEALEEVGLDpAARHRYPHEF 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 135 SGGQKQRVALARAMMIDPQIIGYDEPTSALDpelrQTVEALIVQ-----NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDllrdlQREHGLAYLFISHDLAVVRALAHRVM 497
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-204 |
6.29e-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: 129.08 E-value: 6.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-----GIDHLENRNLLGFVFQDFQLFPHLTVLDNL 95
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrkGIFLPPEKRRIGYVFQEARLFPHLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 96 TLSPTITMGKQKADAKEKALDLLarlGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALD-PELRQTVEA 174
Cdd:TIGR02142 97 RYGMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdPRKYEILPY 173
|
170 180 190
....*....|....*....|....*....|
gi 553319313 175 LIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVV 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-204 |
1.33e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 125.65 E-value: 1.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL---LG 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP--LADWSPAELarrRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQL-FPhLTVLD--NLTLSPTITMGKQKADAKEKALDLLARLGLKEHAqvYPySLSGGQKQRVALARAMM----- 149
Cdd:PRK13548 80 VLPQHSSLsFP-FTVEEvvAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRD--YP-QLSGGEQQRVQLARVLAqlwep 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 150 -IDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK13548 156 dGPPRWLLLDEPTSALDLAHQHHVLRLARQlAHERGLAVIVVLHDLNLAARYADRIV 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-204 |
1.44e-35 |
|
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: 122.92 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIdhlenrnllgfvfq 81
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 dfqlfphltvldnltLSPtitmgkqkADAKekaldllaRLGLkehAQVYpySLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:cd03216 67 ---------------ASP--------RDAR--------RAGI---AMVY--QLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 162 SALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVT 153
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-207 |
2.17e-35 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 124.22 E-value: 2.17e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL---- 75
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHD--ITRLKNREVpflr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 --LGFVFQDFQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:PRK10908 79 rqIGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 154 IIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLS 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-193 |
2.96e-35 |
|
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: 124.43 E-value: 2.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQ---VF---YNGEDVgidhLENRN 74
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerRGGEDV----WELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 75 LLGFVFQDFQLF--PHLTVLD--------NLTLSPTITmgkqkADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVAL 144
Cdd:COG1119 79 RIGLVSPALQLRfpRDETVLDvvlsgffdSIGLYREPT-----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 145 ARAMMIDPQIIGYDEPTSALDP----ELRQTVEALIvqnREMGITQIVVTHDL 193
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLgareLLLALLDKLA---AEGAPTLVLVTHHV 203
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-204 |
3.95e-35 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 129.41 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGeDVGIDHLEnrnllgfvfQDF 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLRIGYLP---------QEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 84 QLFPHLTVLDNLT--LSPTITMGKQKA-----------------------------DAKEKALDLLARLGLKEHAQVYPY 132
Cdd:COG0488 71 PLDDDLTVLDTVLdgDAELRALEAELEeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 133 S-LSGGQKQRVALARAMMIDPQIIGYDEPTSALDPElrqTVEAL--IVQNREMGItqIVVTHDLVFAEAISDRII 204
Cdd:COG0488 151 SeLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLE---SIEWLeeFLKNYPGTV--LVVSHDRYFLDRVATRIL 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-207 |
7.30e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 125.20 E-value: 7.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKT-----IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL------ 70
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 -------------------ENRNLLGFVFQ--DFQLFPHlTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLKE-HAQ 128
Cdd:PRK13651 83 vleklviqktrfkkikkikEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGP-VSMGVSKEEAKKRAAKYIELVGLDEsYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 129 VYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPElrQTVEAL-IVQN-REMGITQIVVTHDLVFAEAISDRIIRV 206
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQ--GVKEILeIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
.
gi 553319313 207 N 207
Cdd:PRK13651 239 K 239
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-204 |
8.86e-35 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 123.97 E-value: 8.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDS---------GQVFYNGEDVGIDHLE 71
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 72 NRNLLGFVFQDFQLFPHLTVLDNLTLSptiTMGKQ----------KADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQR 141
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLIG---ALGSTpfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553319313 142 VALARAMMIDPQIIGYDEPTSALDPE-LRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPEsARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIV 224
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-191 |
1.20e-34 |
|
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: 120.78 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFG--QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLLGF 78
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHlTVLDNLtlsptitmgkqkadakekaldllarlglkehaqvypysLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:cd03246 81 LPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190
....*....|....*....|....*....|...
gi 553319313 159 EPTSALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAH 154
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-201 |
2.56e-34 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.95 E-value: 2.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV---GIDHL-ENRNLL 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamSRSRLyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPHLTVLDNLT------------LSPTITMGKQKAdakekaldllarLGLKEHAQVYPYSLSGGQKQRVAL 144
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAyplrehtqlpapLLHSTVMMKLEA------------VGLRGAAKLMPSELSGGMARRAAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 145 ARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISD 201
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElNSALGVTCVVVSHDVPEVLSIAD 212
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-203 |
5.26e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.11 E-value: 5.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDH---LENRNLL 76
Cdd:PRK13639 1 ILETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQ--DFQLFPHlTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDVAFGP-LNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553319313 155 IGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKV 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-204 |
8.98e-34 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 122.89 E-value: 8.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDH---LENRNLLGFVFQD--FQLFPHLTV 91
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDdewRAVRSDIQMIFQDplASLNPRMTI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNL-----TLSPTITmgkqKADAKEKALDLLARLGLKEHA-QVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALD 165
Cdd:PRK15079 118 GEIIaeplrTYHPKLS----RQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553319313 166 PELR-QTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK15079 194 VSIQaQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVL 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-208 |
9.04e-34 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.95 E-value: 9.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYnGEDVGIdhlenrnllGFVF 80
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKI---------GYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDF-QLFPHLTVLDNLT-LSPTITmgkqkadaKEKALDLLARLGLK-EHAQVYPYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:COG0488 385 QHQeELDPDKTVLDELRdGAPGGT--------EQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 158 DEPTSALDPElrqTVEALivqnrEMGITQ-----IVVTHDLVFAEAISDRIIRVNP 208
Cdd:COG0488 457 DEPTNHLDIE---TLEAL-----EEALDDfpgtvLLVSHDRYFLDRVATRILEFED 504
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-207 |
1.07e-33 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 120.87 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GI-DHLENRnlLGF 78
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeGLpGHQIAR--MGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 V--FQDFQLFPHLTVLDNLT--------------LSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRV 142
Cdd:PRK11300 83 VrtFQHVRLFREMTVIENLLvaqhqqlktglfsgLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 143 ALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAElRNEHNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-207 |
1.15e-33 |
|
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: 119.62 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF-GQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLLGF 78
Cdd:cd03245 3 IEFRNVSFSYpNQEIpALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqLDPADLRRNIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFpHLTVLDNltlsptITMGKQKADaKEKALDLLARLGLKEHAQVYP-----------YSLSGGQKQRVALARA 147
Cdd:cd03245 83 VPQDVTLF-YGTLRDN------ITLGAPLAD-DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 553319313 148 MMIDPQIIGYDEPTSALDpelrQTVEALIVQN-REM--GITQIVVTHDLVFAEaISDRIIRVN 207
Cdd:cd03245 155 LLNDPPILLLDEPTSAMD----MNSEERLKERlRQLlgDKTLIIITHRPSLLD-LVDRIIVMD 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-193 |
1.91e-33 |
|
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: 119.25 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFVF 80
Cdd:cd03254 4 EFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIrDISRKSLRSMIGVVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHlTVLDNLTLS-PTITMGKQKADAKE-KALDLLARL--GLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:cd03254 84 QDTFLFSG-TIMENIRLGrPNATDEEVIEAAKEaGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 553319313 157 YDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDL 193
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRL 198
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
16-196 |
3.88e-33 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 117.52 E-value: 3.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 16 IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDH---LENRNLLGFVFQ--DFQLFpHLT 90
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRkglLERRQRVGLVFQdpDDQLF-AAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 91 VLDNLTLSPtITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQ 170
Cdd:TIGR01166 86 VDQDVAFGP-LNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|....*.
gi 553319313 171 TVEALIVQNREMGITQIVVTHDLVFA 196
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-204 |
3.94e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.45 E-value: 3.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL---LG 77
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRP--LAAWSPWELarrRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQL-FPhLTVLD--NLTLSPTITMGKQKADAKEKALDLLARLGLKEHAqvYPySLSGGQKQRVALARAM------ 148
Cdd:COG4559 79 VLPQHSSLaFP-FTVEEvvALGRAPHGSSAAQDRQIVREALALVGLAHLAGRS--YQ-TLSGGEQQRVQLARVLaqlwep 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 149 -MIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4559 155 vDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRIL 211
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-192 |
4.55e-33 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 118.28 E-value: 4.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLLGFV 79
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHlTVLDNLTLSPTItmgKQKADAKEKALDLLARLGLKEHAQVYPYS-LSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQI---RNQQPDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 553319313 159 EPTSALDPELRQTVEALIVQ-NREMGITQIVVTHD 192
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRyVREQNIAVLWVTHD 197
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-203 |
7.75e-33 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 121.68 E-value: 7.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNL----LGFVFQDFQLFPHLTVLDNL 95
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkISDAELREVrrkkIAMVFQSFALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 96 TLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEAL 175
Cdd:PRK10070 128 AFGMELA-GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDE 206
|
170 180
....*....|....*....|....*....
gi 553319313 176 IVQ-NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK10070 207 LVKlQAKHQRTIVFISHDLDEAMRIGDRI 235
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
1.04e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 119.96 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKT-----IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQV----FYNGEDVGIDHLE 71
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 72 N-------------RNLLGFVFQ--DFQLFPHlTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLKE-HAQVYPYSLS 135
Cdd:PRK13631 101 TnpyskkiknfkelRRRVSMVFQfpEYQLFKD-TIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 136 GGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-203 |
1.05e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.09 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL-----ESIDSGQVFYNGEDV-GIDHLENRNL 75
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIfKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 LGFVFQDFQLFPHLTVLDNLTLSPTIT-MGKQKADAKEKALDLLARLGL----KEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNrLVKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGItqIVVTHDLVFAEAISDRI 203
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLElKKDMTI--VLVTHFPQQAARISDYV 215
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-193 |
1.11e-32 |
|
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: 117.64 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 16 IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV---GIDHLenRNLLGFVFQDFQLFPhLTVL 92
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlNLRWL--RSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 93 DNltlsptITMGKQKADAKE--------KALDLLARLGLKEHAQVYPY--SLSGGQKQRVALARAMMIDPQIIGYDEPTS 162
Cdd:cd03249 95 EN------IRYGKPDATDEEveeaakkaNIHDFIMSLPDGYDTLVGERgsQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190
....*....|....*....|....*....|..
gi 553319313 163 ALDPELRQTV-EALivQNREMGITQIVVTHDL 193
Cdd:cd03249 169 ALDAESEKLVqEAL--DRAMKGRTTIVIAHRL 198
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-203 |
1.18e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 119.52 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQ 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNL-TLSPTITMGKQKADAKEKALDLLARLGLKEHAQVypYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:PRK13537 88 FDNLDPDFTVRENLlVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV--GELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 161 TSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRL 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-193 |
4.38e-32 |
|
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: 121.31 E-value: 4.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFV 79
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVsSLDQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFpHLTVLDNLTLSptitmgkqKADA-KEKALDLLARLGLKEHAQVYPY-----------SLSGGQKQRVALARA 147
Cdd:TIGR02868 415 AQDAHLF-DTTVRENLRLA--------RPDAtDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDL 193
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALS-GRTVVLITHHL 530
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-204 |
5.50e-32 |
|
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: 115.70 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLEN----RNLLG 77
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGED--ITKLPPheraRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLDNLTlsptitMGKQKADAKEKAL------------DLLARLGlkehaqvypYSLSGGQKQRVALA 145
Cdd:TIGR03410 79 YVPQGREIFPRLTVEENLL------TGLAALPRRSRKIpdeiyelfpvlkEMLGRRG---------GDLSGGQQQQLAIA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 146 RAMMIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRlRAEGGMAILLVEQYLDFARELADRYY 203
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-203 |
1.89e-31 |
|
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: 119.40 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQ----KTIFDGFNLTVQDGEVLSLVGPSGGGKT----TLLRMLAGLESIDSGQVFYNGEDvgIDHLEN 72
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQD--LLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 RNL-------LGFVFQDfqlfPhLTVLDnltlsPTITMGKQ------------KADAKEKALDLLARLGLKEHAQ---VY 130
Cdd:COG4172 84 RELrrirgnrIAMIFQE----P-MTSLN-----PLHTIGKQiaevlrlhrglsGAAARARALELLERVGIPDPERrldAY 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 131 PYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPelrqTVEALIVQ-----NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQAQILDllkdlQRELGMALLLITHDLGVVRRFADRV 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
2.62e-31 |
|
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: 119.31 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFV 79
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHlTVLDNLTLSptitmgkqKADAKEKAL-DLLARLGLKEHAQVYPYS-----------LSGGQKQRVALARA 147
Cdd:TIGR02857 402 PQHPFLFAG-TIAENIRLA--------RPDASDAEIrEALERAGLDEFVAALPQGldtpigeggagLSGGQAQRLALARA 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDLVFAEAiSDRIIRV 206
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-203 |
2.98e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 116.47 E-value: 2.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQ 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTL-SPTITMGKQKADAKEKALDLLARLGLKEHAQVypYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:PRK13536 122 FDNLDLEFTVRENLLVfGRYFGMSTREIEAVIPSLLEFARLESKADARV--SDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 161 TSALDPELRQTV----EALIVQnremGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK13536 200 TTGLDPHARHLIwerlRSLLAR----GKTILLTTHFMEEAERLCDRL 242
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-204 |
3.35e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.02 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidHLENRNL---LG 77
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVA--TTPSRELakrLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQLFPHLTVLD------------NLTlsptitmgkqKADAK--EKALDllaRLGLKEHAQVYPYSLSGGQKQRVA 143
Cdd:COG4604 79 ILRQENHINSRLTVRElvafgrfpyskgRLT----------AEDREiiDEAIA---YLDLEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 144 LARAMMIDPQIIGYDEPTSALDPE--------LRQTVealivqnREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKhsvqmmklLRRLA-------DELGKTVVIVLHDINFASCYADHIV 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-205 |
4.08e-31 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 112.59 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLL--- 76
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrQRDEYHQDLLylg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 ---GfvfqdfqLFPHLTVLDNLTLSPTITmgkQKADAkEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:PRK13538 81 hqpG-------IKTELTALENLRFYQRLH---GPGDD-EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553319313 154 IIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIR 205
Cdd:PRK13538 150 LWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASDKVRKLR 201
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-191 |
4.09e-31 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 112.26 E-value: 4.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLES--IDSGQVFYNGEDVGIDHLenRNLLGFVFQDFQLFPHL 89
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKRSF--RKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 90 TVldnltlsptitmgkqkadakEKALDLLARLglkehaqvypYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELR 169
Cdd:cd03213 98 TV--------------------RETLMFAAKL----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|..
gi 553319313 170 QTVEALIVQNREMGITQIVVTH 191
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIH 169
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-202 |
5.35e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.72 E-value: 5.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESID-----SGQVFYNGEDV---GIDHLEN 72
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIyspRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 RNLLGFVFQDFQLFPhLTVLDNLTLSPTITMGKQKA---DAKEKALDLLARLG-LKEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:PRK14239 85 RKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQvldEAVEKSLKGASIWDeVKDRLHDSALGLSGGQQQRVCIARVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDLVFAEAISDR 202
Cdd:PRK14239 164 ATSPKIILLDEPTSALDPISAGKIEETLLGLKD-DYTMLLVTRSMQQASRISDR 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
1.06e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.55 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFG--QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL-ENRNLLG 77
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLkEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQ--DFQlFPHLTV-------LDNLTLSPTitmgkqkaDAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:PRK13632 87 IIFQnpDNQ-FIGATVeddiafgLENKKVPPK--------KMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGI-TQIVVTHDLvfAEAI-SDRII 204
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDM--DEAIlADKVI 213
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-207 |
1.15e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 113.57 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF--GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL-ENRNLLGF 78
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQ--DFQlFPHLTVLDNLTLS------PTITMGKQKADAkekaldlLARLGLKEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:PRK13635 86 VFQnpDNQ-FVGATVQDDVAFGlenigvPREEMVERVDQA-------LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAeAISDRIIRVN 207
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQlKEQKGITVLSITHDLDEA-AQADRVIVMN 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-192 |
1.54e-30 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 117.16 E-value: 1.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL---LGFVFQDFQLFPH 88
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD--LSQWDREELgrhIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 89 lTVLDNLTLSPTITMGK-----QKADAKEkaldLLARLglkehAQVY-------PYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:COG4618 421 -TIAENIARFGDADPEKvvaaaKLAGVHE----MILRL-----PDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVV 490
|
170 180 190
....*....|....*....|....*....|....*.
gi 553319313 157 YDEPTSALDPELRQTVEALIVQNREMGITQIVVTHD 192
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALKARGATVVVITHR 526
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-204 |
1.95e-30 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 112.22 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFVF 80
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLhGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKAL---DLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGRIPHRSLWAGDSPHDAAvvdRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 553319313 158 DEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR03873 162 DEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVV 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-207 |
2.26e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.52 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgidHLEN----RNLLGFVFQD--FQLFPhLTV 91
Cdd:PRK13647 22 KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENekwvRSKVGLVFQDpdDQVFS-STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNLTLSPtITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQT 171
Cdd:PRK13647 98 WDDVAFGP-VNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 553319313 172 VEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK13647 177 LMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLK 212
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-204 |
3.25e-30 |
|
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: 111.17 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKT--IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGF 78
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFpHLTVLDNltlsptITMGKQKADAKE--------KALDLLARLGLKEHAQV--YPYSLSGGQKQRVALARAM 148
Cdd:cd03251 81 VSQDVFLF-NDTVAEN------IAYGRPGATREEveeaaraaNAHEFIMELPEGYDTVIgeRGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALI---VQNRemgiTQIVVTHDLVFAEAiSDRII 204
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALerlMKNR----TTFVIAHRLSTIEN-ADRIV 207
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-203 |
7.85e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 110.59 E-value: 7.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF-GQKTIfDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgIDHLENR--NL-L 76
Cdd:COG4674 10 ILYVEDLTVSFdGFKAL-NDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDEHEiaRLgI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPHLTVLDNLTLS--------PTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:COG4674 88 GRKFQKPTVFEELTVFENLELAlkgdrgvfASL-FARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 149 MIDPQIIGYDEPTSAL-DPELRQTVEAL--IVQNRemgiTQIVVTHDLVFAEAISDRI 203
Cdd:COG4674 167 AQDPKLLLLDEPVAGMtDAETERTAELLksLAGKH----SVVVVEHDMEFVRQIARKV 220
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-204 |
7.98e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.36 E-value: 7.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQ---KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL-ENRNLL 76
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQ--DFQlFPHLTVLDNLTLSPTiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:PRK13650 84 GMVFQnpDNQ-FVGATVEDDVAFGLE-NKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 155 IGYDEPTSALDPELR----QTVEALIVQNremGITQIVVTHDLVfAEAISDRII 204
Cdd:PRK13650 162 IILDEATSMLDPEGRleliKTIKGIRDDY---QMTVISITHDLD-EVALSDRVL 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
11-204 |
1.10e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 1.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 11 FGQKTIFDgFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYnGEDVGIDHLENRNL------LGFVFQ--D 82
Cdd:PRK13634 18 FERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNKKLkplrkkVGIVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 83 FQLFPHlTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLKEHA-QVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:PRK13634 96 HQLFEE-TVEKDICFGP-MNFGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553319313 162 SALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKlHKEKGLTTVLVTHSMEDAARYADQIV 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-204 |
1.42e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.55 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF---------GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV----GI 67
Cdd:PRK10419 3 LLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 68 DHLENRNLLGFVFQDF---------------QLFPHLTVLDnltlsptitmgkqKADAKEKALDLLARLGLK-EHAQVYP 131
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisavnprktvreiirEPLRHLLSLD-------------KAERLARASEMLRAVDLDdSVLDKRP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553319313 132 YSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK10419 150 PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlQQQFGTACLFITHDLRLVERFCQRVM 223
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-204 |
1.98e-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: 114.58 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF-GQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLLGF 78
Cdd:TIGR03375 464 IEFRNVSFAYpGQETpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqIDPADLRRNIGY 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFpHLTVLDNltlsptITMGKQKADaKEKALDLLARLGLKEHAQVYP-----------YSLSGGQKQRVALARA 147
Cdd:TIGR03375 544 VPQDPRLF-YGTLRDN------IALGAPYAD-DEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARA 615
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 148 MMIDPQIIGYDEPTSALDpelrQTVEALIVQNREMGI---TQIVVTH-----DLVfaeaisDRII 204
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMD----NRSEERFKDRLKRWLagkTLVLVTHrtsllDLV------DRII 670
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-203 |
2.37e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 114.18 E-value: 2.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 27 GEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL------LGFVFQD--FQLFPHLTVLDNLtLS 98
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQR--IDTLSPGKLqalrrdIQFIFQDpyASLDPRQTVGDSI-ME 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 99 PTITMGKQKADAKEKALD-LLARLGLK-EHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELR-QTVEAL 175
Cdd:PRK10261 427 PLRVHGLLPGKAAAARVAwLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRgQIINLL 506
|
170 180
....*....|....*....|....*...
gi 553319313 176 IVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK10261 507 LDLQRDFGIAYLFISHDMAVVERISHRV 534
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-205 |
3.31e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.12 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELkNISKQFGQkTIFDgFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGeDVGIDHLENRNL----- 75
Cdd:PRK11144 1 MLEL-NFKQQLGD-LCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLFDAEKGICLppekr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 -LGFVFQDFQLFPHLTVLDNLTlsptitMGKQKADaKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:PRK11144 77 rIGYVFQDARLFPHYKVRGNLR------YGMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 155 IGYDEPTSALD-P---ELRQTVEALivqNREMGITQIVVTHDLvfaeaisDRIIR 205
Cdd:PRK11144 150 LLMDEPLASLDlPrkrELLPYLERL---AREINIPILYVSHSL-------DEILR 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
9-180 |
5.63e-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: 107.74 E-value: 5.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 9 KQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL---ESIDSGQVFYNGEDVGIDHLENRnlLGFVFQDFQL 85
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNGQPRKPDQFQKC--VAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 86 FPHLTVLDNLTLSPTITMGKQKADAKEKALD---LLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTS 162
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPRKSSDAIRKKRVedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180
....*....|....*....|..
gi 553319313 163 ALDP----ELRQTVEALIVQNR 180
Cdd:cd03234 173 GLDSftalNLVSTLSQLARRNR 194
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-201 |
6.90e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 6.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESID-----SGQVFYNGEDV---GIDHLENR 73
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIyspDVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 74 NLLGFVFQDFQLFPHLTVLDNLTLSPTIT-MGKQKADAKEKALDLLARLGL----KEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVAIGVKLNgLVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDLVFAEAISD 201
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPAQAARVSD 216
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-191 |
7.63e-29 |
|
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: 106.67 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLE-NRNLLGFVF 80
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDfQLFPHLTVLDNLTLSPTITMGKQKAdakekALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:TIGR01189 81 LP-GLKPELSALENLHFWAAIHGGAQRT-----IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 553319313 161 TSALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-203 |
3.48e-28 |
|
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: 105.56 E-value: 3.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENrnlLGFVFQ 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHK---IGSLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSpTITMGKQKADAKEkaldLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:TIGR03740 78 SPPLYENLTARENLKVH-TTLLGLPDSRIDE----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPT 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553319313 162 SALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:TIGR03740 153 NGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHI 194
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-193 |
4.65e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 4.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIF-----DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-------GIDH 69
Cdd:PRK13641 3 IKFENVDYIYSPGTPMekkglDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 70 LENRNLLGFVFQDFQLFPHlTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLKEH-AQVYPYSLSGGQKQRVALARAM 148
Cdd:PRK13641 83 LRKKVSLVFQFPEAQLFEN-TVLKDVEFGP-KNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDL 193
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNM 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-204 |
6.03e-28 |
|
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: 103.67 E-value: 6.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISkqfgQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVF 80
Cdd:cd03215 4 VLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 -----QDFQLFPHLTVLDNLTLsptitmgkqkadakekaldllarlglkehaqvyPYSLSGGQKQRVALARAMMIDPQII 155
Cdd:cd03215 80 vpedrKREGLVLDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553319313 156 GYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03215 127 ILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRIL 175
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
11-193 |
7.03e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.85 E-value: 7.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 11 FGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVfyngedvgidHLENRNLLGFVFQDFQL---FP 87
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV----------RRAGGARVAYVPQRSEVpdsLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 88 hLTVLDnltlspTITMG---------KQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:NF040873 72 -LTVRD------LVAMGrwarrglwrRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190
....*....|....*....|....*....|....*
gi 553319313 159 EPTSALDPELRQTVEALIVQNREMGITQIVVTHDL 193
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-193 |
1.38e-27 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 104.23 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQ-KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGED---VGIDHLenRNLLG 77
Cdd:cd03253 1 IEFENVTFAYDPgRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDireVTLDSL--RRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDfqlfphlTVLDNLTLSPTITMGKQKA------DAKEKAL--DLLARL-----------GLKehaqvypysLSGGQ 138
Cdd:cd03253 79 VVPQD-------TVLFNDTIGYNIRYGRPDAtdeeviEAAKAAQihDKIMRFpdgydtivgerGLK---------LSGGE 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 139 KQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDL 193
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRL 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-207 |
2.18e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 2.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIF-----DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV---GIDHLENR 73
Cdd:PRK13637 3 IKIENLTHIYMEGTPFekkalDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 74 NLLGFVFQ--DFQLFPHlTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLK--EHAQVYPYSLSGGQKQRVALARAMM 149
Cdd:PRK13637 83 KKVGLVFQypEYQLFEE-TIEKDIAFGP-INLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNKIKElHKEYNMTIILVSHSMEDVAKLADRIIVMN 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-204 |
5.85e-27 |
|
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: 106.81 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESI--DSGQVFYN------------------ 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 62 ----------GEDV---GIDHLENRNL---LGFVFQ-DFQLFPHLTVLDNLtLSPTITMGKQKADAKEKALDLLARLGLK 124
Cdd:TIGR03269 81 pcpvcggtlePEEVdfwNLSDKLRRRIrkrIAIMLQrTFALYGDDTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 125 EHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTV-EALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
.
gi 553319313 204 I 204
Cdd:TIGR03269 240 I 240
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-208 |
5.89e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.87 E-value: 5.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGI-DHLENRNLLGfv 79
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDpDVAEACHYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFqLFPHLTVLDNLTLSPTItmgkqKADAKEKALDLLARLGLKEHAQVyPY-SLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:PRK13539 80 HRNA-MKPALTVAENLEFWAAF-----LGGEELDIAAALEAVGLAPLAHL-PFgYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 159 EPTSALDPELRQTVEALIVQNREMGITQIVVTH-DLVFAEAisdRIIRVNP 208
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLPGA---RELDLGP 200
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-204 |
7.31e-27 |
|
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: 100.85 E-value: 7.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFG--QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFV 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFpHLTVLDNLtlsptitmGKQkadakekaldllarlglkehaqvypysLSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:cd03247 81 NQRPYLF-DTTLRNNL--------GRR---------------------------FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553319313 160 PTSALDPELRQTVEALIVQNREmGITQIVVTHDLVFAEAIsDRII 204
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHM-DKIL 167
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-204 |
1.10e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.31 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFV 79
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQL--------------FPHLTVLDnltlsptiTMGKQKADAKEKALDllaRLGLKEHAQVYPYSLSGGQKQRVALA 145
Cdd:PRK09536 83 PQDTSLsfefdvrqvvemgrTPHRSRFD--------TWTETDRAAVERAME---RTGVAQFADRPVTSLSGGERQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 146 RAMMIDPQIIGYDEPTSALDpeLRQTVEALIVQNR--EMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLD--INHQVRTLELVRRlvDDGKTAVAAIHDLDLAARYCDELV 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-209 |
1.69e-26 |
|
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: 99.06 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVfyngedvgidhlenrnllgfvfq 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 dfqlfphltvldnlTLSPTITMG--KQkadakekaldllarlglkehaqvypysLSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:cd03221 58 --------------TWGSTVKIGyfEQ---------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 160 PTSALDPElrqTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVNPK 209
Cdd:cd03221 97 PTNHLDLE---SIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-201 |
2.34e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.78 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLES-IDS----GQVFYNGEDV---GIDHLENR 73
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlIPGfrveGKVTFHGKNLyapDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 74 NLLGFVFQDFQLFPHlTVLDNLTLSPTITMGKQKADA-KEKALDLLA-----RLGLKEHAQvypySLSGGQKQRVALARA 147
Cdd:PRK14243 91 RRIGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDElVERSLRQAAlwdevKDKLKQSGL----SLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMgITQIVVTHDLVFAEAISD 201
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-204 |
3.12e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF------GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLEN- 72
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdEENLWDi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 RNLLGFVFQ--DFQLFPHLtVLDNLTLSPTiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:PRK13633 84 RNKAGMVFQnpDNQIVATI-VEEDVAFGPE-NLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 151 DPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHdlVFAEAI-SDRII 204
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKElNKKYGITIILITH--YMEEAVeADRII 215
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-191 |
3.21e-26 |
|
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: 105.12 E-value: 3.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL---LGFVFQDFQLFPH 88
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGAD--LKQWDRETFgkhIGYLPQDVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 89 lTVLDNltlsptITMGKQKADAKE--------KALDLLARL--GLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:TIGR01842 407 -TVAEN------IARFGENADPEKiieaaklaGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190
....*....|....*....|....*....|...
gi 553319313 159 EPTSALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-202 |
3.50e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 101.71 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 6 NISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESI-----DSGQVFYNGEDV--GIDHLENRNLLGF 78
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPhLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGL----KEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 155 IGYDEPTSALDPELRQTVEALIvqnREMG--ITQIVVTHDLVFAEAISDR 202
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFI---RSLAdrLTVIIVTHNLAQAARISDR 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
3.64e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.85 E-value: 3.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDH---LENRNLL 76
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQ--DFQLFPhLTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLkEHAQVYP-YSLSGGQKQRVALARAMMIDPQ 153
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGI-EHLKDKPtHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553319313 154 IIGYDEPTSALDPE-LRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK13636 162 VLVLDEPTAGLDPMgVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVF 213
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-204 |
4.72e-26 |
|
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: 100.25 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 16 IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLLGFVFQDFQLFpHLTVLDN 94
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLAlADPAWLRRQVGVVLQENVLF-NRSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 95 LTLS-PTITMGK-----QKADAKEKALDLlaRLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPEl 168
Cdd:cd03252 96 IALAdPGMSMERvieaaKLAGAHDFISEL--PEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYE- 172
|
170 180 190
....*....|....*....|....*....|....*....
gi 553319313 169 rqtVEALIVQNRE---MGITQIVVTHDLVfAEAISDRII 204
Cdd:cd03252 173 ---SEHAIMRNMHdicAGRTVIIIAHRLS-TVKNADRII 207
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-204 |
5.63e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 101.24 E-value: 5.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFGQKTIF-----DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV--GIDHLEN---- 72
Cdd:PRK13645 9 LDNVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpaNLKKIKEvkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 RNLLGFVFQ--DFQLFPHlTVLDNLTLSPtITMGKQKADAKEKALDLLARLGL-KEHAQVYPYSLSGGQKQRVALARAMM 149
Cdd:PRK13645 89 RKEIGLVFQfpEYQLFQE-TIEKDIAFGP-VNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-205 |
6.26e-26 |
|
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: 104.11 E-value: 6.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGF-----NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNL 75
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFtlgpiDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAyRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 LGFVFQDFQLFPHLtvldnltlsptitMGKQKADAKEKALDLLARLGLKEHAQVY-----PYSLSGGQKQRVALARAMMI 150
Cdd:COG4615 408 FSAVFSDFHLFDRL-------------LGLDGEADPARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLE 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 151 DPQIIGYDEPTSALDPELRQTV-EALIVQNREMGITQIVVTHD-LVFAEAisDRIIR 205
Cdd:COG4615 475 DRPILVFDEWAADQDPEFRRVFyTELLPELKARGKTVIAISHDdRYFDLA--DRVLK 529
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-203 |
6.79e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 6 NISKQF---GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL-ESIDS-----GQVFYNGEDV-GIDHLENRNL 75
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIfQIDAIKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 LGFVFQDFQLFPHLTVLDNLTLsPTITMG-KQKADAKEKALDLLARLGLKEhaQVY-----PYS-LSGGQKQRVALARAM 148
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAY-PLKSHGiKEKREIKKIVEECLRKVGLWK--EVYdrlnsPASqLSGGQQQRLTIARAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGItqIVVTHDLVFAEAISDRI 203
Cdd:PRK14246 169 ALKPKVLLMDEPTSMIDIVNSQAIEKLITElKNEIAI--VIVSHNPQQVARVADYV 222
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-202 |
7.31e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.97 E-value: 7.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNL--LGFV 79
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 160 PTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDR 202
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCER 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-204 |
8.95e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.45 E-value: 8.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKT-IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLEN-RNLLG 77
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdFSKLQGiRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQDFQL-FPHLTVLDNLTLSPTiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPE-NLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 157 YDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAiSDRII 204
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRII 206
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-205 |
9.22e-26 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 103.47 E-value: 9.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDS--GQVFYNGEDVGIDHLENRNLLGF 78
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 V--FQDFQLFPHLTVLDNLTLSPTITMGKQKADAK--EKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:PRK13549 85 AiiHQELALVKELSVLENIFLGNEITPGGIMDYDAmyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 155 IGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI--IR 205
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTIcvIR 217
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-204 |
1.05e-25 |
|
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: 99.33 E-value: 1.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 13 QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVF-QDFQLFPHLTV 91
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVFgQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQT 171
Cdd:cd03267 113 IDSFYLLAAI-YDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQEN 191
|
170 180 190
....*....|....*....|....*....|....
gi 553319313 172 VEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03267 192 IRNFLKEyNRERGTTVLLTSHYMKDIEALARRVL 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-203 |
3.06e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL-ENRNLLGF 78
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIrEVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQ--DFQLFPHlTVLDNLTLSPtITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:PRK13652 83 VFQnpDDQIFSP-TVEQDIAFGP-INLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 157 YDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDlPETYGMTVIFSTHQLDLVPEMADYI 208
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-206 |
3.15e-25 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 97.72 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESidsgqvfyNGEDVGIdhlenrnllgFVFQ 81
Cdd:COG2401 31 LEAFGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK--------GTPVAGC----------VDVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DFQLFPHLTVLDNLTLSPTItmgkqkADAKEkaldLLARLGLKEhAQVY--PYS-LSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:COG2401 93 DNQFGREASLIDAIGRKGDF------KDAVE----LLNAVGLSD-AVLWlrRFKeLSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 159 EPTSALDPELRQTVeALIVQN--REMGITQIVVTHDLVFAEAIS-DRIIRV 206
Cdd:COG2401 162 EFCSHLDRQTAKRV-ARNLQKlaRRAGITLVVATHHYDVIDDLQpDLLIFV 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-207 |
4.03e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 98.67 E-value: 4.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIF--DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLLG 77
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQ--DFQlFPHLTV-------LDNLTLsPTITMgkqkadaKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:PRK13648 87 IVFQnpDNQ-FVGSIVkydvafgLENHAV-PYDEM-------HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLvfAEAI-SDRIIRVN 207
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKvKSEHNITIISITHDL--SEAMeADHVIVMN 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2-203 |
6.23e-25 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 101.14 E-value: 6.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF-GQKTIfDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-----------GIdh 69
Cdd:PRK11288 5 LSFDGIGKTFpGVKAL-DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasttaalaaGV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 70 lenrnllGFVFQDFQLFPHLTVLDNLTLS--PTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARA 147
Cdd:PRK11288 82 -------AIIYQELHLVPEMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 148 MMIDPQIIGYDEPTSALD-PELRQTVeALIVQNREMGITQIVVTH--DLVFaeAISDRI 203
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSaREIEQLF-RVIRELRAEGRVILYVSHrmEEIF--ALCDAI 210
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-203 |
6.72e-25 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.01 E-value: 6.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDH-LENRNLLGF 78
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNkLDHkLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTLSPTIT---MGKQKADAKE---KALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDP 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTkkvCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 153 QIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRY 215
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-191 |
7.00e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.28 E-value: 7.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDG-----FNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN---- 72
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 73 -RNLLGFVFQ--DFQLFPHlTVLDNLTLSPTiTMGKQKADAKEKALDLLARLGLKEHA-QVYPYSLSGGQKQRVALARAM 148
Cdd:PRK13649 83 iRKKVGLVFQfpESQLFEE-TVLKDVAFGPQ-NFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-204 |
1.14e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 98.66 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFG-QKTIF---DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLesID-SGQVF-----YNGEDV-GIDH 69
Cdd:PRK11022 3 LLNVDKLSVHFGdESAPFravDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL--IDyPGRVMaekleFNGQDLqRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 70 LENRNLLG----FVFQD--FQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHA---QVYPYSLSGGQKQ 140
Cdd:PRK11022 81 KERRNLVGaevaMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 141 RVALARAMMIDPQIIGYDEPTSALDPELR-QTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQaQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-204 |
1.25e-24 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 97.17 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIF---------DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGI-DHL 70
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWfrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFgDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 ENRNLLGFVFQD--FQLFPHLTVLDNLTLsPTITMGKQKADAKEKALDL-LARLGLK-EHAQVYPYSLSGGQKQRVALAR 146
Cdd:PRK15112 84 YRSQRIRMIFQDpsTSLNPRQRISQILDF-PLRLNTDLEPEQREKQIIEtLRQVGLLpDHASYYPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 147 AMMIDPQIIGYDEPTSALDPELRQTVEALIVQNRE-MGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEkQGISYIYVTQHLGMMKHISDQVL 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
2-191 |
2.63e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 95.90 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLES--IDSGQVFYNGEDvgIDHL--ENRNLLG 77
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGED--ILELspDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 fVFQDFQL---FPHLTVLDNLTLSPTITMGKQK--ADAKEKALDLLARLGL-KEHAQVY-PYSLSGGQKQRVALARAMMI 150
Cdd:COG0396 79 -IFLAFQYpveIPGVSVSNFLRTALNARRGEELsaREFLKLLKEKMKELGLdEDFLDRYvNEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553319313 151 DPQIIGYDEPTSALDPE----LRQTVEALivQNREMGItqIVVTH 191
Cdd:COG0396 158 EPKLAILDETDSGLDIDalriVAEGVNKL--RSPDRGI--LIITH 198
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-203 |
4.34e-24 |
|
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: 94.48 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLE-NRNLLGFVF 80
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSiARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDfQLFPHLTVLDNLTLSPTItmgkqkaDAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:cd03231 81 AP-GIKTTLSVLENLRFWHAD-------HSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553319313 161 TSALDPELRQTVEALIVQNREMGITQIVVTH-DLVFAEAISDRI 203
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-204 |
4.36e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 4.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKqfgqKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL---------- 70
Cdd:COG1129 256 VLEVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrdairagiay 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 --ENRNLLGfvfqdfqLFPHLTVLDNLTLSptiTMGK-------QKADAKEKALDLLARLGLK---EHAQVypYSLSGGQ 138
Cdd:COG1129 332 vpEDRKGEG-------LVLDLSIRENITLA---SLDRlsrggllDRRRERALAEEYIKRLRIKtpsPEQPV--GNLSGGN 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 139 KQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLvfAE--AISDRII 204
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSEL--PEllGLSDRIL 465
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
12-204 |
6.14e-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: 94.52 E-value: 6.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIdhLEnrnlLGFVFQdfqlfPHLTV 91
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSL--LG----LGGGFN-----PELTG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNLTLSPTItMGKQKADAKEKALDLLARLGLKEHAQvYPYS-LSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQ 170
Cdd:cd03220 102 RENIYLNGRL-LGLSRKEIDEKIDEIIEFSELGDFID-LPVKtYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179
|
170 180 190
....*....|....*....|....*....|....
gi 553319313 171 TVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDPSSIKRLCDRAL 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-193 |
7.27e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 95.08 E-value: 7.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidhlenrnllgfVF 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS------------ML 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSPT-ITMGKQKADAKEKALDLLARLGLKEHAQVYPY---------------SLSGGQKQRVAL 144
Cdd:PRK11231 70 SSRQLARRLALLPQHHLTPEgITVRELVAYGRSPWLSLWGRLSAEDNARVNQAmeqtrinhladrrltDLSGGQRQRAFL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 145 ARAMMIDPQIIGYDEPTSALDpeLRQTVE--ALIVQNREMGITQIVVTHDL 193
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD--INHQVElmRLMRELNTQGKTVVTVLHDL 198
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-204 |
9.37e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 94.61 E-value: 9.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL------ENRN 74
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 75 LL----GFVFQDfqlfphltVLDNltLSPTITMG------------KQKADAKEKALDLLARLGLKEhAQV--YPYSLSG 136
Cdd:PRK11701 86 LLrtewGFVHQH--------PRDG--LRMQVSAGgnigerlmavgaRHYGDIRATAGDWLERVEIDA-ARIddLPTTFSG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 137 GQKQRVALARAMMIDPQIIGYDEPTSALDPE--------LRQTVealivqnREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSvqarlldlLRGLV-------RELGLAVVIVTHDLAVARLLAHRLL 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-202 |
9.43e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.56 E-value: 9.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLEN----RNLL 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKD--ITDWQTakimREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVypYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRA--GTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 157 YDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDR 202
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-209 |
1.54e-23 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 97.27 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNgedvgidhlENRNlLGFVFQ 81
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS---------ENAN-IGYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 DfqlfpHLTVLDN-LTLSPTITMGKQKADAKEKALDLLARL-----GLKEHAQVypysLSGGQKQRVALARAMMIDPQII 155
Cdd:PRK15064 390 D-----HAYDFENdLTLFDWMSQWRQEGDDEQAVRGTLGRLlfsqdDIKKSVKV----LSGGEKGRMLFGKLMMQKPNVL 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 156 GYDEPTSALDPElrqTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVNPK 209
Cdd:PRK15064 461 VMDEPTNHMDME---SIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPD 511
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-201 |
1.71e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDS-----GQVFYNGED-----VGIDHLe 71
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNiyerrVNLNRL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 72 nRNLLGFVFQDFQLFPhLTVLDNLTLSPTITMGKQKADAKE------KALDLLARLGLKEHAQVYpySLSGGQKQRVALA 145
Cdd:PRK14258 87 -RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDivesalKDADLWDEIKHKIHKSAL--DLSGGQQQRLCIA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 146 RAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNR-EMGITQIVVTHDLVFAEAISD 201
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-203 |
2.34e-23 |
|
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: 96.82 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDS--GQVFYNGEDVGIDHLENRNLLGF 78
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VF--QDFQLFPHLTVLDNLTLSPTITMGKQKADAKE---KALDLLARLGLKEHAQVYPYS-LSGGQKQRVALARAMMIDP 152
Cdd:TIGR02633 81 VIihQELTLVPELSVAENIFLGNEITLPGGRMAYNAmylRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 153 QIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTI 211
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-204 |
2.38e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.18 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF----GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL---ESIDSGQVFYNGEDvgIDHLENR 73
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGRE--ILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 74 NL-------LGFVFQD--FQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQ---VYPYSLSGGQKQR 141
Cdd:PRK09473 90 ELnklraeqISMIFQDpmTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKrmkMYPHEFSGGMRQR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 142 VALARAMMIDPQIIGYDEPTSALDpelrQTVEALIVQ-----NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALD----VTVQAQIMTllnelKREFNTAIIMITHDLGVVAGICDKVL 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-207 |
3.58e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 93.25 E-value: 3.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVfyngedvgidHLENRNLLGFVF 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPH--LTVLDNLTLSPtitmGKQKADakekALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:PRK09544 74 QKLYLDTTlpLTVNRFLRLRP----GTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 159 EPTSALDPELRQTVEALIVQNR-EMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRrELDCAVLMVSHDLHLVMAKTDEVLCLN 195
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
8-191 |
5.36e-23 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.88 E-value: 5.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 8 SKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESID---SGQVFYNGEDVGIDhlENRNLLGFVFQDFQ 84
Cdd:TIGR00955 32 CRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAK--EMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 85 LFPHLTVLDNLTLSPTITMGKQKAdAKEKAL---DLLARLGLKEHAQV------YPYSLSGGQKQRVALARAMMIDPQII 155
Cdd:TIGR00955 110 FIPTLTVREHLMFQAHLRMPRRVT-KKEKRErvdEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 553319313 156 GYDEPTSALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
16-197 |
6.19e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.94 E-value: 6.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 16 IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGED-VGIDHLENRNLLGFVFQDFQLFPHlTVLDN 94
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPlVQYDHHYLHRQVALVGQEPVLFSG-SVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 95 LTLSPTIT-MGKQKADAKEK-ALDLLARLGLKEHAQVYPYS--LSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQ 170
Cdd:TIGR00958 575 IAYGLTDTpDEEIMAAAKAAnAHDFIMEFPNGYDTEVGEKGsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180
....*....|....*....|....*..
gi 553319313 171 TVEALivqNREMGITQIVVTHDLVFAE 197
Cdd:TIGR00958 655 LLQES---RSRASRTVLLIAHRLSTVE 678
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-204 |
9.99e-23 |
|
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: 91.38 E-value: 9.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 16 IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGI-DHLENRNLLGFVFQDFQLFPHlTVLDN 94
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 95 LTLS-PTITMGKQKADA-KEKALDLLARL--GLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQ 170
Cdd:cd03248 108 IAYGlQSCSFECVKEAAqKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQ 187
|
170 180 190
....*....|....*....|....*....|....
gi 553319313 171 TVEALIVQNREmGITQIVVTHDLVFAEAiSDRII 204
Cdd:cd03248 188 QVQQALYDWPE-RRTVLVIAHRLSTVER-ADQIL 219
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-205 |
1.29e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 94.47 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDS--GQVFYNGEDVGIDHLENRNLLGF 78
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VF--QDFQLFPHLTVLDNLTLsptitmGKQKA--------DAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAM 148
Cdd:NF040905 81 VIihQELALIPYLSIAENIFL------GNERAkrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 149 MIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI--IR 205
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSItvLR 213
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-203 |
1.40e-22 |
|
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: 95.08 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQF---GQKTIfDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVF 80
Cdd:TIGR01257 931 VKNLVKIFepsGRPAV-DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLK-GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 161 TSALDPELRQTVEALIVQNREmGITQIVVTHDLVFAEAISDRI 203
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRI 1130
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-204 |
1.49e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 94.65 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKtifdGF-----NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNL 75
Cdd:PRK10522 323 LELRNVTFAYQDN----GFsvgpiNLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDyRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 LGFVFQDFQLFPHLtvldnltlsptitMGKQKADAKEKALDL-LARLGLK-----EHAQVYPYSLSGGQKQRVALARAMM 149
Cdd:PRK10522 399 FSAVFTDFHLFDQL-------------LGPEGKPANPALVEKwLERLKMAhklelEDGRISNLKLSKGQKKRLALLLALA 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 150 IDPQIIGYDEPTSALDPELRQTV-EALIVQNREMGITQIVVTH-DLVFAEAisDRII 204
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFyQVLLPLLQEMGKTIFAISHdDHYFIHA--DRLL 520
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-204 |
1.58e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 92.84 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF-----------GQKTIF----------DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVF 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgALKGLFrreyreveavDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 60 YNGEDVGIDHLENRNLLGFVF-QDFQLFPHLTVLDNLTLSPTItMGKQKADAKEKaLDLLA-RLGLKE--HAQVypYSLS 135
Cdd:COG4586 81 VLGYVPFKRRKEFARRIGVVFgQRSQLWWDLPAIDSFRLLKAI-YRIPDAEYKKR-LDELVeLLDLGEllDTPV--RQLS 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 136 GGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEyNRERGTTILLTSHDMDDIEALCDRVI 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-204 |
1.79e-22 |
|
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: 94.42 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFG-QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLLGFV 79
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHlTVLDNLTLSP----TITMGKQKADAKEKALDLLA-RLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAkenvSQDEIWAACEIAEIKDDIENmPLGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 155 IGYDEPTSALDPEL-RQTVEALIVQNREmgiTQIVVTHDLVFAEAiSDRII 204
Cdd:TIGR01193 633 LILDESTSNLDTITeKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKII 679
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-204 |
2.32e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.91 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF----------------------GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQV 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 59 FYNGEDVGIdhLEnrnlLGFVFQdfqlfPHLTVLDNLTLSPTItMGKQKADAKEKALDLL--ARLGLKEHAQVYPYSlSg 136
Cdd:COG1134 84 EVNGRVSAL--LE----LGAGFH-----PELTGRENIYLNGRL-LGLSRKEIDEKFDEIVefAELGDFIDQPVKTYS-S- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 137 GQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAI 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-164 |
2.44e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 93.91 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF-GQKTIfDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-----------GId 68
Cdd:PRK10762 4 LLQLKGIDKAFpGVKAL-SGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeaGI- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 69 hlenrnllGFVFQDFQLFPHLTVLDNLTLS--PTITMGK-------QKADAkekaldLLARLGLKEHAQVYPYSLSGGQK 139
Cdd:PRK10762 82 --------GIIHQELNLIPQLTIAENIFLGreFVNRFGRidwkkmyAEADK------LLARLNLRFSSDKLVGELSIGEQ 147
|
170 180
....*....|....*....|....*
gi 553319313 140 QRVALARAMMIDPQIIGYDEPTSAL 164
Cdd:PRK10762 148 QMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
11-191 |
2.81e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.72 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 11 FGQKTIFDgFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL-----ESIDSGQVFYNGEDVGIDHLENRNLLGFVFQ--DF 83
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlqpteGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 84 QLFPHlTVLDNLTLSPTiTMGKQKADAKEKALDLLARLGL-KEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTS 162
Cdd:PRK13643 96 QLFEE-TVLKDVAFGPQ-NFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTA 173
|
170 180
....*....|....*....|....*....
gi 553319313 163 ALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:PRK13643 174 GLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-193 |
3.65e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.49 E-value: 3.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLLGFVF 80
Cdd:PRK13657 336 EFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASlRRNIAVVF 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFphltvldNLTLSPTITMGKQKADAKE--------KALDLLAR--LGLKEHAQVYPYSLSGGQKQRVALARAMMI 150
Cdd:PRK13657 416 QDAGLF-------NRSIEDNIRVGRPDATDEEmraaaeraQAHDFIERkpDGYDTVVGERGRQLSGGERQRLAIARALLK 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 151 DPQIIGYDEPTSALDPELRQTV-EAL--IVQNRemgiTQIVVTHDL 193
Cdd:PRK13657 489 DPPILILDEATSALDVETEAKVkAALdeLMKGR----TTFIIAHRL 530
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-203 |
5.42e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGidHLE--NRNLLG- 77
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCA--RLTpaKAHQLGi 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 -FVFQDFQLFPHLTVLDNltlsptITMGKQK-ADAKEKALDLLARLG--LKEHAQVypYSLSGGQKQRVALARAMMIDPQ 153
Cdd:PRK15439 89 yLVPQEPLLFPNLSVKEN------ILFGLPKrQASMQKMKQLLAALGcqLDLDSSA--GSLEVADRQIVEILRGLMRDSR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 553319313 154 IIGYDEPTSALDPelrQTVEALIVQNREM---GITQIVVTHDLVFAEAISDRI 203
Cdd:PRK15439 161 ILILDEPTASLTP---AETERLFSRIRELlaqGVGIVFISHKLPEIRQLADRI 210
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-191 |
7.14e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 92.88 E-value: 7.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQD 82
Cdd:NF033858 268 EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 83 FQLFPHLTVLDNLTLS------PtitmgkqKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:NF033858 348 FSLYGELTVRQNLELHarlfhlP-------AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190
....*....|....*....|....*....|....*.
gi 553319313 157 YDEPTSALDPELR-QTVEALIVQNREMGITQIVVTH 191
Cdd:NF033858 421 LDEPTSGVDPVARdMFWRLLIELSREDGVTIFISTH 456
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-203 |
2.14e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQ----KTIFDGFNLTVQDGEVLSLVGPSGGGKT-TLLRMLAGLES----IDSGQVFYNGEDVgiDHLE 71
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSppvvYPSGDIRFHGESL--LHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 72 NRNLLG-------FVFQD--FQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQV---YPYSLSGGQK 139
Cdd:PRK15134 83 EQTLRGvrgnkiaMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGER 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 140 QRVALARAMMIDPQIIGYDEPTSALDpelrQTVEALIVQ-----NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALD----VSVQAQILQllrelQQELNMGLLFITHNLSIVRKLADRV 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-193 |
7.01e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 7.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTT----LLRMLAGlesidSGQVFYNGEDvgIDHLENRNLLGF------VFQ 81
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQP--LHNLNRRQLLPVrhriqvVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 82 D--FQLFPHLTVL----DNLTL-SPTITMGKQKadakEKALDLLARLGLK-EHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:PRK15134 370 DpnSSLNPRLNVLqiieEGLRVhQPTLSAAQRE----QQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 154 IIGYDEPTSALDpelrQTVEALI------VQNREmGITQIVVTHDL 193
Cdd:PRK15134 446 LIILDEPTSSLD----KTVQAQIlallksLQQKH-QLAYLFISHDL 486
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-204 |
9.08e-21 |
|
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: 89.49 E-value: 9.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 15 TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGFVFQDfqlfphlTVLD 93
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrDVTQASLRAAIGIVPQD-------TVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 94 NLTLSPTITMGKQKADAKE-----KA---LDLLARL-----------GLKehaqvypysLSGGQKQRVALARAMMIDPQI 154
Cdd:COG5265 445 NDTIAYNIAYGRPDASEEEveaaaRAaqiHDFIESLpdgydtrvgerGLK---------LSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 155 IGYDEPTSALDPELRQTV-EAL--IVQNRemgiTQIVVTHDL-VFAEAisDRII 204
Cdd:COG5265 516 LIFDEATSALDSRTERAIqAALreVARGR----TTLVIAHRLsTIVDA--DEIL 563
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-165 |
1.11e-20 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 89.17 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 8 SKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL--ESIDSGQVFYNGEDVGIDHLENrnlLGFVFQDFQL 85
Cdd:PLN03211 75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQILKR---TGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 86 FPHLTVLDNLTLSPTITMGKQ--KADAKEKALDLLARLGLKEHAQV-----YPYSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:PLN03211 152 YPHLTVRETLVFCSLLRLPKSltKQEKILVAESVISELGLTKCENTiignsFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
....*..
gi 553319313 159 EPTSALD 165
Cdd:PLN03211 232 EPTSGLD 238
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-191 |
1.19e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 89.10 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 14 KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQvfyngedvgIDHLENRNLLgFVFQDfqlfPHL---T 90
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR---------IARPAGARVL-FLPQR----PYLplgT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 91 VLDNLT---LSPTITmgkqkaDAK-EKAL------DLLARLGLKEH-AQVypysLSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:COG4178 442 LREALLypaTAEAFS------DAElREALeavglgHLAERLDEEADwDQV----LSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 553319313 160 PTSALDPELRQTVEALIvQNREMGITQIVVTH 191
Cdd:COG4178 512 ATSALDEENEAALYQLL-REELPGTTVISVGH 542
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-207 |
2.13e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.39 E-value: 2.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 13 QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL---ESIDSGQVFYNGEDVGIDHLEN-RNLLGFVFQ--DFQlF 86
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDiREKVGIVFQnpDNQ-F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 87 PHLTVLDNLTLSPTiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDP 166
Cdd:PRK13640 98 VGATVGDDVAFGLE-NRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553319313 167 ELRQTVEALIVQ-NREMGITQIVVTHDLVFAEaISDRIIRVN 207
Cdd:PRK13640 177 AGKEQILKLIRKlKKKNNLTVISITHDIDEAN-MADQVLVLD 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-204 |
4.60e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.22 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgidhLENRNLLGFVFQDF 83
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP-----LESWSSKAFARKVA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 84 QLFPHLTVLDNLTLSPTITMGKQ---------KADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:PRK10575 89 YLPQQLPAAEGMTVRELVAIGRYpwhgalgrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 155 IGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRlSQERGLTVIAVLHDINMAARYCDYLV 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-207 |
7.07e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.83 E-value: 7.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNG-------EDVGIDHLenRNLLGFVFQ--DFQLFPHlTV 91
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPV--RKRIGMVFQfpESQLFED-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNLTLSPTiTMGKQKADAKEKALDLLARLGLKEHA-QVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQ 170
Cdd:PRK13646 104 EREIIFGPK-NFKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKR 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 553319313 171 TVEALIVQ-NREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:PRK13646 183 QVMRLLKSlQTDENKTIILVSHDMNEVARYADEVIVMK 220
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-191 |
1.76e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.19 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLES--IDSGQVFYNGEDvgIDHL--ENRNLLG 77
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGED--ITDLppEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 fVFQDFQLFPHLtvldnltlsPTITMGkqkadakekalDLLARLGlkehaqvypYSLSGGQKQRVALARAMMIDPQIIGY 157
Cdd:cd03217 79 -IFLAFQYPPEI---------PGVKNA-----------DFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190
....*....|....*....|....*....|....
gi 553319313 158 DEPTSALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-193 |
2.27e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 85.28 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIdSGQVFYNG-EDVGIDHLENRNLLGFVFQDFQLFpHLTVLDNLTLS- 98
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGiELRELDPESWRKHLSWVGQNPQLP-HGTLRDNVLLGn 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 99 PTITMGK-QKADAKEKALDLLARL--GL----KEHAQvypySLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQT 171
Cdd:PRK11174 448 PDASDEQlQQALENAWVSEFLPLLpqGLdtpiGDQAA----GLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQL 523
|
170 180
....*....|....*....|....
gi 553319313 172 V-EALivqNREM-GITQIVVTHDL 193
Cdd:PRK11174 524 VmQAL---NAASrRQTTLMVTHQL 544
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-203 |
5.99e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 83.03 E-value: 5.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF----GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESiDSGQV-----FYNGedvgIDHL- 70
Cdd:COG4170 3 LLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITK-DNWHVtadrfRWNG----IDLLk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 ----ENRNLLG----FVFQDFQ--LFPHLTVLDNLTLS-PTITMG----KQKADAKEKALDLLARLGLKEHAQV---YPY 132
Cdd:COG4170 78 lsprERRKIIGreiaMIFQEPSscLDPSAKIGDQLIEAiPSWTFKgkwwQRFKWRKKRAIELLHRVGIKDHKDImnsYPH 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 133 SLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPelrqTVEALIV-------QNREMGItqIVVTHDLVFAEAISDRI 203
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMES----TTQAQIFrllarlnQLQGTSI--LLISHDLESISQWADTI 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
21-191 |
1.07e-18 |
|
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: 79.12 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQvfyngedvgIDHLENRNLLgFVFQDfqlfPHLtvldnltlsPT 100
Cdd:cd03223 21 SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR---------IGMPEGEDLL-FLPQR----PYL---------PL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 101 ITmgkqkadakekaldllarlgLKEhAQVYPYS--LSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIvq 178
Cdd:cd03223 78 GT--------------------LRE-QLIYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL-- 134
|
170
....*....|...
gi 553319313 179 nREMGITQIVVTH 191
Cdd:cd03223 135 -KELGITVISVGH 146
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
8-204 |
1.20e-18 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 80.21 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 8 SKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEdvgidhlenrnlLGFVFQdfqlFP 87
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQ----EP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 88 HL---TVLDNltlsptITMGKQKADAK-EKALDLLArlgLKEHAQVYPY-----------SLSGGQKQRVALARAMMIDP 152
Cdd:cd03250 76 WIqngTIREN------ILFGKPFDEERyEKVIKACA---LEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 153 QIIGYDEPTSALDPElrqtVEALIVQNREMGI-----TQIVVTHDLVFAEAiSDRII 204
Cdd:cd03250 147 DIYLLDDPLSAVDAH----VGRHIFENCILGLllnnkTRILVTHQLQLLPH-ADQIV 198
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-204 |
1.28e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 81.68 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKT---IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLL 76
Cdd:PRK13642 4 ILEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNlRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQ--DFQlFPHLTVLDNLTLSPTiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQI 154
Cdd:PRK13642 84 GMVFQnpDNQ-FVGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 155 IGYDEPTSALDPELRQTVEALIVQNRE-MGITQIVVTHDLVFAeAISDRII 204
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEkYQLTVLSITHDLDEA-ASSDRIL 211
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-203 |
1.46e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 82.16 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQF----GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLeSIDSGQVF---YNGEDVGIDHL--- 70
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTadrMRFDDIDLLRLspr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 71 ENRNLLG----FVFQDFQlfphlTVLDnltlsPTITMGKQKADA-----------------KEKALDLLARLGLKEHAQV 129
Cdd:PRK15093 82 ERRKLVGhnvsMIFQEPQ-----SCLD-----PSERVGRQLMQNipgwtykgrwwqrfgwrKRRAIELLHRVGIKDHKDA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 130 ---YPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQ-NREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK15093 152 mrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-205 |
1.55e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.95 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISkqFG----QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgIDHLEN--RNL 75
Cdd:PRK11160 339 LTLNNVS--FTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEAalRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 LGFVFQDFQLFPHlTVLDNLTL-SPTITmgkqkadaKEKALDLLARLGLKEHAQVYP----------YSLSGGQKQRVAL 144
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLLLaAPNAS--------DEALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGI 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 145 ARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREmGITQIVVTHDLVFAEAIsDRIIR 205
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRLTGLEQF-DRICV 545
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-204 |
2.09e-18 |
|
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: 82.68 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYnGEDVGI-------DHLENRN 74
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLayvdqsrDALDPNK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 75 LlgfVFQDfqlfphltVLDNLTLsptITMGKQKADAKEkaldLLARLGLKEHAQVYPYS-LSGGQKQRVALARAMMIDPQ 153
Cdd:TIGR03719 402 T---VWEE--------ISGGLDI---IKLGKREIPSRA----YVGRFNFKGSDQQKKVGqLSGGERNRVHLAKTLKSGGN 463
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 553319313 154 IIGYDEPTSALDPE-LRQTVEALIvqnrEMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR03719 464 VLLLDEPTNDLDVEtLRALEEALL----NFAGCAVVISHDRWFLDRIATHIL 511
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
17-204 |
3.46e-18 |
|
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: 82.14 E-value: 3.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 17 FDGFNLTVQDG-----EVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFyngEDVGI----DHLEnrnllgfvfQDFQLfp 87
Cdd:COG1245 351 YGGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLKIsykpQYIS---------PDYDG-- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 88 hlTVLDNL--TLSPTITMGKQKADakekaldLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALD 165
Cdd:COG1245 417 --TVEEFLrsANTDDFGSSYYKTE-------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 553319313 166 PELRQTVEALI---VQNRemGITQIVVTHDLVFAEAISDRII 204
Cdd:COG1245 488 VEQRLAVAKAIrrfAENR--GKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-193 |
3.97e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDvgIDHLENRNL---LGF 78
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEH--IQHYASKEVarrIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDfqlfphLTVLDNLTLSPTITMG------------KQKADAKEKALDllaRLGLKEHAQVYPYSLSGGQKQRVALAR 146
Cdd:PRK10253 86 LAQN------ATTPGDITVQELVARGryphqplftrwrKEDEEAVTKAMQ---ATGITHLADQSVDTLSGGQRQRAWIAM 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 147 AMMIDPQIIGYDEPTSALDPELR-QTVEALIVQNREMGITQIVVTHDL 193
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLDISHQiDLLELLSELNREKGYTLAAVLHDL 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-204 |
4.94e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 81.39 E-value: 4.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGqktifdGFNLTVQDG-----EVLSLVGPSGGGKTTLLRMLAGLESIDSGQVF------YNGEDVGIDh 69
Cdd:PRK13409 340 LVEYPDLTKKLG------DFSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkisYKPQYIKPD- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 70 lenrnllgfvfqdfqlfPHLTVLDNLtlsptitmGKQKADAKEKAL--DLLARLGLKEHAQVYPYSLSGGQKQRVALARA 147
Cdd:PRK13409 413 -----------------YDGTVEDLL--------RSITDDLGSSYYksEIIKPLQLERLLDKNVKDLSGGELQRVAIAAC 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALI---VQNREMgiTQIVVTHDLVFAEAISDRII 204
Cdd:PRK13409 468 LSRDADLYLLDEPSAHLDVEQRLAVAKAIrriAEEREA--TALVVDHDIYMIDYISDRLM 525
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-204 |
8.08e-18 |
|
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: 78.30 E-value: 8.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF--GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-GIDHLENRNLLGF 78
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIsKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHlTVLDNLtlSPTitmgKQKADakEKALDLLARLGLKEHAQVYPYSL-----------SGGQKQRVALARA 147
Cdd:cd03244 83 IPQDPVLFSG-TIRSNL--DPF----GEYSD--EELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALIvqnREM--GITQIVVTHDLvfaEAI--SDRII 204
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTI---REAfkDCTVLTIAHRL---DTIidSDRIL 208
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-191 |
1.44e-17 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 77.58 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 16 IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgiDHLENRNLLGFVFQDFQLFPHLTVLDNL 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTA--TRGDRSRFMAYLGHLPGLKADLSTLENL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 96 TLsptiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEAL 175
Cdd:PRK13543 104 HF----LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|....*.
gi 553319313 176 IVQNREMGITQIVVTH 191
Cdd:PRK13543 180 ISAHLRGGGAALVTTH 195
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-191 |
1.55e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 76.91 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVF 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSPTITMGKQKadakekaLDLLARLGLKEHAQVYPYS-LSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:PRK13540 81 HRSGINPYLTLRENCLYDIHFSPGAVG-------ITELCRLFSLEHLIDYPCGlLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|..
gi 553319313 160 PTSALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-204 |
1.62e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNIS-KQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-----------GIDH 69
Cdd:COG3845 258 LEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprerrrlGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 70 L-ENRNLLGfvfqdfqLFPHLTVLDNLTLSPTITMGKQK------ADAKEKALDLLARLGLK---EHAQVypYSLSGGQK 139
Cdd:COG3845 338 IpEDRLGRG-------LVPDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEFDVRtpgPDTPA--RSLSGGNQ 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 553319313 140 QRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDL--VFaeAISDRII 204
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLdeIL--ALSDRIA 473
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-203 |
2.04e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDH---LENRNLLG 77
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrglLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFQD--FQLFphLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQII 155
Cdd:PRK13638 81 TVFQDpeQQIF--YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 156 GYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK13638 159 LLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAV 206
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-193 |
2.97e-17 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 22 LTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVgiDHLENRNLLGFVFQDFQL---FPHLtVLDNLTLS 98
Cdd:PRK15056 28 FTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT--RQALQKNLVAYVPQSEEVdwsFPVL-VEDVVMMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 99 PTITMG---KQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEAL 175
Cdd:PRK15056 105 RYGHMGwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISL 184
|
170
....*....|....*...
gi 553319313 176 IVQNREMGITQIVVTHDL 193
Cdd:PRK15056 185 LRELRDEGKTMLVSTHNL 202
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-204 |
8.97e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 8.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFGQKTIFDGFNLT-------------VQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV----- 65
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVTsrdrkkvrdisfsVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprsp 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 66 ------GIDHL-ENRNLLGFvfqdfqlFPHLTVLDNLTLSPTITMGKQKA--------DAKEKALDLLARLGLKEHA-QV 129
Cdd:PRK09700 333 ldavkkGMAYItESRRDNGF-------FPNFSIAQNMAISRSLKDGGYKGamglfhevDEQRTAENQRELLALKCHSvNQ 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 130 YPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIA 480
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-204 |
1.18e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 77.68 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGeDVGIDHLEN---RNLLG 77
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVARLQQdppRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 FVFqDF----------QLFPHLTVLDNLTLSPTITMGKQKADAKEKaLD-------------LLARLGLKEHAQVYpySL 134
Cdd:PRK11147 82 TVY-DFvaegieeqaeYLKRYHDISHLVETDPSEKNLNELAKLQEQ-LDhhnlwqlenrineVLAQLGLDPDAALS--SL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 135 SGGQKQRVALARAMMIDPQIIGYDEPTSALDPElrqTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIE---TIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIV 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-204 |
2.34e-16 |
|
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: 74.75 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFNLTVQ-----DGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-------IDH-LENRNLLGFVFQDFQ 84
Cdd:cd03237 11 GEFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikADYeGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 85 LFPHLT--VLDNLTLsptitmgkqkadakEKALDLLARlglkehaqvypySLSGGQKQRVALARAMMIDPQIIGYDEPTS 162
Cdd:cd03237 91 THPYFKteIAKPLQI--------------EQILDREVP------------ELSGGELQRVAIAACLSKDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553319313 163 ALDPELRQTVEALI---VQNREMgiTQIVVTHDLVFAEAISDRII 204
Cdd:cd03237 145 YLDVEQRLMASKVIrrfAENNEK--TAFVVEHDIIMIDYLADRLI 187
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-206 |
2.50e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.60 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLLGFVFQDFQLFphltvldNLTLSP 99
Cdd:PRK11176 363 NFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASlRNQVALVSQNVHLF-------NDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 100 TITMGKQKADAKEK---------ALDLLARL--GLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPEL 168
Cdd:PRK11176 436 NIAYARTEQYSREQieeaarmayAMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 553319313 169 RQTVEALIVQ---NRemgiTQIVVTHDLVFAEAiSDRIIRV 206
Cdd:PRK11176 516 ERAIQAALDElqkNR----TSLVIAHRLSTIEK-ADEILVV 551
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-193 |
3.82e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.35 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQfGQKTIFDGFNLTVQDGEVLSLVGPSGGGKT----TLLRML-AGLESIdSGQVFYNGEDVGIDHLENRNLL 76
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGVRQT-AGRVLLDGKPVAPCALRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 gfvfqdfqlfphlTVLDN--LTLSPTITM-----------GKQKADAKekALDLLARLGLKEHAQV---YPYSLSGGQKQ 140
Cdd:PRK10418 83 -------------TIMQNprSAFNPLHTMhtharetclalGKPADDAT--LTAALEAVGLENAARVlklYPFEMSGGMLQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 141 RVALARAMMIDPQIIGYDEPTSALDPELRQTVEAL---IVQNREMGItqIVVTHDL 193
Cdd:PRK10418 148 RMMIALALLCEAPFIIADEPTTDLDVVAQARILDLlesIVQKRALGM--LLVTHDM 201
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
19-193 |
8.42e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 8.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 19 GFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESiDSGQVFYNGEDVG-IDHLENRNLLGFVFQDFQLFPHLTVLDNLTL 97
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSdWSAAELARHRAYLSQQQSPPFAMPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 98 S-PtitmGKQKADAKEKALDLLA-RLGL--KEHAQVypYSLSGGQKQRVALARAMM-IDPQIIGY------DEPTSALDP 166
Cdd:COG4138 93 HqP----AGASSEAVEQLLAQLAeALGLedKLSRPL--TQLSGGEWQRVRLAAVLLqVWPTINPEgqllllDEPMNSLDV 166
|
170 180
....*....|....*....|....*..
gi 553319313 167 ELRQTVEALIVQNREMGITQIVVTHDL 193
Cdd:COG4138 167 AQQAALDRLLRELCQQGITVVMSSHDL 193
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-203 |
1.06e-15 |
|
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: 73.17 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 23 TVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGE-DVGIDHLENRNLlgfvfQDFqlfphLTVLDNLTLSPTI 101
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDwDEILDEFRGSEL-----QNY-----FTKLLEGDVKVIV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 102 -----------TMGK-----QKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALD 165
Cdd:cd03236 92 kpqyvdlipkaVKGKvgellKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 553319313 166 PELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:cd03236 172 IKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYI 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-207 |
1.07e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 75.07 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 54 DSGQVFYNGEDVGIDHLEN-RNLLGFVFQDFQLFphltvldNLTLSPTITMGKQKA---DAKE----KALD-LLARLGLK 124
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDlRNLFSIVSQEPMLF-------NMSIYENIKFGKEDAtreDVKRackfAAIDeFIESLPNK 1347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 125 EHAQVYPY--SLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDR 202
Cdd:PTZ00265 1348 YDTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDK 1427
|
....*
gi 553319313 203 IIRVN 207
Cdd:PTZ00265 1428 IVVFN 1432
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-203 |
2.33e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.61 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGI----DHLENRnlLGFV 79
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFksskEALENG--ISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHLTVLDNLTLS--PT----ITMGKQKADAKekalDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGryPTkgmfVDQDKMYRDTK----AIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 154 IIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEI 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-203 |
3.65e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 73.23 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYnGEDVGI-------DHLENRN 74
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLayvdqsrDALDPNK 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 75 LlgfVFQDfqlfphltVLDNLTlspTITMGKQKADAKEkaldLLARLGLKEHAQVYPYS-LSGGQKQRVALARAMMIDPQ 153
Cdd:PRK11819 404 T---VWEE--------ISGGLD---IIKVGNREIPSRA----YVGRFNFKGGDQQKKVGvLSGGERNRLHLAKTLKQGGN 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 553319313 154 IIGYDEPTSALDPE-LRQTVEALIvqnrEMGITQIVVTHDLVFAeaisDRI 203
Cdd:PRK11819 466 VLLLDEPTNDLDVEtLRALEEALL----EFPGCAVVISHDRWFL----DRI 508
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-204 |
8.98e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 8.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIF----DGFNLTVQDGEVLSLVGPSGGGKT----TLLRML--AGLEsIDSGQVFY---NGEDVGI 67
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKiaavRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGL-VQCDKMLLrrrSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 68 DHLENRNL-------LGFVFQD--FQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKEHAQV---YPYSLS 135
Cdd:PRK10261 91 SEQSAAQMrhvrgadMAMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 136 GGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALI-VQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkVLQKEMSMGVIFITHDMGVVAEIADRVL 240
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-204 |
1.24e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.78 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL-ESIDSGQVFYNGEDVGIDHLEN--RNLLGFVFQDFQ---LFPHLTV 91
Cdd:TIGR02633 277 DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQaiRAGIAMVPEDRKrhgIVPILGV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNLTLSPT---ITMGKQKADAKEKALDL-LARLGLKEHAQVYPY-SLSGGQKQRVALARAMMIDPQIIGYDEPTSALDP 166
Cdd:TIGR02633 357 GKNITLSVLksfCFKMRIDAAAELQIIGSaIQRLKVKTASPFLPIgRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190
....*....|....*....|....*....|....*...
gi 553319313 167 ELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:TIGR02633 437 GAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVL 474
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-195 |
4.17e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVfyngeDVGIdHLEnrnllgfV--F 80
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----HCGT-KLE-------VayF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQ--LFPHLTVLDNLTLSP-TITMGKQKADAKEKALDLL-----ARLGLKehaqvypySLSGGQKQRVALARAMMIDP 152
Cdd:PRK11147 388 DQHRaeLDPEKTVMDNLAEGKqEVMVNGRPRHVLGYLQDFLfhpkrAMTPVK--------ALSGGERNRLLLARLFLKPS 459
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 153 QIIGYDEPTSALDPELRQTVEALIVQNREmgiTQIVVTHDLVF 195
Cdd:PRK11147 460 NLLILDEPTNDLDVETLELLEELLDSYQG---TVLLVSHDRQF 499
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-203 |
4.60e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 17 FDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVF--QDFQ---LFPHLTV 91
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYlpEDRQssgLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNLTLSPTITMGKQKADAKEKA-LDLLAR-LGLK-EHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPEL 168
Cdd:PRK15439 359 AWNVCALTHNRRGFWIKPARENAvLERYRRaLNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190
....*....|....*....|....*....|....*
gi 553319313 169 RQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRV 473
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
4-165 |
5.33e-14 |
|
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: 67.67 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFGQ----KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL----ESIdSGQVFYNGEDVGIDHLENRNL 75
Cdd:cd03233 6 WRNISFTTGKgrskIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSV-EGDIHYNGIPYKEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 LGFVFQDFQLFPHLTVldnltlsptitmgkqkadakEKALDLLARlgLKEHAQVypYSLSGGQKQRVALARAMMIDPQII 155
Cdd:cd03233 85 IIYVSEEDVHFPTLTV--------------------RETLDFALR--CKGNEFV--RGISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 553319313 156 GYDEPTSALD 165
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-204 |
5.54e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 5.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNIS---KQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGL-ESIDSGQVFYNGEDVGIDHLEN--RN 74
Cdd:PRK13549 259 ILEVRNLTawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQaiAQ 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 75 LLGFVFQD---FQLFPHLTVLDNLTLS--PTITMGKQKADAKEK--ALDLLARLGLK-EHAQVYPYSLSGGQKQRVALAR 146
Cdd:PRK13549 339 GIAMVPEDrkrDGIVPVMGVGKNITLAalDRFTGGSRIDDAAELktILESIQRLKVKtASPELAIARLSGGNQQKAVLAK 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 147 AMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVL 476
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
3-203 |
8.76e-14 |
|
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: 69.04 E-value: 8.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 EL-KNISKQFGQktifDGFNL----TVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVfynGEDVGIDHLENRnllg 77
Cdd:COG1245 74 ELeEDPVHRYGE----NGFRLyglpVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDY---DEEPSWDEVLKR---- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 78 fvFQDFQLFPHLTVLDNLTLS-----------PTITMGK-----QKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQR 141
Cdd:COG1245 143 --FRGTELQDYFKKLANGEIKvahkpqyvdliPKVFKGTvrellEKVDERGKLDELAEKLGLENILDRDISELSGGELQR 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 553319313 142 VALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:COG1245 221 VAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYV 282
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
20-193 |
1.05e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 20 FNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESiDSGQVFYNGEDVG-IDHLENRNLLGFVFQDFQLFPHLTVLDNLTLS 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEaWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 99 -PTitmgKQKADAKEKALDLLA-RLGL--KEHAQVypYSLSGGQKQRVALARAMM-IDPQIIGY------DEPTSALDPE 167
Cdd:PRK03695 94 qPD----KTRTEAVASALNEVAeALGLddKLGRSV--NQLSGGEWQRVRLAAVVLqVWPDINPAgqllllDEPMNSLDVA 167
|
170 180
....*....|....*....|....*.
gi 553319313 168 LRQTVEALIVQNREMGITQIVVTHDL 193
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-191 |
1.15e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 67.36 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLES--IDSGQVFYNGEDVGIDHLENRNLLGf 78
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAHLG- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQL---FPHLTVLDNLTL---SPTITMGKQKADA-------KEKaLDLlarLGLKEH--AQVYPYSLSGGQKQRVA 143
Cdd:CHL00131 86 IFLAFQYpieIPGVSNADFLRLaynSKRKFQGLPELDPlefleiiNEK-LKL---VGMDPSflSRNVNEGFSGGEKKRNE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 144 LARAMMIDPQIIGYDEPTSALDPELRQTVEALIvqNREMGITQ--IVVTH 191
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGI--NKLMTSENsiILITH 209
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-177 |
1.26e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 66.43 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDgFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYngEDVGIDHLEnRNLLGFVF 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIA-KPYCTYIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLFPHLTVLDNLTLSPTITMGKQKADAKEKALDLLARLGLKehaqvyPYSLSGGQKQRVALARAMMIDPQIIGYDEP 160
Cdd:PRK13541 77 HNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFKLHDLLDEK------CYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
|
170
....*....|....*..
gi 553319313 161 TSALDPELRQTVEALIV 177
Cdd:PRK13541 151 ETNLSKENRDLLNNLIV 167
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-193 |
1.78e-13 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 68.20 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 13 QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNG---EDVGIDHLENR----NLLGFVFQDfql 85
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDiplTKLQLDSWRSRlavvSQTPFLFSD--- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 86 fphlTVLDNLTLSptitmgkqKADAKEKALDLLARLglkehAQVYP--------YS---------LSGGQKQRVALARAM 148
Cdd:PRK10789 404 ----TVANNIALG--------RPDATQQEIEHVARL-----ASVHDdilrlpqgYDtevgergvmLSGGQKQRISIARAL 466
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 149 MIDPQIIGYDEPTSALDPelrQTvEALIVQN-REMGI--TQIVVTHDL 193
Cdd:PRK10789 467 LLNAEILILDDALSAVDG---RT-EHQILHNlRQWGEgrTVIISAHRL 510
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-195 |
2.83e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.65 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQF-GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIdsgqvfYNGEDV---GIDhlenrnlLGFV 79
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD------FNGEARpqpGIK-------VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHLTVLDNLTLS--------------------PTITMGK---------QKADAKeKALDLLARLGLKEHAQVY 130
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGvaeikdaldrfneisakyaePDADFDKlaaeqaelqEIIDAA-DAWDLDSQLEIAMDALRC 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 553319313 131 P------YSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPElrqTVEALIVQNREMGITQIVVTHDLVF 195
Cdd:TIGR03719 153 PpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYF 220
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-207 |
4.61e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 67.31 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 13 QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLR-MLAGLESIDSGQVFYNGEdvgidhlenrnlLGFVfqdfqlfPHLTV 91
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS------------VAYV-------PQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDNLTLSPTITMGKQ----------KADAKEKALDLLARLGLKEHAQvYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:PLN03232 690 IFNATVRENILFGSDfeserywraiDVTALQHDLDLLPGRDLTEIGE-RGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 553319313 162 SALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAIsDRIIRVN 207
Cdd:PLN03232 769 SALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVS 813
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
18-204 |
6.37e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 6.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDV-----------GIDHL-ENRNLLGFVFQdfql 85
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtrspqdglanGIVYIsEDRKRDGLVLG---- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 86 fphLTVLDNLTLSP----TITMGKQKADAKEKALDLLARL-GLKEHAQVYPYS-LSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:PRK10762 345 ---MSVKENMSLTAlryfSRAGGSLKHADEQQAVSDFIRLfNIKTPSMEQAIGlLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 553319313 160 PTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRIL 466
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
12-193 |
8.76e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.28 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVG-IDHLENRNLLGFVFQDFQLFPHlT 90
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSsLSHSVLRQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 91 VLDNLTLSPTITmgkqkadaKEKALDLLARLGLKEHAQVYP-----------YSLSGGQKQRVALARAMMIDPQIIGYDE 159
Cdd:PRK10790 431 FLANVTLGRDIS--------EEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDE 502
|
170 180 190
....*....|....*....|....*....|....
gi 553319313 160 PTSALDPELRQTVEALIVQNREMgITQIVVTHDL 193
Cdd:PRK10790 503 ATANIDSGTEQAIQQALAAVREH-TTLVVIAHRL 535
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-204 |
1.19e-12 |
|
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: 63.36 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 24 VQDGEVLSLVGPSGGGKTTLLRMLAGlesidsgQVFYNGEDVGIDHLenrnllgfvfqdfqlfphltvldnltlspTITM 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAG-------QLIPNGDNDEWDGI-----------------------------TPVY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 104 GKQKADakekaldllarlglkehaqvypysLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMG 183
Cdd:cd03222 66 KPQYID------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|..
gi 553319313 184 I-TQIVVTHDLVFAEAISDRII 204
Cdd:cd03222 122 KkTALVVEHDLAVLDYLSDRIH 143
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-191 |
1.40e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 65.81 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGlesiDSGQVFYN-----------GEDVgidhLE 71
Cdd:PRK10938 262 VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQGYSNdltlfgrrrgsGETI----WD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 72 NRNLLGFVFQDFqlfpHL-----TVLDNLTLS---PTITMGKQKADAKEK-ALDLLARLGLKEHAQVYPY-SLSGGQkQR 141
Cdd:PRK10938 334 IKKHIGYVSSSL----HLdyrvsTSVRNVILSgffDSIGIYQAVSDRQQKlAQQWLDILGIDKRTADAPFhSLSWGQ-QR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 142 VAL-ARAMMIDPQIIGYDEPTSALDPELRQTV----EALIVQnremGITQIV-VTH 191
Cdd:PRK10938 409 LALiVRALVKHPTLLILDEPLQGLDPLNRQLVrrfvDVLISE----GETQLLfVSH 460
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-203 |
1.41e-12 |
|
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: 65.81 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGFVFQDFQLFPHLTVLDNLTL 97
Cdd:TIGR01257 1956 DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYL 2035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 98 SPTITmGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIV 177
Cdd:TIGR01257 2036 YARLR-GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
170 180
....*....|....*....|....*.
gi 553319313 178 QNREMGITQIVVTHDLVFAEAISDRI 203
Cdd:TIGR01257 2115 SIIREGRAVVLTSHSMEECEALCTRL 2140
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
19-203 |
2.23e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.21 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 19 GFNL----TVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNG--EDVgIDHlenrnllgfvFQDFQLFPHLTVL 92
Cdd:PRK13409 87 GFKLyglpIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswDEV-LKR----------FRGTELQNYFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 93 DNLTLS-----------PTITMGK-----QKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:PRK13409 156 YNGEIKvvhkpqyvdliPKVFKGKvrellKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 553319313 157 YDEPTSALDPELRQTVEALIvqnREM--GITQIVVTHDLVFAEAISDRI 203
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLI---RELaeGKYVLVVEHDLAVLDYLADNV 281
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-176 |
2.53e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.88 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEdVGIDhlenrnllgfVFQDFqlfpHLTV 91
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK-VRMA----------VFSQH----HVDG 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 LDnLTLSPTITMGKQKADAKEKALDL-LARLGLKEHAQVYP-YSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPElr 169
Cdd:PLN03073 585 LD-LSSNPLLYMMRCFPGVPEQKLRAhLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD-- 661
|
....*..
gi 553319313 170 qTVEALI 176
Cdd:PLN03073 662 -AVEALI 667
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-204 |
4.27e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 20 FNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL------------ENRNLLGFVfqdfqlfP 87
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrdairagimlcpEDRKAEGII-------P 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 88 HLTVLDNLTLSP---TITMGKQKADAKEK--ALDLLARLGLKE-HAQVYPYSLSGGQKQRVALARAMMIDPQIIGYDEPT 161
Cdd:PRK11288 345 VHSVADNINISArrhHLRAGCLINNRWEAenADRFIRSLNIKTpSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 162 SALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRII 204
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIV 467
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
12-206 |
1.06e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.22 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLR-MLAGLESIDSGQVFYNGEdvgidhlenrnlLGFVFQDFQLFpHLT 90
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT------------VAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 91 VLDNltlsptITMGKQ-KADAKEKALDLLArlgLKEHAQVYP-----------YSLSGGQKQRVALARAMMIDPQIIGYD 158
Cdd:PLN03130 695 VRDN------ILFGSPfDPERYERAIDVTA---LQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFD 765
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 553319313 159 EPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAIsDRIIRV 206
Cdd:PLN03130 766 DPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILV 812
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-195 |
1.85e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.66 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 17 FDGFNLTVQDGEVLSLVGPSGGGKTTLLR-MLAGLESID-----SGQVFYNGEDVGI--DHLENRNLLGFVFQDFQlfpH 88
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKVEghvhmKGSVAYVPQQAWIqnDSLRENILFGKALNEKY---Y 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 89 LTVLDNLTLSPTITM--GKQKADAKEKALDLlarlglkehaqvypyslSGGQKQRVALARAMMIDPQIIGYDEPTSALDP 166
Cdd:TIGR00957 731 QQVLEACALLPDLEIlpSGDRTEIGEKGVNL-----------------SGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190
....*....|....*....|....*....|.
gi 553319313 167 ELRQTVEALIVQNREM--GITQIVVTHDLVF 195
Cdd:TIGR00957 794 HVGKHIFEHVIGPEGVlkNKTRILVTHGISY 824
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-207 |
2.22e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.06 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLlRMLAGLESIDSGQVFYNGEDVGIDHLENRNLLGF--- 78
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*hrp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 ----VFQDFQLFPHLTVLDN-LTLSptitmgkqKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQ 153
Cdd:NF000106 93 vr*gRRESFSGRENLYMIGR*LDLS--------RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 154 IIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAISDRIIRVN 207
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVID 218
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-195 |
5.47e-11 |
|
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: 59.65 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYN-----GEDVGIDHLENRNLLGFVFQDFQLFpHLTVLDNL 95
Cdd:cd03290 21 NIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknesEPSFEATRSRNRYSVAYAAQKPWLL-NATVEENI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 96 TL-SPtitMGKQKADAKEKALDLLARLGLKEHAQVYPY-----SLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELR 169
Cdd:cd03290 100 TFgSP---FNKQRYKAVTDACSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176
|
170 180
....*....|....*....|....*...
gi 553319313 170 QTV--EALIVQNREMGITQIVVTHDLVF 195
Cdd:cd03290 177 DHLmqEGILKFLQDDKRTLVLVTHKLQY 204
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-191 |
1.18e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLE--SIDSGQVFYNGED-------------- 64
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDllelspedragegi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 65 -------VGIDHLENRNLLGFVFQDFQLFPHLTVLDNLTLSPTItmgkqkaDAKEKALDLLARLgLKEHAQVypySLSGG 137
Cdd:PRK09580 81 fmafqypVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLM-------EEKIALLKMPEDL-LTRSVNV---GFSGG 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 553319313 138 QKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTH 191
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
12-191 |
1.19e-10 |
|
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: 60.15 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDgFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGqVFYNGEDVGIDHLENRnllgfvfqdfqlfPHLTv 91
Cdd:TIGR00954 464 GDVLIES-LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGG-RLTKPAKGKLFYVPQR-------------PYMT- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 92 ldNLTLSPTITMGKQKADAKEKAL---------------DLLARLGLKEHAQVYPYSLSGGQKQRVALARAMMIDPQIIG 156
Cdd:TIGR00954 528 --LGTLRDQIIYPDSSEDMKRRGLsdkdleqildnvqltHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 553319313 157 YDEPTSALDPElrqtVEALIVQN-REMGITQIVVTH 191
Cdd:TIGR00954 606 LDECTSAVSVD----VEGYMYRLcREFGITLFSVSH 637
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-203 |
2.46e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.30 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 14 KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAG--LESIDS------GQVFYNGEDVG-IDHLE---NRNLL----- 76
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPrgarvtGDVTLNGEPLAaIDAPRlarLRAVLpqaaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 -GFVFQDFQL-----FPHLTvldnltlsptiTMGKQKADAKEKALDLLARLGLKEHAQVYPYSLSGGQKQRVALARAM-- 148
Cdd:PRK13547 94 pAFAFSAREIvllgrYPHAR-----------RAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaq 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 553319313 149 -------MIDPQIIGYDEPTSALD----PELRQTVEALiVQNREMGITQIVvtHDLVFAEAISDRI 203
Cdd:PRK13547 163 lwpphdaAQPPRYLLLDEPTAALDlahqHRLLDTVRRL-ARDWNLGVLAIV--HDPNLAARHADRI 225
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-165 |
5.24e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAG-LESiDSGQVfyngedvgidHLENRNLLGFV 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGdLEP-SAGNV----------SLDPNERLGKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHLTVLDnltlspTITMG-------KQKAD------------------------------AKEKALDLLARLG 122
Cdd:PRK15064 70 RQDQFAFEEFTVLD------TVIMGhtelwevKQERDriyalpemseedgmkvadlevkfaemdgytAEARAGELLLGVG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 553319313 123 LKEHAQVYPYS-LSGGQKQRVALARAMMIDPQIIGYDEPTSALD 165
Cdd:PRK15064 144 IPEEQHYGLMSeVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-193 |
5.26e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 5.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKT---IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVF----YNGEDVGIDHLenRN 74
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIindsHNLKDINLKWW--RS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 75 LLGFVFQDFQLFPH-----------------------------------------------LTVLDNLTLSPTITMGKQK 107
Cdd:PTZ00265 461 KIGVVSQDPLLFSNsiknnikyslyslkdlealsnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 108 ---------ADAKEKAL--DLLARLGLKEHAQVYPYS--LSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEA 174
Cdd:PTZ00265 541 yqtikdsevVDVSKKVLihDFVSALPDKYETLVGSNAskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
250 260
....*....|....*....|.
gi 553319313 175 LI--VQNREMGITqIVVTHDL 193
Cdd:PTZ00265 621 TInnLKGNENRIT-IIIAHRL 640
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-192 |
1.10e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.10 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 1 MLELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVfynGEDVGIDhlenrnlLGFvF 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI---GLAKGIK-------LGY-F 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 QDFQLfphltvldnltlsptitmgkQKADAKEKALDLLARLGLKE-HAQVYPY----------------SLSGGQKQRVA 143
Cdd:PRK10636 381 AQHQL--------------------EFLRADESPLQHLARLAPQElEQKLRDYlggfgfqgdkvteetrRFSGGEKARLV 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 553319313 144 LARAMMIDPQIIGYDEPTSALDPELRQTV-EALIvqnrEMGITQIVVTHD 192
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQALtEALI----DFEGALVVVSHD 486
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-165 |
1.14e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 55.88 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQK--TIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLLGF 78
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDlRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDfqlfphltvldnltlsPTITMG--KQKADAKEKALD--LLARLGLKEHAQvypySLSGGQKQRVALARAMMIDPQI 154
Cdd:cd03369 87 IPQD----------------PTLFSGtiRSNLDPFDEYSDeeIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRV 146
|
170
....*....|.
gi 553319313 155 IGYDEPTSALD 165
Cdd:cd03369 147 LVLDEATASID 157
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-167 |
1.52e-09 |
|
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: 55.33 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLE--SIDSGQVFYNGEDVGIDHlenRNLLGFVFQDFQLFPHL 89
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKtaGVITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 90 TVLDNLTLSptitmgkqkadAKEKAldllarlglkehaqvypysLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPE 167
Cdd:cd03232 95 TVREALRFS-----------ALLRG-------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-166 |
2.71e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.29 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 3 ELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNL------- 75
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCpriaymp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 76 --LGfvfqdFQLFPHLTVLDNL----TLsptitMGKQKADAKEKALDLLARLGLkehaqvYPYS------LSGGQKQRVA 143
Cdd:NF033858 83 qgLG-----KNLYPTLSVFENLdffgRL-----FGQDAAERRRRIDELLRATGL------APFAdrpagkLSGGMKQKLG 146
|
170 180
....*....|....*....|...
gi 553319313 144 LARAMMIDPQIIGYDEPTSALDP 166
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDP 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-195 |
8.89e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 4 LKNISKQFG-QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIdsgqvfYNGEDV---GIDhlenrnlLGFV 79
Cdd:PRK11819 9 MNRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKE------FEGEARpapGIK-------VGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 80 FQDFQLFPHLTVLDNLT--LSPTI----------------------TMGKQ-----KADAK---------EKALDLLaRL 121
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEegVAEVKaaldrfneiyaayaepdadfdaLAAEQgelqeIIDAAdawdldsqlEIAMDAL-RC 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553319313 122 GLKEhAQVYPysLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPElrqTVEALIVQNREMGITQIVVTHDLVF 195
Cdd:PRK11819 155 PPWD-AKVTK--LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYF 222
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
133-206 |
2.14e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.22 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 133 SLSGGQKQ------RVALARAMMIDPQIIGYDEPTSALDPE-LRQTVEALIVQNREMGITQ-IVVTHDLVFAEAIsDRII 204
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQKNFQlIVITHDEELVDAA-DHIY 193
|
..
gi 553319313 205 RV 206
Cdd:cd03240 194 RV 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-206 |
9.85e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 27 GEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFY-NGEDVGIDHLENRNLLGFVFqdfqlfphltvldnltlsptitmgk 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGG------------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 106 qkadakekaldllarlglkehaqvYPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTV------EALIVQN 179
Cdd:smart00382 57 ------------------------KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelRLLLLLK 112
|
170 180 190
....*....|....*....|....*....|..
gi 553319313 180 REMGITQIVVTHDLVF-----AEAISDRIIRV 206
Cdd:smart00382 113 SEKNLTVILTTNDEKDlgpalLRRRFDRRIVL 144
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-193 |
1.41e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.13 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 16 IFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLEN-RNLLGFVFQDFQLFPHlTVLDN 94
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDlRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 95 LT-LSPTITMGKQKADAKEKALDLLARLGLKEHAQVYP--YSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQT 171
Cdd:PLN03232 1330 IDpFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEggENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180
....*....|....*....|....
gi 553319313 172 VEALIvqnRE--MGITQIVVTHDL 193
Cdd:PLN03232 1410 IQRTI---REefKSCTMLVIAHRL 1430
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-193 |
1.90e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVfyngedvgidhLENRNLlGFVFQDFQLFpHLTVLDNL----- 95
Cdd:PTZ00243 680 SVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------WAERSI-AYVPQQAWIM-NATVRGNIlffde 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 96 ----TLSPTITMGKQKADAKEKALDLLARLGLKEhaqvypYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQT 171
Cdd:PTZ00243 747 edaaRLADAVRVSQLEADLAQLGGGLETEIGEKG------VNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGER 820
|
170 180
....*....|....*....|..
gi 553319313 172 VEALIVQNREMGITQIVVTHDL 193
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQV 842
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
12-206 |
2.21e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.55 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 12 GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFY---------NGEDVGIDhlenRNLLGFVF-- 80
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFpgnwqlawvNQETPALP----QPALEYVIdg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 81 -QDF-QLFPHLTVLDNLTLSPTITMGKQKADA------KEKALDLLARLGLKEHAQVYPYS-LSGGQKQRVALARAMMID 151
Cdd:PRK10636 88 dREYrQLEAQLHDANERNDGHAIATIHGKLDAidawtiRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 152 PQIIGYDEPTSALDpelrqtVEALIVQNREMGI---TQIVVTHDLVFAEAISDRIIRV 206
Cdd:PRK10636 168 SDLLLLDEPTNHLD------LDAVIWLEKWLKSyqgTLILISHDRDFLDPIVDKIIHI 219
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-165 |
4.47e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 49.72 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 27 GEVLSLVGPSGGGKTTLLRMLA----GLESIDSGQVFYNGedVGIDHLENRnLLGFVFQDFQL---FPHLTVLDNLTLSP 99
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDG--ITPEEIKKH-YRGDVVYNAETdvhFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 100 ------TITMGKQKADAKEKALDLLAR-LGLK--EHAQV---YPYSLSGGQKQRVALARAMMIDPQIIGYDEPTSALD 165
Cdd:TIGR00956 164 rcktpqNRPDGVSREEYAKHIADVYMAtYGLShtRNTKVgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
18-165 |
8.17e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.95 E-value: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 18 DGFnltVQDGEVLSLVGPSGGGKTTLLRMLAGLES---IDSGQVFYNGEdvGIDHLENRNlLGFVFQ-DFQLfPHLTVLD 93
Cdd:TIGR00956 783 DGW---VKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGR--PLDSSFQRS-IGYVQQqDLHL-PTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 94 NLTLS-----PTITMGKQKADAKEKALDLlarLGLKEHAQ----VYPYSLSGGQKQRVALARAMMIDPQIIGY-DEPTSA 163
Cdd:TIGR00956 856 SLRFSaylrqPKSVSKSEKMEYVEEVIKL---LEMESYADavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLFlDEPTSG 932
|
..
gi 553319313 164 LD 165
Cdd:TIGR00956 933 LD 934
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-204 |
1.19e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQFGQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAgLESID----SGQVFY-NGEDVGID-------- 68
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA-MHAIDgipkNCQILHvEQEVVGDDttalqcvl 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 69 --HLENRNLL----GFVFQDFQL-FPHLTVLDNLTLSPTI---TMGKQKAD------------AKEKALDLLARLGLKEH 126
Cdd:PLN03073 257 ntDIERTQLLeeeaQLVAQQRELeFETETGKGKGANKDGVdkdAVSQRLEEiykrlelidaytAEARAASILAGLSFTPE 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 127 AQVYPY-SLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQNREmgiTQIVVTHDLVFAEAISDRII 204
Cdd:PLN03073 337 MQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK---TFIVVSHAREFLNTVVTDIL 412
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-178 |
1.30e-06 |
|
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: 48.37 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF--GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDsGQVFYNGEDVGIDHLEN-RNLLGF 78
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTwRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHltvldnlTLSPTITMGKQKADakEKALDLLARLGLKEHAQVYP-----------YSLSGGQKQRVALARA 147
Cdd:TIGR01271 1297 IPQKVFIFSG-------TFRKNLDPYEQWSD--EEIWKVAEEVGLKSVIEQFPdkldfvlvdggYVLSNGHKQLMCLARS 1367
|
170 180 190
....*....|....*....|....*....|.
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALIVQ 178
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ 1398
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
14-193 |
1.68e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 14 KTIF--DGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGE--DVGIDHLENRNLLGFVFQDFQLfphl 89
Cdd:PRK13546 35 KTFFalDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvsVIAISAGLSGQLTGIENIEFKM---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 90 tvldnltlsptITMGKQKADAKEKALDLL--ARLGLKEHAQVYPYslSGGQKQRVALARAMMIDPQIIGYDEPTSALDPE 167
Cdd:PRK13546 111 -----------LCMGFKRKEIKAMTPKIIefSELGEFIYQPVKKY--SSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
|
170 180
....*....|....*....|....*.
gi 553319313 168 LRQTVEALIVQNREMGITQIVVTHDL 193
Cdd:PRK13546 178 FAQKCLDKIYEFKEQNKTIFFVSHNL 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-176 |
2.19e-06 |
|
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: 47.63 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNG---EDVGIDHLenRNLLGFVFQDFQLFPHLTvldNLTL 97
Cdd:TIGR00957 1306 NVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniAKIGLHDL--RFKITIIPQDPVLFSGSL---RMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 98 SPtitMGKQKADAKEKALDLLArlgLKEHAQVYP-----------YSLSGGQKQRVALARAMMIDPQIIGYDEPTSALDP 166
Cdd:TIGR00957 1381 DP---FSQYSDEEVWWALELAH---LKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAAVDL 1454
|
170
....*....|
gi 553319313 167 ELRQTVEALI 176
Cdd:TIGR00957 1455 ETDNLIQSTI 1464
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
14-208 |
2.34e-06 |
|
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: 45.81 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 14 KTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSgQVFYNGEDVGIDHLENRNLLGFVFQDFQLfphltvld 93
Cdd:cd03227 8 PSYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQ-SATRRRSGVKAGCIVAAVSAELIFTRLQL-------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 94 nltlsptitmgkqkadakekaldllarlglkehaqvypyslSGGQKQRVALARAMMI-----DPQIIgYDEPTSALDPEL 168
Cdd:cd03227 79 -----------------------------------------SGGEKELSALALILALaslkpRPLYI-LDEIDRGLDPRD 116
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 553319313 169 RQTVEALIVQNREMGITQIVVTHDLVFAEaISDRIIRVNP 208
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITHLPELAE-LADKLIHIKK 155
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-165 |
2.40e-06 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 46.77 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEdvgidhlenrnlLGFVFQDFQLFPHlTVLDNLTLSPT 100
Cdd:cd03291 57 NLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------ISFSSQFSWIMPG-TIKENIIFGVS 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 553319313 101 ITMGKQKADAKEKALDL-LARLGLKEHAQVYP--YSLSGGQKQRVALARAMMIDPQIIGYDEPTSALD 165
Cdd:cd03291 124 YDEYRYKSVVKACQLEEdITKFPEKDNTVLGEggITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
133-209 |
3.77e-06 |
|
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: 45.39 E-value: 3.77e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 133 SLSGGQKQRVALARAMM--IDPQIIGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAiSDRIIRVNPK 209
Cdd:cd03238 87 TLSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-178 |
2.78e-05 |
|
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: 43.69 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNISKQF--GQKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSgqvfyngeDVGIDHLE-NRNLLGF 78
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG--------DIQIDGVSwNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 79 VFQDFQLFPHLTVLDNLTLSPTITMGKQKADakEKALDLLARLGLKEHAQVYP-----------YSLSGGQKQRVALARA 147
Cdd:cd03289 75 WRKAFGVIPQKVFIFSGTFRKNLDPYGKWSD--EEIWKVAEEVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMCLARS 152
|
170 180 190
....*....|....*....|....*....|.
gi 553319313 148 MMIDPQIIGYDEPTSALDPELRQTVEALIVQ 178
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
77-208 |
2.94e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDFQLFPhltvLDNL-----TLSPTITMGKQKADAKEKALDLLARLGLkehaqvyPY--------SLSGGQKQRVA 143
Cdd:PRK00635 418 GKTFAEFQQMS----LQELfiflsQLPSKSLSIEEVLQGLKSRLSILIDLGL-------PYltperalaTLSGGEQERTA 486
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 553319313 144 LARAMMIDPQIIGY--DEPTSALDPELRQTVEALIVQNREMGITQIVVTHDlvfAEAIS--DRIIRVNP 208
Cdd:PRK00635 487 LAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD---EQMISlaDRIIDIGP 552
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
133-209 |
3.97e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.02 E-value: 3.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 133 SLSGGQKQRVALARamMIDPQIIG----YDEPTSALDP----ELRQTVEALivqnREMGITQIVVTHDLvfaEAIS--DR 202
Cdd:cd03270 137 TLSGGEAQRIRLAT--QIGSGLTGvlyvLDEPSIGLHPrdndRLIETLKRL----RDLGNTVLVVEHDE---DTIRaaDH 207
|
....*..
gi 553319313 203 IIRVNPK 209
Cdd:cd03270 208 VIDIGPG 214
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-193 |
5.07e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 5.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 21 NLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHLENRNllgfvfqdfqlfPHLTVLDNLTLSpT 100
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLN------------GQLTGIENIELK-G 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 101 ITMGKQKADAKE---KALDlLARLGLKEHAQVYPYslSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIV 177
Cdd:PRK13545 111 LMMGLTKEKIKEiipEIIE-FADIGKFIYQPVKTY--SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170
....*....|....*.
gi 553319313 178 QNREMGITQIVVTHDL 193
Cdd:PRK13545 188 EFKEQGKTIFFISHSL 203
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-204 |
5.73e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 19 GFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGLESIDSGQVFYNGEDVGIDHL-ENRNLLGFVFQDFQLFPHlTVLDNltL 97
Cdd:PTZ00243 1328 GVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLrELRRQFSMIPQDPVLFDG-TVRQN--V 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 98 SPTItmgkqKADAKE--KALDLlarLGLKEH---------AQVYP----YSLsgGQKQRVALARAMMI-DPQIIGYDEPT 161
Cdd:PTZ00243 1405 DPFL-----EASSAEvwAALEL---VGLRERvasesegidSRVLEggsnYSV--GQRQLMCMARALLKkGSGFILMDEAT 1474
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 553319313 162 SALDPELRQTVEAlIVQNREMGITQIVVTHDLvFAEAISDRII 204
Cdd:PTZ00243 1475 ANIDPALDRQIQA-TVMSAFSAYTVITIAHRL-HTVAQYDKII 1515
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-165 |
6.55e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 13 QKTIFDGFNLTVQDGEVLSLVGPSGGGKTTLLRMLAGlES----IdSGQVFYNGEDV-------GIDH-----LENRNLL 76
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFG-RSygrnI-SGTVFKDGKEVdvstvsdAIDAglayvTEDRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 77 GFVFQDfqlfphlTVLDNLTLSptitmgkqkadakekALDLLARLG-LKEH-----AQVYPYS--------------LSG 136
Cdd:NF040905 350 GLNLID-------DIKRNITLA---------------NLGKVSRRGvIDENeeikvAEEYRKKmniktpsvfqkvgnLSG 407
|
170 180
....*....|....*....|....*....
gi 553319313 137 GQKQRVALARAMMIDPQIIGYDEPTSALD 165
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
133-204 |
3.19e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 3.19e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 553319313 133 SLSGGQKQRVALARAMMIDPQIIGYDEPTSALDPELRQTVEALIVQ--NREMGItqIVVTHDLVFAEAISDRII 204
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElaKKDKGI--IIISSEMPELLGITDRIL 462
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-209 |
3.78e-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: 40.77 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 133 SLSGGQKQRVALARamMIDPQIIG--Y--DEPTSALDPELRQTVEALIVQNREMGITQIVVTHDlvfAEAIS--DRIIRV 206
Cdd:TIGR00630 488 TLSGGEAQRIRLAT--QIGSGLTGvlYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD---EDTIRaaDYVIDI 562
|
...
gi 553319313 207 NPK 209
Cdd:TIGR00630 563 GPG 565
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
135-200 |
3.70e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 37.72 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 135 SGGQKQ------RVALARAMMIDPQIIGYDEPTSALDpelRQTVEAL------IVQNREMG--ITQIVVTHDLVFAEAIS 200
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLD---RENIESLahalveIIKSRSQQrnFQLLVITHDEDFVELLG 1277
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-193 |
5.67e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.53 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 2 LELKNIsKQFGQKTIFD-GFNLTVqdgevlsLVGPSGGGKTTLLR-MLAGL-------ESIDSGQVFYNGEDVGID---H 69
Cdd:COG0419 5 LRLENF-RSYRDTETIDfDDGLNL-------IVGPNGAGKSTILEaIRYALygkarsrSKLRSDLINVGSEEASVElefE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 70 LENRNLLGFVFQ-DFQLFPHLT------VLDNLTLSPTITMGKQKA----DAKEKALDLLARLGLKEHAQVYPYS----- 133
Cdd:COG0419 77 HGGKRYRIERRQgEFAEFLEAKpserkeALKRLLGLEIYEELKERLkeleEALESALEELAELQKLKQEILAQLSgldpi 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 553319313 134 --LSGGQKQRVALAR--AMMIDpqiigydepTSALDPE-LRQTVEALivqnREMGItqivVTHDL 193
Cdd:COG0419 157 etLSGGERLRLALADllSLILD---------FGSLDEErLERLLDAL----EELAI----ITHVI 204
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
134-206 |
6.65e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 36.97 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 134 LSGGQKQ------RVALARAMM--IDPQIIgyDEPTSALDPELRQT-VEalIVQNREMGITQ-IVVTHDLVFAEAiSDRI 203
Cdd:PRK03918 789 LSGGERIalglafRLALSLYLAgnIPLLIL--DEPTPFLDEERRRKlVD--IMERYLRKIPQvIIVSHDEELKDA-ADYV 863
|
...
gi 553319313 204 IRV 206
Cdd:PRK03918 864 IRV 866
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
133-209 |
7.65e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 36.09 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 553319313 133 SLSGGQKQRVALARAMMIDPQI----------IGYDEPTSALDPELRQTVEALIVQNREMGITQIVVTHDLVFAEAIsDR 202
Cdd:cd03279 123 TLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERI-PQ 201
|
....*..
gi 553319313 203 IIRVNPK 209
Cdd:cd03279 202 RLEVIKT 208
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
34-59 |
9.86e-03 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 35.55 E-value: 9.86e-03
10 20
....*....|....*....|....*....
gi 553319313 34 GPSGGGKTTLLRMLA---GLESIDSGQVF 59
Cdd:PRK04182 7 GPPGSGKTTVARLLAeklGLKHVSAGEIF 35
|
|
| |
