|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-205 |
7.81e-94 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 273.79 E-value: 7.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSK--QQEQVVG 78
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVV 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-205 |
1.09e-81 |
|
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: 242.05 E-value: 1.09e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQE--QVVGV 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 160 EPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-208 |
4.42e-77 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 231.44 E-value: 4.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFD----PTSSKQQE--Q 75
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkPSEKAIRLlrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 VVGVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYME 215
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-205 |
7.96e-75 |
|
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: 224.71 E-value: 7.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVF 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR--DVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510806666 162 TSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03259 158 LSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIA 202
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-204 |
9.33e-75 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 229.21 E-value: 9.33e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEqvVGVV 80
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRN--VGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIGPRlVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLR-MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510806666 161 PTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG3842 162 PLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRI 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-208 |
2.38e-73 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 221.46 E-value: 2.38e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV 76
Cdd:COG1136 4 LLELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ----VGVVFQDFQLFPHLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:COG1136 84 rrrhIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAeEIGDKVLKVE 208
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHDPELA-ARADRVIRLR 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-208 |
4.83e-73 |
|
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: 218.98 E-value: 4.83e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTS--SKQQEQVVGV 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGprlvlkqdketytskanhlaklldieellnnfpyqLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 160 EPTSALDPALRQQVASLILELKA-DGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLR 175
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-205 |
2.23e-72 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 219.96 E-value: 2.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKqqeqv 76
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFPHLSVMDNITIGPRLVlKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVL 156
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELR-GVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 157 AYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVV 210
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-208 |
2.66e-71 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 216.80 E-value: 2.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFD---PTSSKQQEQV-- 76
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDfskTPSDKAIRELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 -VGVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:PRK11124 83 nVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYME 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-208 |
3.98e-71 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 216.11 E-value: 3.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG-SPFDPTSSKQQ-EQVVG 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLiRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFID 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-205 |
4.42e-71 |
|
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: 215.41 E-value: 4.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSK----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKqqeqvV 77
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYtSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEAR-ERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510806666 158 YDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVV 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-204 |
4.44e-71 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 219.94 E-value: 4.44e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEqvVGVV 80
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN--IAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKL-RKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510806666 161 PTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRI 204
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-210 |
1.17e-69 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 216.17 E-value: 1.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDpTSSKQQEQVVGVVF 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF-TNLPPRERRVGFVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRlVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:COG1118 82 QHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 162 TSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL-----KVEPI 210
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVvmnqgRIEQV 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-205 |
3.51e-68 |
|
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: 208.11 E-value: 3.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV- 76
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ---VGVVFQDFQLFPHLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:cd03255 81 rrhIGFVFQSFNLLPDLTALENVEL-PLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAeEIGDKVL 205
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELA-EYADRII 211
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-204 |
5.57e-68 |
|
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: 208.29 E-value: 5.57e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV---V 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrrI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 158 YDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRV 212
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-205 |
2.57e-67 |
|
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: 206.03 E-value: 2.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQ--DFQLFpHLSVMDNITIGPRlVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:COG1122 81 FQnpDDQLF-APTVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVI 205
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-205 |
5.87e-67 |
|
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: 205.43 E-value: 5.87e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV---VG 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrrMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 159 DEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03261 161 DEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIA 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-204 |
1.03e-66 |
|
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: 204.03 E-value: 1.03e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVF 81
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:cd03301 79 QNYALYPHMTVYDNIAFGLKL-RKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510806666 162 TSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRI 201
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
3-205 |
2.41e-66 |
|
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: 203.08 E-value: 2.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGS--KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:cd03225 1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDF--QLFpHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:cd03225 81 FQNPddQFF-GPTVEEEVAFGLEN-LGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVI 205
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-205 |
2.59e-64 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 198.75 E-value: 2.59e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTS-SKQQEQVVGVV 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG--EDVARdPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARL-YGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510806666 161 PTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-205 |
2.26e-63 |
|
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: 196.41 E-value: 2.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVF 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRL---VLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLRVkprSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 159 DEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVV 208
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-205 |
2.81e-62 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 194.25 E-value: 2.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFD----------PTSS 70
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvPADR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 71 KQQEQV---VGVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIAR 147
Cdd:COG4598 88 RQLQRIrtrLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVV 225
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-208 |
4.22e-62 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 192.57 E-value: 4.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQE----- 74
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG--QDLSRLKRREipylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 QVVGVVFQDFQLFPHLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPK 154
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510806666 155 VLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELE 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-205 |
5.10e-62 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 200.90 E-value: 5.10e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSK-----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQ 75
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 V---VGVVFQD--FQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKL--LDiEELLNNFPYQLSGGQKQRLAIARA 148
Cdd:COG1123 340 LrrrVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERvgLP-PDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVA 476
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-204 |
3.09e-61 |
|
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: 190.91 E-value: 3.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEqvVGVVF 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP--VNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 162 TSALDPALRQQvasLILELKA----DGVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03300 158 LGALDLKLRKD---MQLELKRlqkeLGITFVFVTHDQEEALTMSDRI 201
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-205 |
5.12e-61 |
|
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: 190.10 E-value: 5.12e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSK----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG---SPFDPTSSKQQ 73
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdlTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 74 EQVVGVVFQDFQLFPHLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVA 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-204 |
3.22e-60 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.44 E-value: 3.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG---SPFDPTSSKQQ 73
Cdd:COG1135 1 MIELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdlTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 74 EQVVGVVFQDFQLFPHLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRV 211
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-205 |
4.20e-60 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 188.42 E-value: 4.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTS--SKQQEQV-- 76
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslSQQKGLIrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ----VGVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:PRK11264 83 lrqhVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-205 |
1.69e-59 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 186.17 E-value: 1.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF----GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQE-- 74
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 -QVVGVVFQDFQ--LFPHLSVMDNITIGPRLVLKQDKETYTSKA--NHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAM 149
Cdd:cd03257 81 rKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVA 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-205 |
2.85e-59 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 190.16 E-value: 2.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVF 81
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ--DITHVPAENRHVNTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRL--VLKQDKETYTSKANHLAKLldiEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:PRK09452 93 QSYALFPHMTVFENVAFGLRMqkTPAAEITPRVMEALRMVQL---EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 160 EPTSALDPALRQQVAsliLELKA----DGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK09452 170 ESLSALDYKLRKQMQ---NELKAlqrkLGITFVFVTHDQEEALTMSDRIV 216
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-205 |
4.84e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 185.65 E-value: 4.84e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV--- 76
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFPHLSVMDNITIG-------PRLVL----KQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAI 145
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNVLAGrlgrtstWRSLLglfpPEDRE----RALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRII 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-204 |
5.01e-58 |
|
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: 182.38 E-value: 5.01e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL-----ETADSGTFLLDGSP-----FDPTSSK 71
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDiydldVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 72 QQeqvVGVVFQDFQLFPhLSVMDNITIGPRLVLKQDKETYTSKANHLAKL--LDIEELLNNFPYQLSGGQKQRLAIARAM 149
Cdd:cd03260 81 RR---VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKaaLWDEVKDRLHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRT 210
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-205 |
1.03e-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: 182.31 E-value: 1.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSK----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV 76
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDfqlfPHLSVMDNITIGPRL--VLKQDKETYTSKAnhLAKLLDI----EELLNNFPYQLSGGQKQRLAIARAMA 150
Cdd:COG1124 81 VQMVFQD----PYASLHPRHTVDRILaePLRIHGLPDREER--IAELLEQvglpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 151 MNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVA 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-205 |
1.63e-57 |
|
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: 179.13 E-value: 1.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQvVGVVF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNItigprlvlkqdketytskanhlaklldieellnnfpyQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:cd03230 80 EEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510806666 162 TSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVA 166
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-205 |
3.98e-57 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 184.15 E-value: 3.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVF 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHRSIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510806666 162 TSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVI 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-208 |
7.63e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 179.57 E-value: 7.63e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVinNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEqvVGVV 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP--VSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIG--PRLVL-KQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:COG3840 77 FQENNLFPHLTVAQNIGLGlrPGLKLtAEQRA----QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 158 YDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVA 204
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-204 |
1.56e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 182.59 E-value: 1.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVF 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT--DVSRLHARDRKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDI---EELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:PRK10851 81 QHYALFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMvqlAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 159 DEPTSALDPA----LRQQVASLILELKadgVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK10851 161 DEPFGALDAQvrkeLRRWLRQLHEELK---FTSVFVTHDQEEAMEVADRV 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-204 |
1.16e-55 |
|
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: 177.11 E-value: 1.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP---FDPTSSKQQeqvV 77
Cdd:cd03295 1 IEFENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDireQDPVELRRK---I 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKL--LDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALvgLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRI 206
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-209 |
1.42e-55 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 175.39 E-value: 1.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP---FDPTSSKQQeqvVG 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsaMPPPEWRRQ---VA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHlSVMDNITIGPRLVLKQDKEtytSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:COG4619 78 YVPQEPALWGG-TVRDNLPFPFQLRERKFDR---ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 158 YDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVLKVEP 209
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEA 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-205 |
2.44e-55 |
|
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: 176.22 E-value: 2.44e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGS-KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPF---DPTSSKQQEQVV 77
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMDNITIG-----------PRLVLKQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIA 146
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrstwrslFGLFPKEEKQ----RALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 147 RAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIV 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-208 |
4.97e-54 |
|
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: 171.66 E-value: 4.97e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV--- 76
Cdd:TIGR02673 1 MIEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFPHLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVL 156
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 157 AYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILD 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-205 |
8.71e-54 |
|
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: 171.96 E-value: 8.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQ-EQVVGV 79
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDG--EDVRKEPREaRRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAEL-YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 160 EPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVV 203
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-198 |
3.40e-53 |
|
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: 170.31 E-value: 3.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV 76
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ----VGVVFQDFQLFPHLSVMDNITIgPrLVLKQDKETYTSKANHLAKlLDIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:COG4181 88 rarhVGFVFQSFQLLPTLTALENVML-P-LELAGRRDARARARALLER-VGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAE 198
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAA 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-205 |
5.33e-53 |
|
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: 170.61 E-value: 5.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIG--PRLVL-----KQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGryPHLGLfgrpsAEDRE----AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLV 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
19-208 |
9.44e-53 |
|
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: 168.63 E-value: 9.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 19 NLDLVIPdGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSK----QQEQVVGVVFQDFQLFPHLSVMD 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlpPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 95 NITIG-PRLVLKQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQV 173
Cdd:cd03297 95 NLAFGlKRKRNREDRI----SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 510806666 174 ASLILELKAD-GVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:cd03297 171 LPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVME 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-207 |
1.85e-52 |
|
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: 167.41 E-value: 1.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQ----VVGV 79
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKfrreKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLlDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKV-GLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 160 EPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAeEIGDKVLKV 207
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-205 |
2.20e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.03 E-value: 2.20e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFdptssKQQEQVVGVV 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQL---FPhLSVMDNITIG-------PRLVLKQDKEtytsKANHLAKLLDIEELLNNfPY-QLSGGQKQRLAIARAM 149
Cdd:COG1121 81 PQRAEVdwdFP-ITVRDVVLMGrygrrglFRRPSRADRE----AVDEALERVGLEDLADR-PIgELSGGQQQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVL 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-204 |
2.72e-51 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 165.59 E-value: 2.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKViNNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVF 81
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGK--DITNLPPEKRDISYVP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLVlKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:cd03299 78 QNYALFPHMTVYKNIAYGLKKR-KVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510806666 162 TSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03299 157 FSALDVRTKEKLREELKKIrKEFGVTVLHVTHDFEEAWALADKV 200
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-208 |
5.14e-51 |
|
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: 162.03 E-value: 5.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQ 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 dfqlfphlsvmdnitigprlvlkqdketytskanhlaklldieellnnfpyqLSGGQKQRLAIARAMAMNPKVLAYDEPT 162
Cdd:cd00267 81 ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 163 SALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLK 154
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-205 |
1.89e-50 |
|
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: 163.38 E-value: 1.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspfDPTSSKQQEQVV--GV 79
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG---EDITGLPPHEIArlGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 V--FQDFQLFPHLSVMDNITIGPRLVLK---------QDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARA 148
Cdd:cd03219 78 GrtFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-205 |
2.72e-50 |
|
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: 170.08 E-value: 2.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL---ETADSGTFLLDGSPFDPTSSKQQEQ 75
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 VVGVVFQDF--QLFPhLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:COG1123 84 RIGMVFQDPmtQLNP-VTVGDQIAEALEN-LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVV 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-205 |
6.36e-50 |
|
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: 160.89 E-value: 6.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFG-SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspfDPTSSKQQEQVVGVVF 81
Cdd:cd03226 1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QD--FQLFPHlSVMDNITIGprlvlKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:cd03226 78 QDvdYQLFTD-SVREELLLG-----LKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 160 EPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVL 197
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-204 |
7.45e-50 |
|
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: 161.45 E-value: 7.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQV---VG 78
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR--DITGLPPHERAragIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHLSVMDNITIGPRLVLKQDKETytskanhlakllDIEELLNNFP----------YQLSGGQKQRLAIARA 148
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARRRAKRKA------------RLERVYELFPrlkerrkqlaGTLSGGEQQMLAIARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRA 202
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
4-204 |
7.86e-50 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 165.59 E-value: 7.86e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEqvVGVVFQD 83
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 84 FQLFPHLSVMDNITIGPRLVlKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKLA-GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 164 ALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK11000 163 NLDAALRVQMRIEISRLhKRLGRTMIYVTHDQVEAMTLADKI 204
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-205 |
1.19e-49 |
|
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: 160.39 E-value: 1.19e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKqqeqvVGVVFQ 82
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 DFQL---FPhLSVMDNITIG--PRLVL-----KQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:cd03235 76 RRSIdrdFP-ISVRDVVLMGlyGHKGLfrrlsKADKA----KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-205 |
1.26e-49 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 161.74 E-value: 1.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspfDPTSSKQQEQVV--G 78
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---RDITGLPPHRIArlG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VV--FQDFQLFPHLSVMDNITIG---------------PRLVLKQDKETyTSKANHLAKLLDIEELLNNFPYQLSGGQKQ 141
Cdd:COG0411 81 IArtFQNPRLFPELTVLENVLVAaharlgrgllaallrLPRARREEREA-RERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 142 RLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIV 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-194 |
4.55e-49 |
|
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: 169.63 E-value: 4.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSFG----SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP---FDPTSSKQQe 74
Cdd:COG2274 474 IELENV--SFRypgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDlrqIDPASLRRQ- 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 qvVGVVFQDFQLFpHLSVMDNITIGprlvlkqDKETYTSKANHLAKLLDIEELLNNFP--YQ---------LSGGQKQRL 143
Cdd:COG2274 551 --IGVVLQDVFLF-SGTIRENITLG-------DPDATDEEIIEAARLAGLHDFIEALPmgYDtvvgeggsnLSGGQRQRL 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 144 AIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAdGVTQIVVTHDL 194
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL 670
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-204 |
6.62e-49 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 165.96 E-value: 6.62e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ-QEQVVGV 79
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGpRLVLK----QDKETYTSKANHLAKL---LDIEELLNNfpyqLSGGQKQRLAIARAMAMN 152
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLG-REPRRggliDWRAMRRRARELLARLgldIDPDTPVGD----LSVAQQQLVEIARALSRD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRV 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-205 |
1.07e-48 |
|
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: 159.00 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGS-KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV--- 76
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFPHLSVMDNITIGpRLVLK------------QDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLA 144
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVLHG-RLGYKptwrsllgrfseEDKE----RALSALERVGLADKAYQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806666 145 IARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLHQVDLAKKYADRIV 217
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-204 |
2.01e-48 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 158.66 E-value: 2.01e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTL-------AGLETadSGTFLLDG----SP-FDPTS 69
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGARV--EGEILLDGediyDPdVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 70 SKQQeqvVGVVFQDFQLFPHlSVMDNITIGPRLVLKQDK-------ETYTSKANhlakLLDieEL---LNNFPYQLSGGQ 139
Cdd:COG1117 90 LRRR---VGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKseldeivEESLRKAA----LWD--EVkdrLKKSALGLSGGQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 140 KQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG1117 160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYT 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-197 |
3.03e-48 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 158.49 E-value: 3.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQqeqv 76
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 vGVVFQDFQLFPHLSVMDNITIGPRLVlKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVL 156
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLR-GVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 157 AYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFA 197
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEA 198
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-163 |
3.06e-48 |
|
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: 154.73 E-value: 3.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFPHLSVMDNI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806666 97 TIGPRLvLKQDKETYTSKANHLAKLLDIEELLN----NFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:pfam00005 81 RLGLLL-KGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-205 |
7.13e-48 |
|
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: 160.27 E-value: 7.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELkNVNKSFGSKKVinNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP-FDptsSKQQEQV--- 76
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQD---SARGIFLpph 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ---VGVVFQDFQLFPHLSVMDNITIGPRLVLKQDKetyTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:COG4148 76 rrrIGYVFQEARLFPHLSVRGNLLYGRKRAPRAER---RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKADGVTQIV-VTHDLDFAEEIGDKVL 205
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIPILyVSHSLDEVARLADHVV 205
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-208 |
1.87e-47 |
|
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: 153.69 E-value: 1.87e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGS--KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP---FDPTSSKQQeqv 76
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDlrdLDLESLRKN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFpHLSVMDNItigprlvlkqdketytskanhlaklldieellnnfpyqLSGGQKQRLAIARAMAMNPKVL 156
Cdd:cd03228 78 IAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 157 AYDEPTSALDPALRQQVASLILELkADGVTQIVVTHDLDfAEEIGDKVLKVE 208
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLS-TIRDADRIIVLD 168
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-208 |
2.05e-47 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 154.96 E-value: 2.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVinNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQEQVVGVVF 81
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING--VDVTAAPPADRPVSMLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIG--PRLVLKQDKETYTSKAnhlAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:cd03298 77 QENNLFAHLTVEQNVGLGlsPGLKLTAEDRQAIEVA---LARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 160 EPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLD 203
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-204 |
2.23e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 158.43 E-value: 2.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF--GSKKVI--NNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQE-- 74
Cdd:PRK11153 1 MIELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQ--DLTALSEKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 ---QVVGVVFQDFQLFPHLSVMDNITIGPRLVlKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAM 151
Cdd:PRK11153 79 karRQIGMIFQHFNLLSSRTVFDNVALPLELA-GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 152 NPKVLAYDEPTSALDPALRQQvaslILELKAD-----GVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRS----ILELLKDinrelGLTIVLITHEMDVVKRICDRV 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-205 |
3.52e-47 |
|
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: 157.52 E-value: 3.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSK----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLE---TADSGTFLLDGSPFDPTSSKQQ 73
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 74 EQV----VGVVFQDFQ--LFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDI---EELLNNFPYQLSGGQKQRLA 144
Cdd:COG0444 81 RKIrgreIQMIFQDPMtsLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806666 145 IARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVA 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-208 |
4.10e-47 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 155.61 E-value: 4.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTfLLDGSPfdPTSSKQQEqvVGVVFQD 83
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTA--PLAEARED--TRLMFQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 84 FQLFPHLSVMDNITIGprlvLKQDketYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:PRK11247 90 ARLLPWKKVIDNVGLG----LKGQ---WRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 164 ALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK11247 163 ALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIE 208
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-193 |
1.69e-46 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 156.54 E-value: 1.69e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSK-KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspfdptsskqqeQVVG- 78
Cdd:PRK11650 3 GLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG------------RVVNe 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 ---------VVFQDFQLFPHLSVMDNITIGPRlVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAM 149
Cdd:PRK11650 71 lepadrdiaMVFQNYALYPHMSVRENMAYGLK-IRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHD 193
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHD 194
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-205 |
6.86e-46 |
|
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: 149.89 E-value: 6.86e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQ 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 dfqlfphlsVMDnitigprlvlkqdketytskanhlakLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPT 162
Cdd:cd03214 81 ---------ALE--------------------------LLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510806666 163 SALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03214 126 SHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVI 169
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-193 |
9.13e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 155.38 E-value: 9.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVV 80
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLSHVPPYQRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIGprlvLKQDK---ETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFG----LKQDKlpkAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 510806666 158 YDEPTSALDPALRQQVASLILE-LKADGVTQIVVTHD 193
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDiLERVGVTCVMVTHD 209
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
1-206 |
1.01e-45 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 150.64 E-value: 1.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSK----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQ--- 73
Cdd:NF038007 1 MLNMQNAEKCYITKtiktKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQKiil 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 74 -EQVVGVVFQDFQLFPHLSVMDNITIgP---RLVLKQDKetyTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAM 149
Cdd:NF038007 81 rRELIGYIFQSFNLIPHLSIFDNVAL-PlkyRGVAKKER---IERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAM 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDlDFAEEIGDKVLK 206
Cdd:NF038007 157 VSNPALLLADEPTGNLDSKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIIN 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-209 |
1.21e-45 |
|
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: 149.94 E-value: 1.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVvGVV 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRL-AYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNItigpRLVLKQDKETYT-SKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:COG4133 81 GHADGLKPELTVRENL----RFWAALYGLRADrEAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 160 EPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEeiGDKVLKVEP 209
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELA--AARVLDLGD 204
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
9-204 |
3.11e-45 |
|
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: 150.87 E-value: 3.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 9 KSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV----VGVVFQDF 84
Cdd:cd03294 32 KKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 85 QLFPHLSVMDNITIGprLVLK-QDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:cd03294 112 ALLPHRTVLENVAFG--LEVQgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 164 ALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRI 231
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-204 |
1.25e-44 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 151.11 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 32 IVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVFQDFQLFPHLSVMDNITIGPRLvLKQDKETY 111
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE--DVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKM-RKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 112 TSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVAsliLELKAD----GVTQ 187
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQ---LELKTIqeqlGITF 154
|
170
....*....|....*..
gi 510806666 188 IVVTHDLDFAEEIGDKV 204
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRI 171
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-205 |
2.02e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 149.14 E-value: 2.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFG-----SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQE-- 74
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDG--RDITAKKKKKlk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 ---QVVGVVFQ--DFQLFpHLSVMDNITIGPRlVLKQDKETYTSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLAIARA 148
Cdd:TIGR04521 79 dlrKKVGLVFQfpEHQLF-EETVYKDIAFGPK-NLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:TIGR04521 157 LAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVI 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-202 |
5.98e-44 |
|
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: 146.67 E-value: 5.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSkqqEQVV--G 78
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP---HRIArlG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVF--QDFQLFPHLSVMDNITIGPRLVLKQDKetytSKAnhlakllDIEELLNNFPY----------QLSGGQKQRLAIA 146
Cdd:COG0410 80 IGYvpEGRRIFPSLTVEENLLLGAYARRDRAE----VRA-------DLERVYELFPRlkerrrqragTLSGGEQQMLAIG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 147 RAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGD 202
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIAD 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-197 |
8.85e-44 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 146.77 E-value: 8.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQqeqvvGVV 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIGPRLVlKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLA-GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 510806666 161 PTSALDPALRQQVASLILELKADGVTQI-VVTHDLDFA 197
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVlLITHDIEEA 192
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-205 |
1.09e-43 |
|
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: 146.81 E-value: 1.09e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG-SPFDPTSSKQQEQVVG 78
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQ--DFQlFPHLSVMDNITIGPR-LVLKQDKetYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:TIGR04520 81 MVFQnpDNQ-FVGATVEDDVAFGLEnLGVPREE--MRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEiGDKVL 205
Cdd:TIGR04520 158 IILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVI 207
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-200 |
1.38e-43 |
|
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: 145.16 E-value: 1.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGS----KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV- 76
Cdd:TIGR02982 2 ISIRNLNHYYGHgslrKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 --VGVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPK 154
Cdd:TIGR02982 82 rrIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 155 VLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHD---LDFAEEI 200
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEqGCTILMVTHDnriLDVADRI 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-204 |
1.94e-43 |
|
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: 144.96 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGS--KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGsPFDPTSSKQQEQVVGV 79
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-YSIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGPRL---VLKQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVL 156
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLkglPKSEIKE----EVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 157 AYDEPTSALDPALRQQVASLILELKAdGVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRK-GRSIILTTHSMDEAEALCDRI 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-192 |
4.73e-43 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.86 E-value: 4.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSF---GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP---FDPTSSKQQeq 75
Cdd:COG1132 340 IEFENV--SFsypGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDirdLTLESLRRQ-- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 vVGVVFQDFQLFpHLSVMDNITIGprlvlkqdKETYTS----KAnhlAKLLDIEELLNNFP--YQ---------LSGGQK 140
Cdd:COG1132 416 -IGVVPQDTFLF-SGTIRENIRYG--------RPDATDeeveEA---AKAAQAHEFIEALPdgYDtvvgergvnLSGGQR 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 141 QRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAdGVTQIVVTH 192
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-208 |
1.90e-42 |
|
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: 142.16 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSK-KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQ---EQVV 77
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMDNITIGPRLVLKQDKEtYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPRE-IRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 158 YDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALE 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-204 |
1.90e-42 |
|
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: 140.64 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ-QEQVVGVV 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 fqdfqlfphlsvmdnitigprlvlkqdketytskanhlaklldieellnnfpYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:cd03216 81 ----------------------------------------------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510806666 161 PTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRV 152
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-207 |
2.43e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 142.41 E-value: 2.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 21 DLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVFQDFQLFPHLSVMDNITIG- 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 100 -PRLVLKQDKEtytSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLIL 178
Cdd:PRK10771 97 nPGLKLNAAQR---EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVS 173
|
170 180 190
....*....|....*....|....*....|
gi 510806666 179 ELKAD-GVTQIVVTHDLDFAEEIGDKVLKV 207
Cdd:PRK10771 174 QVCQErQLTLLMVSHSLEDAARIAPRSLVV 203
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-205 |
2.28e-41 |
|
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: 139.25 E-value: 2.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGqILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQ-EQVVGVV 80
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ--DVLKQPQKlRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSV---MDNITIGPRLVLKQDKETytskANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:cd03264 78 PQEFGVYPNFTVrefLDYIAWLKGIPSKEVKAR----VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 158 YDEPTSALDPALRQQVASLILELKADGVTqIVVTHDLDFAEEIGDKVL 205
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIV-ILSTHIVEDVESLCNQVA 200
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-208 |
4.94e-41 |
|
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: 137.35 E-value: 4.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSF----GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVV 77
Cdd:cd03246 1 LEVENV--SFrypgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHlSVMDNItigprlvlkqdketytskanhlaklldieellnnfpyqLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:cd03246 79 GYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 158 YDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIgDKVLKVE 208
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASA-DRILVLE 169
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
12-197 |
6.03e-41 |
|
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: 137.55 E-value: 6.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQE--QVVGVVFQ--DFQLF 87
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLErrQRVGLVFQdpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 88 pHLSVMDNITIGPR-LVLKQDKetYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALD 166
Cdd:TIGR01166 83 -AADVDQDVAFGPLnLGLSEAE--VERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 510806666 167 PALRQQVASLILELKADGVTQIVVTHDLDFA 197
Cdd:TIGR01166 160 PAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-201 |
1.80e-40 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 136.84 E-value: 1.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETAD---SGTFLLDGSPFD--PTSSKQqeq 75
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTalPAEQRR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 vVGVVFQDFQLFPHLSVMDNITIG-PRLVLKQDKETYTSKAnhLAKLlDIEELLNNFPYQLSGGQKQRLAIARAMAMNPK 154
Cdd:COG4136 78 -IGILFQDDLLFPHLSVGENLAFAlPPTIGRAQRRARVEQA--LEEA-GLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 155 VLAYDEPTSALDPALRQQVASLILE-LKADGVTQIVVTHDLDFAEEIG 201
Cdd:COG4136 154 ALLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEEDAPAAG 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-205 |
2.64e-40 |
|
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: 144.13 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFpHLSVMDNITIGprlvlkqdKETYTSKA-NHLAKLLDIEELLNNFP-----------YQLSGGQKQRLAIARA 148
Cdd:COG4988 417 PQNPYLF-AGTIRENLRLG--------RPDASDEElEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELkADGVTQIVVTHDLDFAEEIgDKVL 205
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQA-DRIL 542
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-204 |
3.75e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 137.67 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL-----ETADSGTFLLDG----SP-FDPTSSK 71
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGrniySPdVDPIEVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 72 QQeqvVGVVFQDFQLFPHLSVMDNITIGPRL--VLKQDKE--TYTSKANHLAKLLD-IEELLNNFPYQLSGGQKQRLAIA 146
Cdd:PRK14267 85 RE---VGMVFQYPNPFPHLTIYDNVAIGVKLngLVKSKKEldERVEWALKKAALWDeVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 147 RAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYV 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-205 |
4.42e-40 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 138.32 E-value: 4.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ-----QEQ 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRigylpEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 vvGvvfqdfqLFPHLSVMDNITigpRLV-LKQ-DKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:COG4152 81 --G-------LYPKMKVGEQLV---YLArLKGlSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIV 200
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-208 |
9.16e-40 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 142.98 E-value: 9.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSFG----SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVV 77
Cdd:COG4987 334 LELEDV--SFRypgaGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFpHLSVMDNITIG-PRLvlkQDKEtytskanhLAKLLD---IEELLNNFPY-----------QLSGGQKQR 142
Cdd:COG4987 412 AVVPQRPHLF-DTTLRENLRLArPDA---TDEE--------LWAALErvgLGDWLAALPDgldtwlgeggrRLSGGERRR 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 143 LAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELkADGVTQIVVTHDLDfAEEIGDKVLKVE 208
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRLA-GLERMDRILVLE 543
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-209 |
1.23e-39 |
|
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: 135.25 E-value: 1.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-----GSKK--VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLL--DGSPFDPTSSK 71
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 72 QQE------QVVGVVFQDFQLFPHLSVMDnITIGPRLVLKQDKETYTSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLA 144
Cdd:COG4778 84 PREilalrrRTIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 145 IARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVEP 209
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTP 227
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
3-208 |
3.89e-39 |
|
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: 134.19 E-value: 3.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFdpTSSKQQEQV---VGV 79
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI--TKLPPHERAragIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGPRLVLKQDKETytskanhlaklldIEELLNNFPY----------QLSGGQKQRLAIARAM 149
Cdd:TIGR03410 80 VPQGREIFPRLTVEENLLTGLAALPRRSRKI-------------PDEIYELFPVlkemlgrrggDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVME 206
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-204 |
4.04e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 134.66 E-value: 4.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL-----ETADSGTFLLDGSPFDPTSSKQQEQV 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFPHLSVMDNITIGPRL--VLKQDKETY--TSKANHLAKLLD-IEELLNNFPYQLSGGQKQRLAIARAMAM 151
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLnrLVKSKKELQerVRWALEKAQLWDeVKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 152 NPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYV 215
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
6-205 |
4.80e-39 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 134.71 E-value: 4.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 6 NVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFD---------PTSSKQQEQV 76
Cdd:PRK10619 10 DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 V----GVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKA-NHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAM 151
Cdd:PRK10619 90 LrtrlTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAvKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510806666 152 NPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVI 223
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
5.95e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 134.73 E-value: 5.95e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFG--SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVG 78
Cdd:PRK13632 7 MIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQ--DFQlFPHLSVMDNITIGprLVLKQ-DKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:PRK13632 87 IIFQnpDNQ-FIGATVEDDIAFG--LENKKvPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKADGV-TQIVVTHDLDfaEEI-GDKVL 205
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMD--EAIlADKVI 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-204 |
1.21e-38 |
|
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: 132.49 E-value: 1.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQ-EQ 75
Cdd:cd03266 1 MITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVKEPAEaRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 VVGVVFQDFQLFPHLSVMDNITIGPRLV-LKQDKetYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPK 154
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYgLKGDE--LTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 155 VLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRV 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-204 |
4.58e-38 |
|
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: 130.80 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQqeQVVGVVF 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLVLKQDKEtytskanhlaklldIEELLNNFPY---------QLSGGQKQRLAIARAMAMN 152
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKR--------------IDEVLDVVGLkdsakkkvkGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRI 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-204 |
1.05e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 136.31 E-value: 1.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ-QEQVVGV 79
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIG--PRLVLKQDKETYTSKanhlaklldIEELLNNFP---------YQLSGGQKQRLAIARA 148
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARAR---------IRELSERYGldvdpdakvEDLSVGEQQRVEILKA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 149 MAMNPKVLAYDEPTSALDPalrQQVASL--IL-ELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG3845 156 LYRGARILILDEPTAVLTP---QEADELfeILrRLAAEGKSIIFITHKLREVMAIADRV 211
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-208 |
1.07e-37 |
|
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: 133.70 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 20 LDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQ----EQVVGVVFQDFQLFPHLSVMDN 95
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 96 ITIGPRlvlKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVAS 175
Cdd:TIGR02142 96 LRYGMK---RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190
....*....|....*....|....*....|....
gi 510806666 176 LILELKAD-GVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:TIGR02142 173 YLERLHAEfGIPILYVSHSLQEVLRLADRVVVLE 206
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-205 |
1.95e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 130.62 E-value: 1.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQL-FPhLSVMDNITIG--PRLVLKQDKETYTSKAnhLAkLLDIEELLNNFPYQLSGGQKQRLAIARAMA------- 150
Cdd:COG4559 81 PQHSSLaFP-FTVEEVVALGraPHGSSAAQDRQIVREA--LA-LVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 151 MNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRIL 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-205 |
3.69e-37 |
|
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: 135.20 E-value: 3.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF-----------GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETAdSGTFLLDGSPFDPTSS 70
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 71 KQQEQV---VGVVFQD-FQ-LFPHLSVMDNITIGprLVLKQDKETYTSKANHLAKLLD----IEELLNNFPYQLSGGQKQ 141
Cdd:COG4172 355 RALRPLrrrMQVVFQDpFGsLSPRMTVGQIIAEG--LRVHGPGLSAAERRARVAEALEevglDPAARHRYPHEFSGGQRQ 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 142 RLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG4172 433 RIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVM 497
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-208 |
4.26e-37 |
|
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: 128.44 E-value: 4.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 21 DLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVVFQDFQLFPHLSVMDNITIGP 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ--SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 101 RLVLKQDKETyTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL 180
Cdd:TIGR01277 96 HPGLKLNAEQ-QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180
....*....|....*....|....*....
gi 510806666 181 KAD-GVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:TIGR01277 175 CSErQRTLLMVTHHLSDARAIASQIAVVS 203
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-204 |
5.53e-37 |
|
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: 128.26 E-value: 5.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTS-SKQQEQVVGVV 80
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVRePREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIGPRLV-LKQDKetYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYgVPGAE--RRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 160 EPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRV 202
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-194 |
6.04e-37 |
|
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: 128.50 E-value: 6.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKK-VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHlSVMDNITIGpRLVLKQDKETYTSKANHLAKLldIEELLNNFPYQ-------LSGGQKQRLAIARAMAMNP 153
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLG-RPNATDEEVIEAAKEAGAHDF--IMKLPNGYDTVlgenggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKaDGVTQIVVTHDL 194
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRL 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-197 |
6.56e-37 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 128.36 E-value: 6.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV 76
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ----VGVVFQDFQLFPHLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:PRK10584 86 rakhVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFA 197
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-205 |
7.52e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 129.47 E-value: 7.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 15 KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQD--FQLFPhLSV 92
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpdDQVFS-STV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 93 MDNITIGPRlVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQ 172
Cdd:PRK13647 98 WDDVAFGPV-NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
|
170 180 190
....*....|....*....|....*....|...
gi 510806666 173 VASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK13647 177 LMEILDRLHNQGKTVIVATHDVDLAAEWADQVI 209
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
7-204 |
8.74e-37 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 130.62 E-value: 8.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 7 VNKSFGSKKV-----INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV---VG 78
Cdd:COG4608 19 VRGGLFGRTVgvvkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQ--LFPHLSVMDNITIGPRLVLKQDKETYTSKAnhlAKLLDI----EELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:COG4608 99 MVFQDPYasLNPRMTVGDIIAEPLRIHGLASKAERRERV---AELLELvglrPEHADRYPHEFSGGQRQRIGIARALALN 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG4608 176 PKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRV 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-205 |
8.77e-37 |
|
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: 127.40 E-value: 8.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSskqqEQVVGVVF 81
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLV-LKqdKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKgLK--KEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 510806666 161 PTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVL 199
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
9-204 |
1.50e-36 |
|
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: 129.43 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 9 KSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQ-EQVVGVVFQDFQLF 87
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAG--YDVVREPRKvRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 88 PHLSVMDNITIGPRL--VLKQDKEtytSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSAL 165
Cdd:TIGR01188 79 EDLTGRENLEMMGRLygLPKDEAE---ERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 510806666 166 DPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRI 194
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-205 |
1.50e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 128.35 E-value: 1.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQL-FPhLSVMDNITIG--PRLVLKQDKETYTSKANHLAkllDIEELLNNFPYQLSGGQKQRLAIARAMA------M 151
Cdd:PRK13548 82 PQHSSLsFP-FTVEEVVAMGraPHGLSRAEDDALVAAALAQV---DLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdG 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 152 NPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIV 212
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
12-205 |
2.00e-36 |
|
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: 133.72 E-value: 2.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKK-VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFPHl 90
Cdd:COG4618 342 GSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 91 SVMDNI----TIGPRLVLKqdketytskAnhlAKLLDIEELLNNFP--YQ---------LSGGQKQRLAIARAMAMNPKV 155
Cdd:COG4618 421 TIAENIarfgDADPEKVVA---------A---AKLAGVHEMILRLPdgYDtrigeggarLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIgDKVL 205
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAV-DKLL 537
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
3.65e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 127.89 E-value: 3.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP--FDPTSSKQQEQVV 77
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQ--DFQLFPHlSVMDNITIGPrLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:PRK13639 81 GIVFQnpDDQLFAP-TVEEDVAFGP-LNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKV 207
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-194 |
5.15e-36 |
|
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: 126.19 E-value: 5.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSFG---SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVG 78
Cdd:cd03253 1 IEFENV--TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFpHLSVMDNITIGPrlVLKQDKETYTSkanhlAKLLDIEELLNNFP--YQ---------LSGGQKQRLAIAR 147
Cdd:cd03253 79 VVPQDTVLF-NDTIGYNIRYGR--PDATDEEVIEA-----AKAAQIHDKIMRFPdgYDtivgerglkLSGGEKQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLILELkADGVTQIVVTHDL 194
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDV-SKGRTTIVIAHRL 196
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
6.24e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 127.23 E-value: 6.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGV 79
Cdd:PRK13652 3 LIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQ--DFQLFPHlSVMDNITIGPrLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:PRK13652 83 VFQnpDDQIFSP-TVEQDIAFGP-INLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 158 YDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYI 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-185 |
1.07e-35 |
|
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: 125.35 E-value: 1.07e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQV---VG 78
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ--DITKLPMHKRArlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHLSVMDNItigpRLVL---KQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:cd03218 79 YLPQEASIFRKLTVEENI----LAVLeirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190
....*....|....*....|....*....|
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKADGV 185
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGI 184
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
2-205 |
1.27e-35 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 126.11 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKK---------VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ 72
Cdd:COG4167 5 LEVRNLSKTFKYRTglfrrqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 73 QEQVVGVVFQDfqlfPHLSVMDNITIG-----P-RLVLKQDKETYTSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLAI 145
Cdd:COG4167 85 RCKHIRMIFQD----PNTSLNPRLNIGqileePlRLNTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVL 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-192 |
1.59e-35 |
|
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: 123.82 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL--ETADSGTFLLDGSPFDPTSSKQQeqvVGVVFQDFQLFPH 89
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDKRSFRKI---IGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 90 LSVmdnitigprlvlkqdKET--YTskanhlAKLldieellnnfpYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDP 167
Cdd:cd03213 97 LTV---------------RETlmFA------AKL-----------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
|
170 180
....*....|....*....|....*
gi 510806666 168 ALRQQVASLILELKADGVTQIVVTH 192
Cdd:cd03213 145 SSALQVMSLLRRLADTGRTIICSIH 169
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-205 |
2.40e-35 |
|
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: 124.50 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQeqvvgVVFQDFQLFPHLSVMDNI 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 97 TIGPRLVLKQDKETYTSKA--NHLAkLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVA 174
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRAIveEHIA-LVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|..
gi 510806666 175 SLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:TIGR01184 155 EELMQIWEEhRVTVLMVTHDVDEALLLSDRVV 186
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-208 |
4.26e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 125.69 E-value: 4.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFdPTSSKQQEQVVGVVF 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-PSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPR---LVLKQDKETytskanhLAKLLDIEELLNNFPYQ---LSGGQKQRLAIARAMAMNPKV 155
Cdd:PRK13537 87 QFDNLDPDFTVRENLLVFGRyfgLSAAAARAL-------VPPLLEFAKLENKADAKvgeLSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIE 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-207 |
5.30e-35 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 129.33 E-value: 5.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHlSVMDNItigpRLVLKQDKETYTSKANHLAKLLD--------IEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:TIGR02857 402 PQHPFLFAG-TIAENI----RLARPDASDAEIREALERAGLDEfvaalpqgLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELkADGVTQIVVTHDLDFAEEIgDKVLKV 207
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALA-DRIVVL 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-205 |
5.63e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.16 E-value: 5.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQ----EQVVGVVFQ--DFQLF 87
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDG--VDITDKKVKlsdiRKKVGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 88 PHlSVMDNITIGPRLVLKQDKETYTS--KANHLAKLlDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSAL 165
Cdd:PRK13637 98 EE-TIEKDIAFGPINLGLSEEEIENRvkRAMNIVGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510806666 166 DPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK13637 176 DPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-194 |
7.09e-35 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 123.42 E-value: 7.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSK---KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVG 78
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPhLSVMDNITIG-PRLVLKQDKETytskanhlAKLLDIEELLNNFPY-----------QLSGGQKQRLAIA 146
Cdd:cd03249 81 LVSQEPVLFD-GTIAENIRYGkPDATDEEVEEA--------AKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 147 RAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAdGVTQIVVTHDL 194
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDRAMK-GRTTIVIAHRL 198
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
1-204 |
1.20e-34 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 126.37 E-value: 1.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFG--------------SKKVI----------NNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSG 56
Cdd:COG4175 3 KIEVRNLYKIFGkrperalklldqgkSKDEIlektgqtvgvNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 57 TFLLDGSpfDPTSSKQQEQV------VGVVFQDFQLFPHLSVMDNITIGprL-VLKQDKETYTSKANHLAKLLDIEELLN 129
Cdd:COG4175 83 EVLIDGE--DITKLSKKELRelrrkkMSMVFQHFALLPHRTVLENVAFG--LeIQGVPKAERRERAREALELVGLAGWED 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 130 NFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG4175 159 SYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKlKKTIVFITHDLDEALRLGDRI 234
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-205 |
2.29e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 124.04 E-value: 2.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSK-----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGT--FLLDGSPFD-------- 66
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTieWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 67 --------PTSSKQQEQV------VGVVFQ--DFQLFPHlSVMDNITIGPRlVLKQDKETYTSKANHLAKLLDI-EELLN 129
Cdd:PRK13651 83 vleklviqKTRFKKIKKIkeirrrVGVVFQfaEYQLFEQ-TIEKDIIFGPV-SMGVSKEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 130 NFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
27-205 |
6.54e-34 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 123.15 E-value: 6.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPF---DPTSSKQQEQVVGVVFQDfqlfPHLSVMDNITIGPRLV 103
Cdd:PRK11308 41 GKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQN----PYGSLNPRKKVGQILE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 104 LKQDKETYTSKANHLAKLLDI-------EELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASL 176
Cdd:PRK11308 117 EPLLINTSLSAAERREKALAMmakvglrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL 196
|
170 180 190
....*....|....*....|....*....|
gi 510806666 177 ILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK11308 197 MMDLQQElGLSYVFISHDLSVVEHIADEVM 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-203 |
1.23e-33 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 121.04 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGtFLLDGSPF-----------DPTSS 70
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG-FRVEGKVTfhgknlyapdvDPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 71 KQQeqvVGVVFQDFQLFPHlSVMDNITIGPRLV-LKQDKETYTSKANHLAKLLD-IEELLNNFPYQLSGGQKQRLAIARA 148
Cdd:PRK14243 90 RRR---IGMVFQKPNPFPK-SIYDNIAYGARINgYKGDMDELVERSLRQAALWDeVKDKLKQSGLSLSGGQQQRLCIARA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTHDLDFAEEIGDK 203
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSDM 219
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-205 |
1.91e-33 |
|
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: 120.30 E-value: 1.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVF 81
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARARRVALVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIG--P-RLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:TIGR03873 82 QDSDTAVPLTVRDVVALGriPhRSLWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:TIGR03873 162 DEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVV 208
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-197 |
2.51e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 119.80 E-value: 2.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIG--P----RLVlKQDKEtYTSKAnhLAkLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPK 154
Cdd:COG4604 81 RQENHINSRLTVRELVAFGrfPyskgRLT-AEDRE-IIDEA--IA-YLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 155 VLAYDEPTSALDP----ALRQQVASLILELkadGVTQIVVTHDLDFA 197
Cdd:COG4604 156 YVLLDEPLNNLDMkhsvQMMKLLRRLADEL---GKTVVIVLHDINFA 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-204 |
2.55e-33 |
|
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: 124.91 E-value: 2.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-----GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTF-------LLDGSPFDPT 68
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 69 SSKQQEQVVGVVFQDFQLFPHLSVMDNIT--IGprlvLKQDKETYTSKANHLAKLLDIEE-----LLNNFPYQLSGGQKQ 141
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTeaIG----LELPDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERH 434
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510806666 142 RLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:TIGR03269 435 RVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRA 498
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
3.19e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 121.11 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSK-----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGT-----------FLLDGSP 64
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiqvgdiyigdkKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 65 FDPTSSK-----QQEQVVGVVFQ--DFQLFPHlSVMDNITIGPrLVLKQDKETYTSKAN-HLAKLLDIEELLNNFPYQLS 136
Cdd:PRK13631 101 TNPYSKKiknfkELRRRVSMVFQfpEYQLFKD-TIEKDIMFGP-VALGVKKSEAKKLAKfYLNKMGLDDSYLERSPFGLS 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 137 GGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVI 247
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-209 |
7.71e-33 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.25 E-value: 7.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFlldgspfdptssKQQEQV-VGV 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV------------KLGETVkIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDF-QLFPHLSVMDNItigpRLVLKQDKETYTSkaNHLAKLLdieellnnFPYQ--------LSGGQKQRLAIARAMA 150
Cdd:COG0488 383 FDQHQeELDPDKTVLDEL----RDGAPGGTEQEVR--GYLGRFL--------FSGDdafkpvgvLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806666 151 MNPKVLAYDEPTSALDPALRQqvaslILE--LKA-DGvTQIVVTHDLDFAEEIGDKVLKVEP 209
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLE-----ALEeaLDDfPG-TVLLVSHDRYFLDRVATRILEFED 504
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-195 |
8.73e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 119.18 E-value: 8.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGS-KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQE--QVV 77
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlrESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQ--DFQLFPhLSVMDNITIGPrLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:PRK13636 85 GMVFQdpDNQLFS-ASVYQDVSFGA-VNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510806666 156 LAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLD 195
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDID 203
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-204 |
8.93e-33 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 121.49 E-value: 8.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQL--------------FPHLSVMDNITIGPRLVLKQDKETyTSKANHLAKLLDieellnnfpyQLSGGQKQRLAIA 146
Cdd:PRK09536 83 PQDTSLsfefdvrqvvemgrTPHRSRFDTWTETDRAAVERAMER-TGVAQFADRPVT----------SLSGGERQRVLLA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 147 RAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDEL 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-202 |
1.16e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 118.26 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGS-----KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQE- 74
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLPEYKr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 -QVVGVVFQDFQL--FPHLSVMDNITI--------GPRL-VLKQDKETYTSKanhLAKL-LDIEELLNNFPYQLSGGQKQ 141
Cdd:COG1101 79 aKYIGRVFQDPMMgtAPSMTIEENLALayrrgkrrGLRRgLTKKRRELFREL---LATLgLGLENRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 142 rlAIARAMAM--NPKVLAYDEPTSALDPalrqQVASLILEL-----KADGVTQIVVTHDLDFAEEIGD 202
Cdd:COG1101 156 --ALSLLMATltKPKLLLLDEHTAALDP----KTAALVLELtekivEENNLTTLMVTHNMEQALDYGN 217
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-208 |
1.23e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.78 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFG-----SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDP-TSSKQQEQ 75
Cdd:PRK13641 3 IKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 V---VGVVFQ--DFQLFPHlSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMA 150
Cdd:PRK13641 83 LrkkVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 151 MNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLE 219
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
12-192 |
1.81e-32 |
|
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: 122.46 E-value: 1.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFPHlS 91
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 92 VMDNITigpRLVLKQDKEtytsKANHLAKLLDIEELLNNFP--YQ---------LSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:TIGR01842 408 VAENIA---RFGENADPE----KIIEAAKLAGVHELILRLPdgYDtvigpggatLSGGQRQRIALARALYGDPKLVVLDE 480
|
170 180 190
....*....|....*....|....*....|..
gi 510806666 161 PTSALDPALRQQVASLILELKADGVTQIVVTH 192
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARGITVVVITH 512
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-208 |
2.41e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.92 E-value: 2.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGS-----KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSS----KQ 72
Cdd:PRK13649 3 INLQNVSYTYQAgtpfeGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 73 QEQVVGVVFQ--DFQLFPHlSVMDNITIGPRL--VLKQDKETYTSKANHLAKLldIEELLNNFPYQLSGGQKQRLAIARA 148
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNfgVSQEEAEALAREKLALVGI--SESLFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLE 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-203 |
4.00e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 117.50 E-value: 4.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 6 NVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETA-----DSGTFLLDG-SPFDPTSSKQQEQVVGV 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGrSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPhLSVMDNITIGPR---LVLKQD-KETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRahkLVPRKEfRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELkADGVTQIVVTHDLDFAEEIGDK 203
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDR 231
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-203 |
7.93e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 116.03 E-value: 7.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL-----ETADSGTFLLDG----SPFDPTSSK 71
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGhniySPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 72 QQEqvVGVVFQDFQLFPhLSVMDNITIGPRLVLKQDKETY---TSKANHLAKLLD-IEELLNNFPYQLSGGQKQRLAIAR 147
Cdd:PRK14239 85 RKE--IGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLdeaVEKSLKGASIWDeVKDRLHDSALGLSGGQQQRVCIAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTHDLDFAEEIGDK 203
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDR 216
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-194 |
1.00e-31 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 121.22 E-value: 1.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSF----GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG---SPFDPTSSKQQe 74
Cdd:TIGR03797 452 IEVDRV--TFryrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGqdlAGLDVQAVRRQ- 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 qvVGVVFQDFQLFPHlSVMDNITIGPRLVLKQDKETytskanhlAKLLDIEELLNNFPYQ-----------LSGGQKQRL 143
Cdd:TIGR03797 529 --LGVVLQNGRLMSG-SIFENIAGGAPLTLDEAWEA--------ARMAGLAEDIRAMPMGmhtvisegggtLSGGQRQRL 597
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 144 AIARAMAMNPKVLAYDEPTSALDPalRQQvASLILELKADGVTQIVVTHDL 194
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALDN--RTQ-AIVSESLERLKVTRIVIAHRL 645
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1-195 |
1.39e-31 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 117.67 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELkNVNKSFGSKKVinNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP-FDptsSKQQEQV--- 76
Cdd:PRK11144 1 MLEL-NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlFD---AEKGICLppe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ---VGVVFQDFQLFPHLSVMDNITIGprlVLKQDKETYtskaNHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:PRK11144 75 krrIGYVFQDARLFPHYKVRGNLRYG---MAKSMVAQF----DKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKADGVTQIV-VTHDLD 195
Cdd:PRK11144 148 ELLLMDEPLASLDLPRKRELLPYLERLAREINIPILyVSHSLD 190
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-199 |
1.99e-31 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 120.21 E-value: 1.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF----GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV 76
Cdd:PRK10535 4 LLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ----VGVVFQDFQLFPHLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:PRK10535 84 rrehFGFIFQRYHLLSHLTAAQNVEV-PAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEE 199
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ 209
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
13-204 |
2.29e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 114.14 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 13 SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV----VGVVFQDFQLFP 88
Cdd:PRK11629 21 QTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 89 HLSVMDNITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPA 168
Cdd:PRK11629 101 DFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAR 179
|
170 180 190
....*....|....*....|....*....|....*..
gi 510806666 169 LRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK11629 180 NADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-200 |
2.58e-31 |
|
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: 114.41 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSG-TFLLDGSPFDPTSS---KQQeqv 76
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVwelRKR--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLF--PHLSVMDNI------TIG-PRLVLKQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIAR 147
Cdd:COG1119 80 IGLVSPALQLRfpRDETVLDVVlsgffdSIGlYREPTDEQRE----RARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIV-VTHDLdfaEEI 200
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHHV---EEI 206
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-204 |
3.58e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 114.06 E-value: 3.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQV---V 77
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT--DLTGLDEHEIArlgI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMDNItigpRLVLKQDKETYTS-----------KANHLAKLLDIEELLNNFPYQLSGGQKQRLAIA 146
Cdd:COG4674 88 GRKFQKPTVFEELTVFENL----ELALKGDRGVFASlfarltaeerdRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 147 RAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGvTQIVVTHDLDFAEEIGDKV 204
Cdd:COG4674 164 MLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKH-SVVVVEHDMEFVRQIARKV 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-197 |
3.95e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.34 E-value: 3.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQdfqlfpHLSVMDNITIgPRLV-------------LKQDKETYTSKANHlakLLDIEELLNNFPYQLSGGQKQRLAIAR 147
Cdd:PRK11231 82 PQ------HHLTPEGITV-RELVaygrspwlslwgrLSAEDNARVNQAME---QTRINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 148 AMAMNPKVLAYDEPTSALDpaLRQQVA--SLILELKADGVTQIVVTHDLDFA 197
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLD--INHQVElmRLMRELNTQGKTVVTVLHDLNQA 201
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-197 |
5.94e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 114.34 E-value: 5.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGV 79
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQ--DFQlFPHLSVMDNITIG------PRlvlkqdkETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAM 151
Cdd:PRK13635 86 VFQnpDNQ-FVGATVQDDVAFGlenigvPR-------EEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 152 NPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFA 197
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSITHDLDEA 204
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
14-205 |
6.83e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.35 E-value: 6.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQ----EQVVGVVFQ--DFQLF 87
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkplRKKVGIVFQfpEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 88 PHlSVMDNITIGPRL--VLKQDKEtytSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSA 164
Cdd:PRK13634 100 EE-TVEKDICFGPMNfgVSEEDAK---QKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 165 LDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIV 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-194 |
6.96e-31 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 113.09 E-value: 6.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKK--VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG---SPFDPTSSKQQeqv 76
Cdd:cd03251 1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvRDYTLASLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFpHLSVMDNITIGPRLVLKQDKEtytsKANHLAKLLD-IEELLNNFP-------YQLSGGQKQRLAIARA 148
Cdd:cd03251 78 IGLVSQDVFLF-NDTVAENIAYGRPGATREEVE----EAARAANAHEfIMELPEGYDtvigergVKLSGGQRQRIAIARA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADGvTQIVVTHDL 194
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNR-TTFVIAHRL 197
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-185 |
8.75e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.82 E-value: 8.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspfdptsskqqEQV---- 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG-----------EDIthlp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 --------VGVVFQDFQLFPHLSVMDNItigpRLVL---KQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAI 145
Cdd:COG1137 72 mhkrarlgIGYLPQEASIFRKLTVEDNI----LAVLelrKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGV 185
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGI 187
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-192 |
2.16e-30 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 111.14 E-value: 2.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspfdpTSSKQQE----- 74
Cdd:cd03245 3 IEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG-----TDIRQLDpadlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 QVVGVVFQDFQLFpHLSVMDNITIGPRLVlkQDKETYTSkanhlAKLLDIEELLNNFP-----------YQLSGGQKQRL 143
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDNITLGAPLA--DDERILRA-----AELAGVTDFVNKHPngldlqigergRGLSGGQRQAV 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510806666 144 AIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTH 192
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGD-KTLIIITH 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-205 |
2.28e-30 |
|
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: 110.21 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ-QEQVVGVVFQDFQ---LFPH 89
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAYVPEDRKregLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 90 LSVMDNITIgprlvlkqdketytskanhlaklldieellnnfPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPAL 169
Cdd:cd03215 93 LSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190
....*....|....*....|....*....|....*.
gi 510806666 170 RQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLLISSELDELLGLCDRIL 175
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
2-204 |
2.77e-30 |
|
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: 110.95 E-value: 2.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFdptsSKQQEQVVGVVF 81
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPW----TRKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLVLKQDketytSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:TIGR03740 77 ESPPLYENLTARENLKVHTTLLGLPD-----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 510806666 162 TSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHI 194
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-208 |
3.00e-30 |
|
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: 111.09 E-value: 3.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF----------------------GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFL 59
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 60 LDG---SPFDptsskqqeqvVGVVFQdfqlfPHLSVMDNITIGPRLVLKQDKETYtskanhlAKLLDIEEL--LNNF--- 131
Cdd:cd03220 81 VRGrvsSLLG----------LGGGFN-----PELTGRENIYLNGRLLGLSRKEID-------EKIDEIIEFseLGDFidl 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 132 PY-QLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:cd03220 139 PVkTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLE 216
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-204 |
3.10e-30 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 114.75 E-value: 3.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV----VGVVFQDFQLFPHLSV 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 93 MDNITIGPRLVLKQDKETyTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQ 172
Cdd:PRK10070 124 LDNTAFGMELAGINAEER-REKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190
....*....|....*....|....*....|...
gi 510806666 173 VASLILELKADGVTQIV-VTHDLDFAEEIGDKV 204
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVfISHDLDEAMRIGDRI 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-208 |
4.36e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.39 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFdPTSSKQQEQVVGVVF 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV-PARARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLVLKQDKETYTSkanhLAKLLD---IEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:PRK13536 121 QFDNLDLEFTVRENLLVFGRYFGMSTREIEAV----IPSLLEfarLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLE 246
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-197 |
5.14e-30 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 111.64 E-value: 5.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSG----------TFLLDGS-PFDPTS 69
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRlARDIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 70 SKQQeqvVGVVFQDFQLFPHLSVMDNITIGP-------RLVLKQdkETYTSKANHLAKLLDIEelLNNFPYQ----LSGG 138
Cdd:PRK09984 84 SRAN---TGYIFQQFNLVNRLSVLENVLIGAlgstpfwRTCFSW--FTREQKQRALQALTRVG--MVHFAHQrvstLSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 139 QKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFA 197
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYA 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-208 |
6.04e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.16 E-value: 6.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFlldgspfdptsSKQQEQVVGVVFQD 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----------SIPKGLRIGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 84 FQLFPHLSVMDNITIG--PRLVLKQDKE-------TYTSKANHLAKLLD-------------IEELLN--NFPY------ 133
Cdd:COG0488 70 PPLDDDLTVLDTVLDGdaELRALEAELEeleaklaEPDEDLERLAELQEefealggweaearAEEILSglGFPEedldrp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 134 --QLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDpalrqqVASLI-LE--LKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:COG0488 150 vsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD------LESIEwLEefLKNYPGTVLVVSHDRYFLDRVATRILELD 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-194 |
6.92e-30 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.96 E-value: 6.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQE----- 74
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGH--DITRLKNREvpflr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 QVVGVVFQDFQLFPHLSVMDNITIgPRLVL---KQDKETYTSKANHLAKLLDIEEllnNFPYQLSGGQKQRLAIARAMAM 151
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAI-PLIIAgasGDDIRRRVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 510806666 152 NPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDL 194
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-205 |
9.12e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 111.64 E-value: 9.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSK-----KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLdGSPFDPTSSKQQEQV 76
Cdd:PRK13645 7 IILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ------VGVVFQ--DFQLFPHlSVMDNITIGPrLVLKQDKETYTSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLAIAR 147
Cdd:PRK13645 86 krlrkeIGLVFQfpEYQLFQE-TIEKDIAFGP-VNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVI 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-204 |
1.01e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 110.52 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL-ETADS-----GTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLF 87
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLiEIYDSkikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 88 PHLSVMDNITIGPRLV-LKQDKETYTSKANHLAKL---LDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHgIKEKREIKKIVEECLRKVglwKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510806666 164 ALDPALRQQVASLILELKADgVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYV 222
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-195 |
1.15e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.98 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGS---KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVV 77
Cdd:PRK13650 4 IIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQ--DFQlFPHLSVMDNITIGprlvLKQ---DKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:PRK13650 84 GMVFQnpDNQ-FVGATVEDDVAFG----LENkgiPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLD 195
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD 202
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-203 |
1.15e-29 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 110.62 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFdPTSSKQQ----EQV 76
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI-PAMSRSRlytvRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVL 156
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 157 AYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDL-------DFAEEIGDK 203
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVpevlsiaDHAYIVADK 220
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-205 |
1.41e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK--VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVG 78
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDfqlfPhlsvmDNITIGPrlVLKQD-----------KETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIAR 147
Cdd:PRK13648 87 IVFQN----P-----DNQFVGS--IVKYDvafglenhavpYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAG 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEiGDKVL 205
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVI 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
12-194 |
2.00e-29 |
|
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: 113.99 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFpHLS 91
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF-DTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 92 VMDNITIGPRLVLKQDKETYTSKA---NHLAKLLD-IEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDP 167
Cdd:TIGR02868 425 VRENLRLARPDATDEELWAALERVglaDWLRALPDgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....*..
gi 510806666 168 ALRQQVASLILElKADGVTQIVVTHDL 194
Cdd:TIGR02868 505 ETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
7-192 |
2.63e-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: 108.51 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 7 VNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETAD---SGTFLLDGSPFDPtssKQQEQVVGVVFQD 83
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP---DQFQKCVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 84 FQLFPHLSVMDNITIGPRLVL---KQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:cd03234 90 DILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 510806666 161 PTSALDPALRQQVASLILELKADGVTQIVVTH 192
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
7-205 |
3.39e-29 |
|
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: 108.57 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 7 VNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPtsSKQQEQVV---GVVF-Q 82
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--LVP--WKRRKKFLrriGVVFgQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 DFQLFPHLSVMDNITIGPRlVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPT 162
Cdd:cd03267 103 KTQLWWDLPVIDSFYLLAA-IYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 510806666 163 SALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVL 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-202 |
3.47e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 109.36 E-value: 3.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQE------- 74
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQNIYERRvnlnrlr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 QVVGVVFQDFQLFPhLSVMDNITIGPRLV---LKQDKETYTSKANHLAKLLD-IEELLNNFPYQLSGGQKQRLAIARAMA 150
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVgwrPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510806666 151 MNPKVLAYDEPTSALDPALRQQVASLI--LELKADgVTQIVVTHDLDFAEEIGD 202
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-194 |
3.81e-29 |
|
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: 108.73 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFG--SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPF---DPTSSKQQeqv 76
Cdd:cd03252 1 ITFEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLalaDPAWLRRQ--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFpHLSVMDNITIGprlvlkqDKETYTSKANHLAKLLDIEELLNNFP--YQ---------LSGGQKQRLAI 145
Cdd:cd03252 78 VGVVLQENVLF-NRSIRDNIALA-------DPGMSMERVIEAAKLAGAHDFISELPegYDtivgeqgagLSGGQRQRIAI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDpalRQQVASLILELKA--DGVTQIVVTHDL 194
Cdd:cd03252 150 ARALIHNPRILIFDEATSALD---YESEHAIMRNMHDicAGRTVIIIAHRL 197
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-205 |
4.42e-29 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 109.01 E-value: 4.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQ---EQVVGVVFQDF--QL 86
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRkafRRDIQMVFQDSisAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 87 FPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSAL 165
Cdd:PRK10419 103 NPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510806666 166 DPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVM 223
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-209 |
5.72e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.88 E-value: 5.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHlSVMDNItIGPRLVLKQDKETyTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:PRK10247 87 AQTPTLFGD-TVYDNL-IFPWQIRNQQPDP-AIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 161 PTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDfaeEI--GDKVLKVEP 209
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKD---EInhADKVITLQP 212
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
15-205 |
5.91e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 110.18 E-value: 5.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 15 KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV---VGVVFQD--FQLFPH 89
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 90 LSVMDNI-----TIGPRLVLKQDKETYTskaNHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSA 164
Cdd:PRK15079 115 MTIGEIIaeplrTYHPKLSRQEVKDRVK---AMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 165 LDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK15079 192 LDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVL 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-205 |
6.21e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.79 E-value: 6.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF----------GS-----------KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFL 59
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkGAlkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 60 LDGspFDPtsSKQQEQVV---GVVF-QDFQLFPHLSVMDNITIgprlvLKQ----DKETYTSKANHLAKLLDIEELLNNF 131
Cdd:COG4586 81 VLG--YVP--FKRRKEFArriGVVFgQRSQLWWDLPAIDSFRL-----LKAiyriPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 132 PYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-206 |
1.30e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.80 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV-VGV 79
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGpRLVLKQ-------DKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIG-RHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDK--VLK 206
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRytVMK 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-209 |
1.38e-28 |
|
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: 104.45 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTflldgspfdptsskqqeqvvgvvf 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 qdfqlfphLSVMDNITIGprlvlkqdketytskanHLAklldieellnnfpyQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:cd03221 57 --------VTWGSTVKIG-----------------YFE--------------QLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 162 TSALDPALRQQVASLILELKAdgvTQIVVTHDLDFAEEIGDKVLKVEP 209
Cdd:cd03221 98 TNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELED 142
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
10-195 |
1.72e-28 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 105.39 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 10 SFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdptsskqqeQVVGVVFQDFQL--- 86
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 87 FPhLSVMDNITIG--PRLVL--KQDKETYTSKANHLAKLlDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPT 162
Cdd:NF040873 70 LP-LTVRDLVAMGrwARRGLwrRLTRDDRAAVDDALERV-GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|...
gi 510806666 163 SALDPALRQQVASLILELKADGVTQIVVTHDLD 195
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTHDLE 180
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-204 |
2.93e-28 |
|
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: 110.68 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADS--GTFLLDGSPFDPTSSKQQEQV-V 77
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMDNITIGPRLVLKQDKETY---TSKANHLAKLLDIEELLNNFPY-QLSGGQKQRLAIARAMAMNP 153
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYnamYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTI 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-205 |
3.69e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.10 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNV------NKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQ- 73
Cdd:PRK13633 4 MIKCKNVsykyesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLw 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 74 --EQVVGVVFQ--DFQLFPHLsVMDNITIGPRLVLKQDKETYTSKANHLaKLLDIEELLNNFPYQLSGGQKQRLAIARAM 149
Cdd:PRK13633 82 diRNKAGMVFQnpDNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESL-KKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEiGDKVL 205
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRII 215
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-208 |
5.87e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.74 E-value: 5.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFG-----SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLdGSPFDPTSSKQQE- 74
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVSSTSKQKEi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 ----QVVGVVFQ--DFQLFPHlSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARA 148
Cdd:PRK13643 80 kpvrKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLE 218
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-209 |
1.95e-27 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 103.42 E-value: 1.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfDPTSSKQQEQVVGVV 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG--DIDDPDVAEACHYLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFqLFPHLSVMDNITIGPRlvLKQDKETYTSKANHLAKLLDIEELlnnfPYQ-LSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:PRK13539 80 HRNA-MKPALTVAENLEFWAA--FLGGEELDIAAALEAVGLAPLAHL----PFGyLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 160 EPTSALDPALRQQVASLILELKADGVTQIVVTH-DLDFAeeiGDKVLKVEP 209
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLP---GARELDLGP 200
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-204 |
2.67e-27 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 107.71 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADS--GTFLLDGSPFDPTSSKQQEQV-V 77
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQASNIRDTERAgI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMDNITIGPRLV---LKQDKETYTSKANHLAKL-LDIEEllnNFP-YQLSGGQKQRLAIARAMAMN 152
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITpggIMDYDAMYLRAQKLLAQLkLDINP---ATPvGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTI 213
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-205 |
3.90e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.24 E-value: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF----------------------GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTF 58
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 59 LLDG---SPFDptsskqqeqvVGVVFQdfqlfPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNfPYQ- 134
Cdd:COG1134 84 EVNGrvsALLE----------LGAGFH-----PELTGRENIYLNGRL-LGLSRKEIDEKFDEIVEFAELGDFIDQ-PVKt 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806666 135 LSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAI 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-195 |
3.99e-27 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 107.30 E-value: 3.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQ-EQVVGVVF 81
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAlAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGpRL-----VLKQDKETYTSKA--NHLAKLLDIEELLNNfpyqLSGGQKQRLAIARAMAMNPK 154
Cdd:PRK11288 86 QELHLVPEMTVAENLYLG-QLphkggIVNRRLLNYEAREqlEHLGVDIDPDTPLKY----LSIGQRQMVEIAKALARNAR 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510806666 155 VLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLD 195
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRME 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
14-206 |
4.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 4.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG-SPFDPTSSKQQEQV---VGVVFQ--DFQLF 87
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVrkrIGMVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 88 PHlSVMDNITIGPRlVLKQDKETYTSKANHLakLLDI---EELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSA 164
Cdd:PRK13646 100 ED-TVEREIIFGPK-NFKMNLDEVKNYAHRL--LMDLgfsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 165 LDPALRQQVASLILELKAD-GVTQIVVTHDLD----FAEEIgdKVLK 206
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNevarYADEV--IVMK 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-192 |
7.51e-27 |
|
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: 107.26 E-value: 7.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG---SPFDPTSSKQQeqv 76
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGvdiRQIDPADLRRN--- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFpHLSVMDNITIGPRLVLKQDketyTSKAnhlAKLLDIEELLNNFP-----------YQLSGGQKQRLAI 145
Cdd:TIGR03375 541 IGYVPQDPRLF-YGTLRDNIALGAPYADDEE----ILRA---AELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVAL 612
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDPALRQQvasLILELKA--DGVTQIVVTH 192
Cdd:TIGR03375 613 ARALLRDPPILLLDEPTSAMDNRSEER---FKDRLKRwlAGKTLVLVTH 658
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-204 |
9.88e-27 |
|
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: 106.31 E-value: 9.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGS----KKVINNLDLVIPDGQILAIVGPSGGGKT----TLLRTLAGLETADSGTFLLDGSPFDPTSSKQ 72
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 73 QEQV----VGVVFQDfqlfPHLS---VMdniTIGprlvlKQDKETYT-----SKANHLAK---LL------DIEELLNNF 131
Cdd:COG4172 86 LRRIrgnrIAMIFQE----PMTSlnpLH---TIG-----KQIAEVLRlhrglSGAAARARaleLLervgipDPERRLDAY 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510806666 132 PYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRV 227
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-205 |
1.21e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.73 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGS---KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVG 78
Cdd:TIGR00958 479 IEFQDVSFSYPNrpdVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVA 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHlSVMDNITIGPRlvlKQDKETYTSkanhLAKLLDIEELLNNFPY-----------QLSGGQKQRLAIAR 147
Cdd:TIGR00958 559 LVGQEPVLFSG-SVRENIAYGLT---DTPDEEIMA----AAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIAR 630
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLileLKADGVTQIVVTHDLDFAEEiGDKVL 205
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVER-ADQIL 684
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-208 |
1.28e-26 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 100.47 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFG--SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDpTSSKQQEQVVGV 79
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVS-DLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFphlsvmdNITIgprlvlkqdketytskanhlaklldieelLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:cd03247 80 LNQRPYLF-------DTTL-----------------------------RNNLGRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510806666 160 EPTSALDPALRQQVASLILELkADGVTQIVVTHDLDFAEEIgDKVLKVE 208
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHLTGIEHM-DKILFLE 170
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
27-205 |
1.36e-26 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 101.47 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKqqeqvVGVVFQ------DFQLFPHLSVMDNIT--I 98
Cdd:TIGR03771 6 GELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRH-----IGYVPQrhefawDFPISVAHTVMSGRTghI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 99 GPrlvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLIL 178
Cdd:TIGR03771 81 GW---LRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFI 157
|
170 180
....*....|....*....|....*..
gi 510806666 179 ELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:TIGR03771 158 ELAGAGTAILMTTHDLAQAMATCDRVV 184
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-194 |
2.25e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.51 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 5 KNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFD--PTSSKQQEQVvGVVFQ 82
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGI-GYLPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 DFQLFPHLSVMDNITigPRLVLKQD--KETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:PRK10895 86 EASIFRRLSVYDNLM--AVLQIRDDlsAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190
....*....|....*....|....*....|....
gi 510806666 161 PTSALDPALRQQVASLILELKADGVTQIVVTHDL 194
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNV 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-208 |
4.08e-26 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 101.22 E-value: 4.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSkQQEQVVGVV 80
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPG-HQIARMGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 --FQDFQLFPHLSVMDNITIGPRLVLK--------------QDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLA 144
Cdd:PRK11300 84 rtFQHVRLFREMTVIENLLVAQHQQLKtglfsgllktpafrRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 145 IARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVN 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-194 |
4.39e-26 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 104.66 E-value: 4.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFpHLSVMDNITIGprlvlkqdKETYTS----KANHLAKLLD-IEELLNNFPY-------QLSGGQKQRLAIARA 148
Cdd:PRK13657 415 FQDAGLF-NRSIEDNIRVG--------RPDATDeemrAAAERAQAHDfIERKPDGYDTvvgergrQLSGGERQRLAIARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKaDGVTQIVVTHDL 194
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRL 530
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-208 |
4.74e-26 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 104.80 E-value: 4.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFG--SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGV 79
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHlSVMDNITIG-PRLVLKQDKETYTSKANhlaklldIEELLNNFP-----------YQLSGGQKQRLAIAR 147
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGrTEQADRAEIERALAAAY-------AQDFVDKLPlgldtpigengVLLSGGQRQRLAIAR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLILELKaDGVTQIVVTHDLDFAEEiGDKVLKVE 208
Cdd:TIGR02203 483 ALLKDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLSTIEK-ADRIVVMD 541
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
14-192 |
1.18e-25 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 103.59 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETAD---SGTFLLDGSPFDptsSKQQEQVVGVVFQDFQLFPHL 90
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID---AKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 91 SVMDNITIGPRLVLKQDKeTYTSKANHLAKLLDIEELLN---------NFPYQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:TIGR00955 115 TVREHLMFQAHLRMPRRV-TKKEKRERVDEVLQALGLRKcantrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|.
gi 510806666 162 TSALDPALRQQVASLILELKADGVTQIVVTH 192
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-205 |
1.52e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.86 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSK---------KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSK 71
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 72 QQEQVVGVVFQD--FQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLAIARA 148
Cdd:PRK15112 84 YRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK15112 164 LILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVL 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
11-197 |
1.70e-25 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 99.68 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 11 FGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFPHL 90
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 91 SVMDNITIG--PRLVL-----KQDKETYTSKanhlAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:PRK10253 97 TVQELVARGryPHQPLftrwrKEDEEAVTKA----MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190
....*....|....*....|....*....|....*
gi 510806666 164 ALDPALRQQVASLILEL-KADGVTQIVVTHDLDFA 197
Cdd:PRK10253 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQA 207
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-208 |
2.45e-25 |
|
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: 102.90 E-value: 2.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFG-SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHlSVMDNITIGPRLVLKQDKetyTSKANHLAKL-LDIEEL-------LNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:TIGR01193 554 PQEPYIFSG-SILENLLLGAKENVSQDE---IWAACEIAEIkDDIENMplgyqteLSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKADgvTQIVVTHDLDFAEEIgDKVLKVE 208
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLD 682
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-203 |
3.85e-25 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 98.03 E-value: 3.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPF-DPTSSKQQEQVVGV 79
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItDWQTAKIMREAVAI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGPRLVlkqDKETYTSKanhlaklldIEELLNNFPY----------QLSGGQKQRLAIARAM 149
Cdd:PRK11614 85 VPEGRRVFSRMTVEENLAMGGFFA---ERDQFQER---------IKWVYELFPRlherriqragTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDK 203
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADR 206
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
16-198 |
3.86e-25 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 97.93 E-value: 3.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 16 VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFPHlSVMDN 95
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR-SLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 96 ITIG------PRLVLKQDKETYTSKANHLAKLLDIEelLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPAL 169
Cdd:cd03248 108 IAYGlqscsfECVKEAAQKAHAHSFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180
....*....|....*....|....*....
gi 510806666 170 RQQVASLILELKADgVTQIVVTHDLDFAE 198
Cdd:cd03248 186 EQQVQQALYDWPER-RTVLVIAHRLSTVE 213
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
4-205 |
6.60e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 99.43 E-value: 6.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNK---SFGSKKV----INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL------ETADSGTFllDGSPFDPTSS 70
Cdd:PRK11022 3 LLNVDKlsvHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypgrVMAEKLEF--NGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 71 KQQEQVVG----VVFQDfqlfPHLSVMDNITIGPRLV--LK----QDKETYTSKANHLAKLLDI---EELLNNFPYQLSG 137
Cdd:PRK11022 81 KERRNLVGaevaMIFQD----PMTSLNPCYTVGFQIMeaIKvhqgGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 138 GQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELqQKENMALVLITHDLALVAEAAHKII 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-205 |
7.48e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.86 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 9 KSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ-QEQvvGVVF-----Q 82
Cdd:COG1129 260 EGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRA--GIAYvpedrK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 DFQLFPHLSVMDNITI------GPRLVLKQDKEtyTSKANHLAKLLDI-----EELLNNfpyqLSGGQKQRLAIARAMAM 151
Cdd:COG1129 338 GEGLVLDLSIRENITLasldrlSRGGLLDRRRE--RALAEEYIKRLRIktpspEQPVGN----LSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 152 NPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDfaEEIG--DKVL 205
Cdd:COG1129 412 DPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELP--ELLGlsDRIL 465
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-208 |
1.74e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 100.26 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLET--ADSGTFL----------------LDGS 63
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 64 PFDPTSSKQQEQVV-----------------GVVFQ-DFQLFPHLSVMDNITIG-PRLVLKQDKETYtsKANHLAKLLDI 124
Cdd:TIGR03269 81 PCPVCGGTLEPEEVdfwnlsdklrrrirkriAIMLQrTFALYGDDTVLDNVLEAlEEIGYEGKEAVG--RAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 125 EELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDK 203
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDK 238
|
....*
gi 510806666 204 VLKVE 208
Cdd:TIGR03269 239 AIWLE 243
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-194 |
2.55e-24 |
|
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: 99.89 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSFG---SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspFDPTSSKQQE--QV 76
Cdd:COG5265 358 VRFENV--SFGydpERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDG--QDIRDVTQASlrAA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFphlsvmdNITIGprlvlkqdketY--------TSKA--NHLAKLLDIEELLNNFP--YQ---------L 135
Cdd:COG5265 434 IGIVPQDTVLF-------NDTIA-----------YniaygrpdASEEevEAAARAAQIHDFIESLPdgYDtrvgerglkL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 136 SGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELkADGVTQIVVTHDL 194
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREV-ARGRTTLVIAHRL 553
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-194 |
2.98e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 99.51 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSFG----SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVV 77
Cdd:PRK11160 339 LTLNNV--SFTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHlSVMDNITIG-PRL-------VLKQDKetytskanhLAKLLDIEELLNNF----PYQLSGGQKQRLAI 145
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAaPNAsdealieVLQQVG---------LEKLLEDDKGLNAWlgegGRQLSGGEQRRLGI 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDPALRQQVASLILELkADGVTQIVVTHDL 194
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRL 534
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
27-204 |
3.50e-24 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 99.54 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV---VGVVFQD--FQLFPHLSVMDNItIGPR 101
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrrdIQFIFQDpyASLDPRQTVGDSI-MEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 102 LV--LKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILE 179
Cdd:PRK10261 429 RVhgLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
|
170 180
....*....|....*....|....*.
gi 510806666 180 LKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK10261 509 LQRDfGIAYLFISHDMAVVERISHRV 534
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-208 |
7.40e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.44 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF-GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDG-SPFDPTSSKQQEQVVG 78
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGiDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQL-FPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLlDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEI-GLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 158 YDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLdfaEEI--GDKVLKVE 208
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNL---EELhdADRIIVMD 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-204 |
8.27e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 98.20 E-value: 8.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV-VGV 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGprlvLKQDKETYTSKANHLAKL---LDIEELLNNfpyqLSGGQKQRLAIARAMAMNPKVL 156
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG----LPKRQASMQKMKQLLAALgcqLDLDSSAGS----LEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 157 AYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRI 210
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
3-192 |
8.75e-24 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.75 E-value: 8.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLE--TADSGTFLLDGSpfDPTSSKQQEQV---V 77
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGE--DILELSPDERAragI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPHLSVMD--NITIGPRLVLKQDKETYTSKANHLAKLLDI-EELLN---NfpYQLSGGQKQRLAIARAMAM 151
Cdd:COG0396 80 FLAFQYPVEIPGVSVSNflRTALNARRGEELSAREFLKLLKEKMKELGLdEDFLDryvN--EGFSGGEKKRNEILQMLLL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 152 NPKVLAYDEPTSALD-PALRqQVASLILELKADGVTQIVVTH 192
Cdd:COG0396 158 EPKLAILDETDSGLDiDALR-IVAEGVNKLRSPDRGILIITH 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-192 |
9.26e-24 |
|
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: 93.58 E-value: 9.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVF 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDfQLFPHLSVMDNITIGPRLVlkQDKETYTSKANHLAKLLDIEELLNNfpyQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:TIGR01189 81 LP-GLKPELSALENLHFWAAIH--GGAQRTIEDALAAVGLTGFEDLPAA---QLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 510806666 162 TSALDPALRQQVASLILELKADGVTQIVVTH 192
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-204 |
9.30e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 97.77 E-value: 9.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ-QEQVVGV 79
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSsQEAGIGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGPRLVLK----QDKETYTSKANHLAKLldieellnNFPY-------QLSGGQKQRLAIARA 148
Cdd:PRK10762 84 IHQELNLIPQLTIAENIFLGREFVNRfgriDWKKMYAEADKLLARL--------NLRFssdklvgELSIGEQQMVEIAKV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDV 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-205 |
1.19e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL---ETADSGTFLLDGSPFDPTSSKQQEQV 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQ--DFQlFPHLSVMDNITIG--PRLVLKQDKETYTSKANHLAKLLDieeLLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:PRK13640 86 VGIVFQnpDNQ-FVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADVGMLD---YIDSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAeEIGDKVL 205
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVL 214
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-205 |
2.15e-23 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 95.18 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF----GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETAD---SGTFLLDGSPFDPTSSKQ- 72
Cdd:PRK09473 12 LLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKEl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 73 ----QEQVvGVVFQDfqlfPHLSVMDNITIGPRL--VLKQDKETYTSKA-NHLAKLLDIEEL------LNNFPYQLSGGQ 139
Cdd:PRK09473 92 nklrAEQI-SMIFQD----PMTSLNPYMRVGEQLmeVLMLHKGMSKAEAfEESVRMLDAVKMpearkrMKMYPHEFSGGM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 140 KQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIV-VTHDLDFAEEIGDKVL 205
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVL 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
11-204 |
2.18e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.30 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 11 FGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDptSSKQQ----EQVVGVVFQD--F 84
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD--YSKRGllalRQQVATVFQDpeQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 85 QLFpHLSVMDNITIGPRlVLKQDKETYTSKANHLAKLLDIEELLNNfPYQ-LSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:PRK13638 89 QIF-YTDIDSDIAFSLR-NLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510806666 164 ALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAV 206
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-204 |
4.43e-23 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 95.95 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQ-EQVVGVVFQ 82
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEAlENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 DFQLFPHLSVMDNITIG--PR--LVLKQDKETYTSKAnhLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:PRK10982 81 ELNLVLQRSVMDNMWLGryPTkgMFVDQDKMYRDTKA--IFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK10982 159 DEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEI 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-208 |
4.51e-23 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 96.24 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKV--INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPF-DPTSSKQQEQVvG 78
Cdd:PRK11176 342 IEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrDYTLASLRNQV-A 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFpHLSVMDNITIGPrlvlkqdKETYT----SKANHLAKLLD-IEELLNNFP-------YQLSGGQKQRLAIA 146
Cdd:PRK11176 421 LVSQNVHLF-NDTIANNIAYAR-------TEQYSreqiEEAARMAYAMDfINKMDNGLDtvigengVLLSGGQRQRIAIA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806666 147 RAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGvTQIVVTHDLDFAEEiGDKVLKVE 208
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKNR-TSLVIAHRLSTIEK-ADEILVVE 552
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-199 |
5.30e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 91.76 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKK-----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdptsskqqeqv 76
Cdd:cd03250 1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQdfqlFPHL---SVMDNITIGPRLvlkqDKETYTS--KANHLAKllDIEEL------------LNnfpyqLSGGQ 139
Cdd:cd03250 68 IAYVSQ----EPWIqngTIRENILFGKPF----DEERYEKviKACALEP--DLEILpdgdlteigekgIN-----LSGGQ 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806666 140 KQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVA-SLILELKADGVTQIVVTHDLDFAEE 199
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH 193
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-192 |
9.64e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 95.26 E-value: 9.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 16 VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGT----------------FLLDGS-------PFDPTSskq 72
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRiarpagarvlflpqrpYLPLGTlreallyPATAEA--- 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 73 qeqvvgvvFQDFQLfphlsvmdnitigpRLVLKQdketytskAN--HLAKLLDIEELLNNfpyQLSGGQKQRLAIARAMA 150
Cdd:COG4178 455 --------FSDAEL--------------REALEA--------VGlgHLAERLDEEADWDQ---VLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 151 MNPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTH 192
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPG-TTVISVGH 542
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-204 |
1.47e-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: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDpTSSKQQEQVVGVVF 81
Cdd:TIGR01257 931 VKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDFQLFPHLSVMDNITIGPRLVLKQDKETYtskanhlaklLDIEELL---------NNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLKGRSWEEAQ----------LEMEAMLedtglhhkrNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASLILELKAdGVTQIVVTHDLDFAEEIGDKV 204
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRI 1130
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-198 |
1.65e-22 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 90.79 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLEtadsgtflldgsPFDPTSSKqqeqvvgVVFQDFQLFPHLSVM 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL------------KGTPVAGC-------VDVPDNQFGREASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 94 DNItiGPRLVLKQDKEtytskANHLAKLLDIEELLNNFPyQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQV 173
Cdd:COG2401 104 DAI--GRKGDFKDAVE-----LLNAVGLSDAVLWLRRFK-ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|....*.
gi 510806666 174 ASLILEL-KADGVTQIVVTHDLDFAE 198
Cdd:COG2401 176 ARNLQKLaRRAGITLVVATHHYDVID 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-205 |
4.39e-22 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 93.37 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 19 NLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLeTADSGTFLLDGSPF---DPTSSKQQEQVVGvvfQDFQLFpHLSVMDN 95
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELrelDPESWRKHLSWVG---QNPQLP-HGTLRDN 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 96 ITIGprlvlkqDKETYTSKANHLAKLLDIEELLNNFP----YQ-------LSGGQKQRLAIARAMAMNPKVLAYDEPTSA 164
Cdd:PRK11174 443 VLLG-------NPDASDEQLQQALENAWVSEFLPLLPqgldTPigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 510806666 165 LDPALRQQVASLILELKAdGVTQIVVTHDLDFAEEIgDKVL 205
Cdd:PRK11174 516 LDAHSEQLVMQALNAASR-RQTTLMVTHQLEDLAQW-DQIW 554
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-208 |
6.89e-22 |
|
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: 92.55 E-value: 6.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKK-----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQV 76
Cdd:COG4615 328 LELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFPHLsvmdnitIGPrlvlkqDKETYTSKANHLAKLLDIEELL----NNF-PYQLSGGQKQRLAIARAMAM 151
Cdd:COG4615 408 FSAVFSDFHLFDRL-------LGL------DGEADPARARELLERLELDHKVsvedGRFsTTDLSQGQRKRLALLVALLE 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806666 152 NPKVLAYDEPTSALDPALR----QQvasLILELKADGVTQIVVTHDlD--FaeEIGDKVLKVE 208
Cdd:COG4615 475 DRPILVFDEWAADQDPEFRrvfyTE---LLPELKARGKTVIAISHD-DryF--DLADRVLKMD 531
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-205 |
1.41e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.02 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFlldgspfdptssKQQEQV-VGV 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLrIGY 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSvmdnITIGPRLVLKQDketyTSKANHLAKLLDIE-ELLNNFPYQ-LSGGQKQRLAIARAMAMNPKVLA 157
Cdd:PRK09544 72 VPQKLYLDTTLP----LTVNRFLRLRPG----TKKEDILPALKRVQaGHLIDAPMQkLSGGETQRVLLARALLNRPQLLV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 158 YDEPTSALDpaLRQQVA--SLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK09544 144 LDEPTQGVD--VNGQVAlyDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVL 192
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
9-192 |
1.61e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 91.86 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 9 KSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADS--GTFLLDGSpfDPTssKQQEQVVGVVFQDFQL 86
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNR--KPT--KQILKRTGFVTQDDIL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 87 FPHLSVMDNITIG-----PRLVLKQDKETYTSKANHLAKLLDIEELL--NNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:PLN03211 152 YPHLTVRETLVFCsllrlPKSLTKQEKILVAESVISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190
....*....|....*....|....*....|...
gi 510806666 160 EPTSALDPALRQQVASLILELKADGVTQIVVTH 192
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-205 |
2.13e-21 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 88.44 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 5 KNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLL---DGSPFDPTSSKQQEQVV---- 77
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYALSEAERRRllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 --GVVFQDFQ--LFPHLSVMDNItiGPRLVlkqdketyTSKANHLAKL-------LDIEEL----LNNFPYQLSGGQKQR 142
Cdd:PRK11701 90 ewGFVHQHPRdgLRMQVSAGGNI--GERLM--------AVGARHYGDIratagdwLERVEIdaarIDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510806666 143 LAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLL 223
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1-204 |
7.79e-21 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 89.46 E-value: 7.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADS--GTFLLDGSPFDPTSSKQQEQVvG 78
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRFKDIRDSEAL-G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVF--QDFQLFPHLSVMDNITIG----PRLVLKQDkETYTSKANHLAKL-LDI--EELLNNfpyqLSGGQKQRLAIARAM 149
Cdd:NF040905 80 IVIihQELALIPYLSIAENIFLGneraKRGVIDWN-ETNRRARELLAKVgLDEspDTLVTD----IGVGKQQLVEIAKAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 150 AMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSI 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-194 |
7.99e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.76 E-value: 7.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTT----LLRTLAGletadSGTFLLDGSPFDPTSSKQQEQV---VGVVFQD- 83
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVrhrIQVVFQDp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 84 -FQLFPHLSVMDNITIG-----PRLVLKQDKETYTSKANHLAklLDiEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:PRK15134 372 nSSLNPRLNVLQIIEEGlrvhqPTLSAAQREQQVIAVMEEVG--LD-PETRHRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190
....*....|....*....|....*....|....*...
gi 510806666 158 YDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDL 194
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDL 486
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-205 |
1.06e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.53 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKT----TLLRTL--AGLETADSGTFLLDGS----PFD 66
Cdd:PRK10261 12 VLAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSrqviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 67 PTSSKQQEQVVG----VVFQD--FQLFPHLSVMDNITIGPRLVLKQDKETYTSKANHLAKLLDI---EELLNNFPYQLSG 137
Cdd:PRK10261 92 EQSAAQMRHVRGadmaMIFQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806666 138 GQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD---GVtqIVVTHDLDFAEEIGDKVL 205
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEmsmGV--IFITHDMGVVAEIADRVL 240
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-192 |
1.89e-20 |
|
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: 83.74 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnkSFGS---KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFlldGSPFDPTSskqqeqvvg 78
Cdd:cd03223 1 IELENL--SLATpdgRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGEDL--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 vvfqdfqLF-PHLSVMdnitigPRLVLKQdketytskanHLAKLLDIEellnnfpyqLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:cd03223 67 -------LFlPQRPYL------PLGTLRE----------QLIYPWDDV---------LSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*
gi 510806666 158 YDEPTSALDPALRQQVASLileLKADGVTQIVVTH 192
Cdd:cd03223 115 LDEATSALDEESEDRLYQL---LKELGITVISVGH 146
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
12-194 |
1.95e-20 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 87.27 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLE------TADSGTF----LLDGSPfdptssKQQEQVVG--- 78
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwhvTADRFRWngidLLKLSP------RERRKIIGrei 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 -VVFQDfqlfPhLSVMD-NITIGPRLVLKQDKETYTS--------KANHLAKLL------DIEELLNNFPYQLSGGQKQR 142
Cdd:COG4170 92 aMIFQE----P-SSCLDpSAKIGDQLIEAIPSWTFKGkwwqrfkwRKKRAIELLhrvgikDHKDIMNSYPHELTEGECQK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 510806666 143 LAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDL 194
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDL 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-197 |
3.07e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.61 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQD 83
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 84 FQLFPHLSVMDNITIG--P------RLVlKQDKEtytsKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:PRK10575 94 LPAAEGMTVRELVAIGryPwhgalgRFG-AADRE----KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 510806666 156 LAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFA 197
Cdd:PRK10575 169 LLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMA 211
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-198 |
4.92e-20 |
|
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: 83.70 E-value: 4.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVF 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 82 QDfQLFPHLSVMDNITIGPRLVLKQDKETYTSKANhlakLLDIEELLNNfpyQLSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:cd03231 81 AP-GIKTTLSVLENLRFWHADHSDEQVEEALARVG----LNGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 510806666 162 TSALDPALRQQVASLILELKADGVTQIVVTH-DLDFAE 198
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMVVLTTHqDLGLSE 190
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-194 |
1.47e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.35 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 26 DGQILAIVGPSGGGKTTLLRTLAGLeTADSGTFLLDGSPFDPTS-----------SKQQEQVVGV-VFQDFQLFPHLSVM 93
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSaaelarhraylSQQQSPPFAMpVFQYLALHQPAGAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 94 DnitigprlvlkqdkETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAM-----AMNP--KVLAYDEPTSALD 166
Cdd:COG4138 100 S--------------EAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLD 165
|
170 180 190
....*....|....*....|....*....|
gi 510806666 167 PAlrQQVA--SLILELKADGVTQIVVTHDL 194
Cdd:COG4138 166 VA--QQAAldRLLRELCQQGITVVMSSHDL 193
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-209 |
1.62e-19 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 85.71 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFlldgspfdptssKQQEQV-VGVV 80
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSENAnIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQD-FQLFPH-LSVMDNITigprlVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:PRK15064 388 AQDhAYDFENdLTLFDWMS-----QWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVM 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 159 DEPTSALDpalRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVEP 209
Cdd:PRK15064 463 DEPTNHMD---MESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITP 510
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-192 |
3.11e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 85.18 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPT--SSKQQeqvVGV 79
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGdiATRRR---VGY 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSVMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:NF033858 344 MSQAFSLYGELTVRQNLELHARL-FHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILD 422
|
170 180 190
....*....|....*....|....*....|....
gi 510806666 160 EPTSALDPALRQQVASLILEL-KADGVTQIVVTH 192
Cdd:NF033858 423 EPTSGVDPVARDMFWRLLIELsREDGVTIFISTH 456
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1-205 |
4.63e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 4.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLV---IPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVV 77
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNGVsfsITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQD-FQLFPHLSVMDNITIG------PRlvlkqdkETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMA 150
Cdd:PRK13642 84 GMVFQNpDNQFVGATVEDDVAFGmenqgiPR-------EEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 151 MNPKVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEiGDKVL 205
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRIL 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
22-194 |
4.94e-19 |
|
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: 82.41 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 22 LVIP-DGQILAIVGPSGGGKTTLLRTLAGLETADSGTF--------LLD---GSPFDPTSSKQQEQVVGVVF--QDFQLF 87
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVIVkpQYVDLI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 88 PHlSVMDNItigpRLVLKQDKETytSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDP 167
Cdd:cd03236 100 PK-AVKGKV----GELLKKKDER--GKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*..
gi 510806666 168 ALRQQVASLILELKADGVTQIVVTHDL 194
Cdd:cd03236 173 KQRLNAARLIRELAEDDNYVLVVEHDL 199
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-166 |
1.09e-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: 83.45 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLL---------DGS--PFDPTSS 70
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvklayvDQSrdALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 71 KQQEQVVGvvfqdfqlfphlsvMDNITIGPRLVlkqDKETYTSKANHlaKLLDIEELLNnfpyQLSGGQKQRLAIARAMA 150
Cdd:TIGR03719 403 VWEEISGG--------------LDIIKLGKREI---PSRAYVGRFNF--KGSDQQKKVG----QLSGGERNRVHLAKTLK 459
|
170
....*....|....*.
gi 510806666 151 MNPKVLAYDEPTSALD 166
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLD 475
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-192 |
2.28e-18 |
|
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: 79.11 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLE--TADSGTFLLDGSpfDPTSSKQQEQV--- 76
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGE--DITDLPPEERArlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 VGVVFQDFQLFPHLSVMDnitigprlvlkqdketytskanhlaklldieeLLNNFPYQLSGGQKQRLAIARAMAMNPKVL 156
Cdd:cd03217 79 IFLAFQYPPEIPGVKNAD--------------------------------FLRYVNEGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190
....*....|....*....|....*....|....*..
gi 510806666 157 AYDEPTSALD-PALRqQVASLILELKADGVTQIVVTH 192
Cdd:cd03217 127 ILDEPDSGLDiDALR-LVAEVINKLREEGKSVLIITH 162
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-195 |
4.10e-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: 79.07 E-value: 4.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGV 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHlSVMDNItiGP---------RLVLK--QDKETYTSKANHLAklLDIEELLNNFpyqlSGGQKQRLAIARA 148
Cdd:cd03244 83 IPQDPVLFSG-TIRSNL--DPfgeysdeelWQALErvGLKEFVESLPGGLD--TVVEEGGENL----SVGQRQLLCLARA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADgVTQIVVTHDLD 195
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKD-CTVLTIAHRLD 199
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
24-208 |
6.11e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 6.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 24 IPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPfdpTSSKQQEQVVGVVFQDFQL---FPHLsVMDNITIGP 100
Cdd:PRK15056 30 VPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP---TRQALQKNLVAYVPQSEEVdwsFPVL-VEDVVMMGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 101 -------RLVLKQDKETYTSKanhLAKLlDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQV 173
Cdd:PRK15056 106 yghmgwlRRAKKRDRQIVTAA---LARV-DMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190
....*....|....*....|....*....|....*
gi 510806666 174 ASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK15056 182 ISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-204 |
6.69e-18 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 80.23 E-value: 6.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSF----GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLeTADSGTFLLDGSPFDPT-----SSK 71
Cdd:PRK15093 3 LLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIdllrlSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 72 QQEQVVG----VVFQDFQlfphlSVMD-NITIGPRLVlkQDKETYTSKAN----------------HLAKLLDIEELLNN 130
Cdd:PRK15093 82 ERRKLVGhnvsMIFQEPQ-----SCLDpSERVGRQLM--QNIPGWTYKGRwwqrfgwrkrraiellHRVGIKDHKDAMRS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 131 FPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KADGVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKI 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-194 |
7.75e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 80.92 E-value: 7.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGS-KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:PRK10790 341 IDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDfqlfPHL---SVMDNITIGPRlvLKQDKETYTSKANHLAKLL-----DIEELLNNFPYQLSGGQKQRLAIARAMAMN 152
Cdd:PRK10790 421 QQD----PVVladTFLANVTLGRD--ISEEQVWQALETVQLAELArslpdGLYTPLGEQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 153 PKVLAYDEPTSALDPALRQQVASlILELKADGVTQIVVTHDL 194
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQ-ALAAVREHTTLVVIAHRL 535
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-205 |
1.17e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 78.22 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 24 IPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGspfDPTSSKQQEqvvgvVFQDFQLfphlSVMDnitigprLV 103
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIEL---DTVSYKPQY-----IKADYEG----TVRD-------LL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 104 LKQDKETYTSK--ANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLI--LE 179
Cdd:cd03237 83 SSITKDFYTHPyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIrrFA 162
|
170 180
....*....|....*....|....*.
gi 510806666 180 LKADGvTQIVVTHDLDFAEEIGDKVL 205
Cdd:cd03237 163 ENNEK-TAFVVEHDIIMIDYLADRLI 187
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-205 |
1.41e-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: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVN-KSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQ-QEQVVGVV 80
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQ---LFPHLSVMDNITIGprlvlKQDKETYTS-------KANHLAklldiEELLNNF------PYQ----LSGGQK 140
Cdd:COG3845 339 PEDRLgrgLVPDMSVAENLILG-----RYRRPPFSRggfldrkAIRAFA-----EELIEEFdvrtpgPDTparsLSGGNQ 408
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 141 QRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIA 473
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-193 |
1.72e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.02 E-value: 1.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKV-INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVV 80
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNITIGPRLVlkqDKETYTSKANHLAKLLDiEELLNnfpYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:PRK10522 403 FTDFHLFDQLLGPEGKPANPALV---EKWLERLKMAHKLELED-GRISN---LKLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190
....*....|....*....|....*....|....
gi 510806666 161 PTSALDPALRQQVASLIL-ELKADGVTQIVVTHD 193
Cdd:PRK10522 476 WAADQDPHFRREFYQVLLpLLQEMGKTIFAISHD 509
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
27-205 |
3.86e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.80 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVvGVVF--QDFQ---LFPHLSVMDNITIGPR 101
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRA-GIMLcpEDRKaegIIPVHSVADNINISAR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 102 -------LVLKQDKETYTskANHLAKLLDI-----EELLNNfpyqLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPAL 169
Cdd:PRK11288 358 rhhlragCLINNRWEAEN--ADRFIRSLNIktpsrEQLIMN----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190
....*....|....*....|....*....|....*...
gi 510806666 170 RQQVASLILELKADGVTQIVVTHDLdfAEEIG--DKVL 205
Cdd:PRK11288 432 KHEIYNVIYELAAQGVAVLFVSSDL--PEVLGvaDRIV 467
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-205 |
3.98e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLeTADSGTFLLDGSPFDPTS-----------SKQQEQVVGV-VFQDFQLfpHLSVMD 94
Cdd:PRK03695 22 GEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSaaelarhraylSQQQTPPFAMpVFQYLTL--HQPDKT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 95 NITIGPRLVlkqdketytskaNHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAM-----AMNP--KVLAYDEPTSALDP 167
Cdd:PRK03695 99 RTEAVASAL------------NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDV 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 510806666 168 AlrQQVA--SLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK03695 167 A--QQAAldRLLSELCQQGIAVVMSSHDLNHTLRHADRVW 204
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-207 |
5.10e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 79.01 E-value: 5.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSK---KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAG-LETADSGTFLLDGSpfdptsskqqeqvV 77
Cdd:PLN03130 615 ISIKNGYFSWDSKaerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRGT-------------V 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFpHLSVMDNITIGprlvLKQDKETYtSKANHLAKL---LDI----------EELLNnfpyqLSGGQKQRLA 144
Cdd:PLN03130 682 AYVPQVSWIF-NATVRDNILFG----SPFDPERY-ERAIDVTALqhdLDLlpggdlteigERGVN-----ISGGQKQRVS 750
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806666 145 IARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIgDKVLKV 207
Cdd:PLN03130 751 MARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILV 812
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-204 |
6.85e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.21 E-value: 6.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKT-TLLRTLAGLETAD----SGTFLLDGSPFDPTSSKQQEQVVG----VVFQDf 84
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 85 qlfPHLSVMDNITIGPRL--VLKQDKETYTSKANhlAKLLDIEEL---------LNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:PRK15134 101 ---PMVSLNPLHTLEKQLyeVLSLHRGMRREAAR--GEILNCLDRvgirqaakrLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRV 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
22-194 |
8.52e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 77.93 E-value: 8.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 22 LVIP-DGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPfdptsskqqEQVV----GVVFQDFqlFPHLSvmDN- 95
Cdd:PRK13409 93 LPIPkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSW---------DEVLkrfrGTELQNY--FKKLY--NGe 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 96 ---------ITIGPRLV-------LKQDKETytSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:PRK13409 160 ikvvhkpqyVDLIPKVFkgkvrelLKKVDER--GKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*
gi 510806666 160 EPTSALDPALRQQVASLILELkADGVTQIVVTHDL 194
Cdd:PRK13409 238 EPTSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL 271
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-192 |
8.82e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.23 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFdptsSKQQEQvvgvv 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI----RRQRDE----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLF--------PHLSVMDNITIGPRLVLKQDKETYtskANHLAK--LLDIEELLNNfpyQLSGGQKQRLAIARAMA 150
Cdd:PRK13538 72 YHQDLLYlghqpgikTELTALENLRFYQRLHGPGDDEAL---WEALAQvgLAGFEDVPVR---QLSAGQQRRVALARLWL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 510806666 151 MNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTH 192
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-207 |
1.21e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.71 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSK---KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAG-LETADSGTFLLDGSpfdptsskqqeqvV 77
Cdd:PLN03232 615 ISIKNGYFSWDSKtskPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVIRGS-------------V 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFpHLSVMDNITIGPrlvlKQDKETYtskanhlAKLLDIEEL---LNNFP-----------YQLSGGQKQRL 143
Cdd:PLN03232 682 AYVPQVSWIF-NATVRENILFGS----DFESERY-------WRAIDVTALqhdLDLLPgrdlteigergVNISGGQKQRV 749
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510806666 144 AIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIgDKVLKV 207
Cdd:PLN03232 750 SMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILV 812
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-58 |
1.54e-16 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 1.54e-16
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTF 58
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
22-194 |
4.82e-16 |
|
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: 75.98 E-value: 4.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 22 LVIP-DGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdptsskqQEQVVGVvFQDFQLFPHLSVMDNITIG- 99
Cdd:COG1245 93 LPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPS---------WDEVLKR-FRGTELQDYFKKLANGEIKv 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 100 ----------PRLV-------LKQDKETytSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPT 162
Cdd:COG1245 163 ahkpqyvdliPKVFkgtvrelLEKVDER--GKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170 180 190
....*....|....*....|....*....|..
gi 510806666 163 SALDPALRQQVASLILELKADGVTQIVVTHDL 194
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-205 |
5.57e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.62 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETADSGTFLldgspFDPT-SSKQQEqvvgvVFQDFqlfpHLSVMDnitigprlVLK 105
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-----PELKiSYKPQY-----IKPDY----DGTVED--------LLR 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 106 QDKETYTSK--ANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KA 182
Cdd:PRK13409 423 SITDDLGSSyyKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaEE 502
|
170 180
....*....|....*....|...
gi 510806666 183 DGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK13409 503 REATALVVDHDIYMIDYISDRLM 525
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-205 |
8.00e-16 |
|
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: 75.25 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL-ETADSGTFLLDGSPFDPTSSKQQ-EQVVGVVFQDFQ---LFP 88
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVDIRNPAQAiRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 89 HLSVMDNITIGprlVLkqDKETYTSKANHLAKLLDIEELLNNF------PY----QLSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:TIGR02633 353 ILGVGKNITLS---VL--KSFCFKMRIDAAAELQIIGSAIQRLkvktasPFlpigRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVL 474
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-205 |
1.41e-15 |
|
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: 74.44 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdpTSSKQQEqvvgvVFQDFQLfphlSVMDNITigprlvlKQ 106
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK----ISYKPQY-----ISPDYDG----TVEEFLR-------SA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 107 DKETYTSKA--NHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL-KAD 183
Cdd:COG1245 426 NTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFaENR 505
|
170 180
....*....|....*....|..
gi 510806666 184 GVTQIVVTHDLDFAEEIGDKVL 205
Cdd:COG1245 506 GKTAMVVDHDIYLIDYISDRLM 527
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
3.26e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.75 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVv 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 fqdfqlfPHLSvmdniTIGPRLVLKQD--KETYTSKAN----HLAKLLDIEELLnNFPYQ-LSGGQKQRLAIARAMAMNP 153
Cdd:PRK13540 80 -------GHRS-----GINPYLTLRENclYDIHFSPGAvgitELCRLFSLEHLI-DYPCGlLSSGQKRQVALLRLWMSKA 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 510806666 154 KVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTH 192
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-205 |
3.26e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 19 NLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVvGVVF--QDFQ---LFPHLSVM 93
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLAR-GLVYlpEDRQssgLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 94 DNI---TIG-PRLVLKQDKETYTSKANHLA---KLLDIEELLNNfpyqLSGGQKQRLAIARAMAMNPKVLAYDEPTSALD 166
Cdd:PRK15439 360 WNVcalTHNrRGFWIKPARENAVLERYRRAlniKFNHAEQAART----LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190
....*....|....*....|....*....|....*....
gi 510806666 167 PALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVL 474
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
17-204 |
4.04e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 4.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKT----TLLRTL-AGLeTADSGTFLLDGSPFDPTSSKQQEqvVGVVFQDFQ-LFPHL 90
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILpAGV-RQTAGRVLLDGKPVAPCALRGRK--IATIMQNPRsAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 91 SVMDNITIGPRLVL-KQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARA-MAMNPKVLAyDEPTSALDPA 168
Cdd:PRK10418 96 HTMHTHARETCLALgKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALAlLCEAPFIIA-DEPTTDLDVV 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 510806666 169 LRQQVASLILELKAD-GVTQIVVTHDLDFAEEIGDKV 204
Cdd:PRK10418 175 AQARILDLLESIVQKrALGMLLVTHDMGVVARLADDV 211
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-196 |
7.13e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 70.44 E-value: 7.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKTTLL-RTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQ--LFPHLSVM 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQkpWLLNATVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 94 DNITIGPRLvlkqDKETYTSKANHLAKLLDIEEL-------LNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALD 166
Cdd:cd03290 97 ENITFGSPF----NKQRYKAVTDACSLQPDIDLLpfgdqteIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190
....*....|....*....|....*....|..
gi 510806666 167 PALRQQV--ASLILELKADGVTQIVVTHDLDF 196
Cdd:cd03290 173 IHLSDHLmqEGILKFLQDDKRTLVLVTHKLQY 204
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
9-189 |
1.13e-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: 69.60 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 9 KSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAG-LETADS--GTFLLDGSPFDPTSSKQQEQVVGVVFQDFQ 85
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrTEGNVSveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 86 lFPHLSVmdnitigprlvlkqdKETytskanhlaklLDIEELL--NNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:cd03233 95 -FPTLTV---------------RET-----------LDFALRCkgNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180
....*....|....*....|....*..
gi 510806666 164 ALDPALRQQVASLILEL-KADGVTQIV 189
Cdd:cd03233 148 GLDSSTALEILKCIRTMaDVLKTTTFV 174
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-205 |
1.30e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.50 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGL-ETADSGTFLLDGSPFDPTSSKQQ-EQVVGVVFQD---FQLFP 88
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKPVKIRNPQQAiAQGIAMVPEDrkrDGIVP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 89 HLSVMDNITIGprlVLkqDKETYTSKANHLAKLLDIEELLNNF------PYQ----LSGGQKQRLAIARAMAMNPKVLAY 158
Cdd:PRK13549 355 VMGVGKNITLA---AL--DRFTGGSRIDDAAELKTILESIQRLkvktasPELaiarLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 510806666 159 DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLdfAEEIG--DKVL 205
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSEL--PEVLGlsDRVL 476
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-192 |
1.93e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 71.20 E-value: 1.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLrtlaGLETAD-----------------SGTFLLDgsp 64
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLITGDhpqgysndltlfgrrrgSGETIWD--- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 65 fdptsSKQQeqvVGVVFQDFqlfpHL------SVMDNI------TIGprlVLKQDKETYTSKANHLAKLLDIEELLNNFP 132
Cdd:PRK10938 334 -----IKKH---IGYVSSSL----HLdyrvstSVRNVIlsgffdSIG---IYQAVSDRQQKLAQQWLDILGIDKRTADAP 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806666 133 YQ-LSGGQkQRLA-IARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIV-VTH 192
Cdd:PRK10938 399 FHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSH 460
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
7-191 |
3.31e-14 |
|
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: 68.04 E-value: 3.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 7 VNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETAD--SGTFLLDGSPFDPTSSKqqeqVVGVVFQDF 84
Cdd:cd03232 13 VPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDKNFQR----STGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 85 QLFPHLSVMDNITIGprlvlkqdketytskanhlAKLLDieellnnfpyqLSGGQKQRLAIARAMAMNPKVLAYDEPTSA 164
Cdd:cd03232 89 VHSPNLTVREALRFS-------------------ALLRG-----------LSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180
....*....|....*....|....*..
gi 510806666 165 LDPALRQQVASLILELKADGVTqIVVT 191
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQA-ILCT 164
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
17-194 |
3.44e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSkQQEQVVGVVF--QDFQ---LFPHLS 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSP-QDGLANGIVYisEDRKrdgLVLGMS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 92 VMDNITI---------GPRLVLKQDKETytskANHLAKLLDI-----EELLNNfpyqLSGGQKQRLAIARAMAMNPKVLA 157
Cdd:PRK10762 347 VKENMSLtalryfsraGGSLKHADEQQA----VSDFIRLFNIktpsmEQAIGL----LSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190
....*....|....*....|....*....|....*..
gi 510806666 158 YDEPTSALDPALRQQVASLILELKADGVTQIVVTHDL 194
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEM 455
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
54-192 |
3.77e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 3.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 54 DSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFpHLSVMDNITIGPRLVLKQDketyTSKANHLAKLLD-IEELLNNF- 131
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATRED----VKRACKFAAIDEfIESLPNKYd 1349
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 132 ----PY--QLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILEL--KADGvTQIVVTH 192
Cdd:PTZ00265 1350 tnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADK-TIITIAH 1417
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
13-194 |
5.43e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 69.74 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 13 SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFPHlSV 92
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 93 MDNITIGPRLVLKQDKEtytskanHLAKLLDIEELLNNFP--YQ---------LSGGQKQRLAIARAMAMNPKVLAYDEP 161
Cdd:PRK10789 406 ANNIALGRPDATQQEIE-------HVARLASVHDDILRLPqgYDtevgergvmLSGGQKQRISIARALLLNAEILILDDA 478
|
170 180 190
....*....|....*....|....*....|...
gi 510806666 162 TSALDPALRQQVASlILELKADGVTQIVVTHDL 194
Cdd:PRK10789 479 LSAVDGRTEHQILH-NLRQWGEGRTVIISAHRL 510
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-194 |
5.52e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKK---VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLL-DGSPFDPTSSKQQEQVV 77
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 78 GVVFQDFQLFPH-----------------------------------------------LSVMDNITIGPRLV-LKQDKE 109
Cdd:PTZ00265 463 GVVSQDPLLFSNsiknnikyslyslkdlealsnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNELIeMRKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 110 TYT-SKANHLAKLLDIEELLNNFP-----------YQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLI 177
Cdd:PTZ00265 543 TIKdSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250
....*....|....*...
gi 510806666 178 LELKA-DGVTQIVVTHDL 194
Cdd:PTZ00265 623 NNLKGnENRITIIIAHRL 640
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-196 |
1.08e-13 |
|
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: 69.20 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdptsskqqeqvVGVVFQDfQLFPHLSVMDNI 96
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQ-AWIQNDSLRENI 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 97 TIGPRLvlkqDKETYTSKANHLAKLLDIEEL-------LNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPAL 169
Cdd:TIGR00957 720 LFGKAL----NEKYYQQVLEACALLPDLEILpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795
|
170 180
....*....|....*....|....*....
gi 510806666 170 RQQVASLILELKA--DGVTQIVVTHDLDF 196
Cdd:TIGR00957 796 GKHIFEHVIGPEGvlKNKTRILVTHGISY 824
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-194 |
1.81e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.27 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNkSFGSKKViNNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSS----KQQEQVVG 78
Cdd:PRK09700 267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPldavKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHLSVMDNITIGPRL----------VLKQDKETYTSKANHlaKLLDIE-ELLNNFPYQLSGGQKQRLAIAR 147
Cdd:PRK09700 345 ESRRDNGFFPNFSIAQNMAISRSLkdggykgamgLFHEVDEQRTAENQR--ELLALKcHSVNQNITELSGGNQQKVLISK 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 148 AMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDL 194
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSEL 469
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-167 |
2.73e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 16 VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdPTSSKQQEQVVGVVFQDFQLFPHLSVMDN 95
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806666 96 ITIGPRLVLKQDKETyTSKANHLAKLLDIEELLNNfpyQLSGGQKQRLAIARaMAMNPKVL-AYDEPTSALDP 167
Cdd:PRK13543 103 LHFLCGLHGRRAKQM-PGSALAIVGLAGYEDTLVR---QLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDL 170
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
13-204 |
3.25e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 13 SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETAD--------SGTFLLDGSPFDPTSSKQQEQVVGVVFQDF 84
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 85 Q-LFPhLSVMDNITIGPRLVLKQDKETYTSK---ANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAM--------- 151
Cdd:PRK13547 93 QpAFA-FSAREIVLLGRYPHARRAGALTHRDgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 152 NPKVLAYDEPTSALDPALRQQVASLILELKAD---GVTQIVvtHDLDFAEEIGDKV 204
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwnlGVLAIV--HDPNLAARHADRI 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
3-166 |
1.30e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGSKK----VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETA---DSGTFLLDGSPFDPTSSK---- 71
Cdd:TIGR00956 761 HWRNLTYEVKIKKekrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRsigy 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 72 -QQeqvvgvvfQDFQLfPHLSVMDNITIGPRL-----VLKQDKETYTSKanhLAKLLDIEEL---LNNFPYQ-LSGGQKQ 141
Cdd:TIGR00956 841 vQQ--------QDLHL-PTSTVRESLRFSAYLrqpksVSKSEKMEYVEE---VIKLLEMESYadaVVGVPGEgLNVEQRK 908
|
170 180
....*....|....*....|....*.
gi 510806666 142 RLAIARAMAMNPKVLAY-DEPTSALD 166
Cdd:TIGR00956 909 RLTIGVELVAKPKLLLFlDEPTSGLD 934
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-205 |
1.54e-12 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 63.59 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSK--KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGV 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHlSVMDNITIGPRLvlkQDKETYTSkanhlaklLDIEELLNNfpyqLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDEY---SDEEIYGA--------LRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 160 EPTSALDPALRQQVASLILELKADgVTQIVVTHDL----DFaeeigDKVL 205
Cdd:cd03369 151 EATASIDYATDALIQKTIREEFTN-STILTIAHRLrtiiDY-----DKIL 194
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-192 |
2.52e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLE--TADSGTFLLDGSP---FDPTSSKQQE- 74
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESildLEPEERAHLGi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 75 --------QVVGVVFQDF--------QLFPHLSVMDNIT----IGPRLVLKQDKETYTSKanhlaklldieellnNFPYQ 134
Cdd:CHL00131 87 flafqypiEIPGVSNADFlrlaynskRKFQGLPELDPLEfleiINEKLKLVGMDPSFLSR---------------NVNEG 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 135 LSGGQKQRLAIARAMAMNPKVLAYDEPTSALD-PALRqQVASLILELKADGVTQIVVTH 192
Cdd:CHL00131 152 FSGGEKKRNEILQMALLDSELAILDETDSGLDiDALK-IIAEGINKLMTSENSIILITH 209
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
2-209 |
4.27e-12 |
|
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: 62.62 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnKSFGSKKVINNLDLvipdgqILAIVGPSGGGKTTLLRtlaGLETADSGTFLL--DGSPFDPTSSKQQEqVVGV 79
Cdd:cd03240 4 LSIRNI-RSFHERSEIEFFSP------LTLIVGQNGAGKTTIIE---ALKYALTGELPPnsKGGAHDPKLIREGE-VRAQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFP--------HLSVMDNITIgprlvLKQDketytskanhlakllDIEELLNNFPYQLSGGQKQ------RLAI 145
Cdd:cd03240 73 VKLAFENANgkkytitrSLAILENVIF-----CHQG---------------ESNWPLLDMRGRCSGGEKVlasliiRLAL 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDPA-LRQQVASLILELKADGVTQ-IVVTHDLDFAEEIgDKVLKVEP 209
Cdd:cd03240 133 AETFGSNCGILALDEPTTNLDEEnIEESLAEIIEERKSQKNFQlIVITHDEELVDAA-DHIYRVEK 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-196 |
6.32e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.82 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFL----LDGSPFDptsskqQEQVvg 78
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgtkLEVAYFD------QHRA-- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 vvfqdfQLFPHLSVMDNITIGprlvlKQDKETYTSKANHLAKLLDieeLLnnFPYQ--------LSGGQKQRLAIARAMA 150
Cdd:PRK11147 393 ------ELDPEKTVMDNLAEG-----KQEVMVNGRPRHVLGYLQD---FL--FHPKramtpvkaLSGGERNRLLLARLFL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 510806666 151 MNPKVLAYDEPTSALDpalrqqVASLIL--ELKAD--GvTQIVVTHDLDF 196
Cdd:PRK11147 457 KPSNLLILDEPTNDLD------VETLELleELLDSyqG-TVLLVSHDRQF 499
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-198 |
8.61e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 63.61 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGT-FLLDGspfDPTSSKQQEQV---- 76
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRvEVLGG---DMADARHRRAVcpri 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ------VGVvfqdfQLFPHLSVMDNITIGPRLvLKQDKETYTSKanhlaklldIEELLNN---FPY------QLSGGQKQ 141
Cdd:NF033858 79 aympqgLGK-----NLYPTLSVFENLDFFGRL-FGQDAAERRRR---------IDELLRAtglAPFadrpagKLSGGMKQ 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 142 RLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKAD--GVTQIVVTHDLDFAE 198
Cdd:NF033858 144 KLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAE 202
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2-208 |
1.16e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 62.83 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGG--KTTLLRTLAGLET-----------ADSGTFLLDGSPFDPT 68
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAgrrpwrf*twcANRRALRRTIG*HRPV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 69 SSKQQEQVVGvvfqdfqlfphlsvMDNITIGPRLvLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARA 148
Cdd:NF000106 94 R*GRRESFSG--------------RENLYMIGR*-LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 149 MAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVID 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
27-166 |
1.48e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETAD--SGTFLLDGSPfdptssKQQE---QVVGVVFQDFQLFPHLSVMDNITIG-- 99
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP------KKQEtfaRISGYCEQNDIHSPQVTVRESLIYSaf 979
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806666 100 ---PRLVLKQDKETYTSKANHLAKLLDIEELLNNFP--YQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALD 166
Cdd:PLN03140 980 lrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
13-168 |
2.91e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 13 SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLA----GLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQlFP 88
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVH-FP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 89 HLSVMDNITIGPRLVLKQ------DKETYtskANHLAKL------LDI---EELLNNFPYQLSGGQKQRLAIARAMAMNP 153
Cdd:TIGR00956 152 HLTVGETLDFAARCKTPQnrpdgvSREEY---AKHIADVymatygLSHtrnTKVGNDFVRGVSGGERKRVSIAEASLGGA 228
|
170
....*....|....*
gi 510806666 154 KVLAYDEPTSALDPA 168
Cdd:TIGR00956 229 KIQCWDNATRGLDSA 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-193 |
3.55e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.49 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSFGSKK-VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETadsgtflldgsPFDPTSSKQQEQVVGVVFQ 82
Cdd:TIGR03719 7 MNRVSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-----------DFNGEARPQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 DFQLFPHLSVMDNITIG-PRLVLKQDK------------ETYTSKANHLAKLLDIEELLN--NFPYQ------------- 134
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGvAEIKDALDRfneisakyaepdADFDKLAAEQAELQEIIDAADawDLDSQleiamdalrcppw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 135 ------LSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPalrQQVASLILELKADGVTQIVVTHD 193
Cdd:TIGR03719 156 dadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA---ESVAWLERHLQEYPGTVVAVTHD 217
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-192 |
5.57e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.19 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLE--TADSGTFLLDGSpfDPTSSKQQEQVVG 78
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGK--DLLELSPEDRAGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQ-----------LFPHLSVmdNITIGPRLVLKQDKETYTSKANHLAKLLDIEE--LLNNFPYQLSGGQKQRLAI 145
Cdd:PRK09580 79 GIFMAFQypveipgvsnqFFLQTAL--NAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTH 192
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-199 |
6.09e-11 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.87 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKTTLLrtLAGLETadSGTFLLDGSPfdPTSSKQQeqvvgVVFQDfqlfpHLSVMDNI 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV--NEGLYA--SGKARLISFL--PKFSRNK-----LIFID-----QLQFLIDV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 97 TIGpRLVLKQDKETytskanhlaklldieellnnfpyqLSGGQKQRLAIARAMAMNPK--VLAYDEPTSALDPALRQQVA 174
Cdd:cd03238 75 GLG-YLTLGQKLST------------------------LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLL 129
|
170 180
....*....|....*....|....*
gi 510806666 175 SLILELKADGVTQIVVTHDLDFAEE 199
Cdd:cd03238 130 EVIKGLIDLGNTVILIEHNLDVLSS 154
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-201 |
9.92e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.41 E-value: 9.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 21 DLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQlfphlsvMDNITIGP 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNN-------TDMLSPGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 101 ----RLVLK--QDKETYTSKANHLAKLLDIEELLNN-FPYqLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQV 173
Cdd:PRK10938 96 ddtgRTTAEiiQDEVKDPARCEQLAQQFGITALLDRrFKY-LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
|
170 180 190
....*....|....*....|....*....|..
gi 510806666 174 ASLILELKADGVTQIVVT---HDL-DFAEEIG 201
Cdd:PRK10938 175 AELLASLHQSGITLVLVLnrfDEIpDFVQFAG 206
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-192 |
1.13e-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: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 15 KVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETAdsgtflldgspFDPTSSKQQEQVVGVVFQDfqlfPHLSV-- 92
Cdd:TIGR00954 466 VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPV-----------YGGRLTKPAKGKLFYVPQR----PYMTLgt 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 93 -MDNItIGPRLVLKQDKETYTSKanHLAKLLDIEELLN------------NFPYQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:TIGR00954 531 lRDQI-IYPDSSEDMKRRGLSDK--DLEQILDNVQLTHilereggwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|...
gi 510806666 160 EPTSALDPALRQQVASLileLKADGVTQIVVTH 192
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRL---CREFGITLFSVSH 637
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-171 |
1.35e-10 |
|
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: 60.31 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADsGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLF---- 87
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFsgtf 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 88 -----PHLSVMDN--ITIGPRLVLKQDKETYTSKANHlaklldieeLLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:TIGR01271 1309 rknldPYEQWSDEeiWKVAEEVGLKSVIEQFPDKLDF---------VLVDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379
|
170
....*....|.
gi 510806666 161 PTSALDPALRQ 171
Cdd:TIGR01271 1380 PSAHLDPVTLQ 1390
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-166 |
1.49e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLD-----------------GS 63
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqdpprnveGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 64 PFDPTSSKQQEQvvGVVFQDFQLFPHLSVMD----NITIGPRLVLKQDKET---YTSKANH-LAKL-LDIEELLNnfpyQ 134
Cdd:PRK11147 83 VYDFVAEGIEEQ--AEYLKRYHDISHLVETDpsekNLNELAKLQEQLDHHNlwqLENRINEvLAQLgLDPDAALS----S 156
|
170 180 190
....*....|....*....|....*....|..
gi 510806666 135 LSGGQKQRLAIARAMAMNPKVLAYDEPTSALD 166
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-205 |
2.58e-10 |
|
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: 58.33 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 16 VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGS-PFDPTSSkqqeqvvgvvfqdfQLFPHlSVMD 94
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRiSFSSQFS--------------WIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 95 NITIGprlvLKQDKETYTSkanhLAKLLDIEELLNNFPYQ-----------LSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:cd03291 117 NIIFG----VSYDEYRYKS----VVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 510806666 164 ALDPALRQQV-ASLILELKADGvTQIVVTHDLDFAeEIGDKVL 205
Cdd:cd03291 189 YLDVFTEKEIfESCVCKLMANK-TRILVTSKMEHL-KKADKIL 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-205 |
9.02e-10 |
|
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: 57.61 E-value: 9.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 16 VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGS-PFDPTSSkqqeqvvgvvfqdfQLFPHlSVMD 94
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRiSFSPQTS--------------WIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 95 NITIGprlvLKQDKETYTSkanhLAKLLDIEELLNNFPYQ-----------LSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:TIGR01271 506 NIIFG----LSYDEYRYTS----VIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 510806666 164 ALDPALRQQV-ASLILELKADGvTQIVVTHDLDFAEEiGDKVL 205
Cdd:TIGR01271 578 HLDVVTEKEIfESCLCKLMSNK-TRILVTSKLEHLKK-ADKIL 618
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-208 |
1.77e-09 |
|
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: 54.89 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 23 VIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdptsskqqeqvvgvvfqdfqlfphlsvmdNITIGPRL 102
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI-------------------------------TPVYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 103 VlkqdketytskanhlaklldieellnnfpyQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKA 182
Cdd:cd03222 70 I------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170 180
....*....|....*....|....*..
gi 510806666 183 DGV-TQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:cd03222 120 EGKkTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
13-200 |
2.06e-09 |
|
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: 56.56 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 13 SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKqqeqvvgvVFQDFQLFPHLSV 92
Cdd:TIGR01257 1951 SSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISD--------VHQNMGYCPQFDA 2022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 93 MDNITIG-PRLVLKQDKETYTSK-----ANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALD 166
Cdd:TIGR01257 2023 IDDLLTGrEHLYLYARLRGVPAEeiekvANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMD 2102
|
170 180 190
....*....|....*....|....*....|....
gi 510806666 167 PALRQQVASLILELKADGVTQIVVTHDLDFAEEI 200
Cdd:TIGR01257 2103 PQARRMLWNTIVSIIREGRAVVLTSHSMEECEAL 2136
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
7-209 |
2.58e-09 |
|
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: 53.90 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 7 VNKSFGSKKVINNLDLviPDGQILAIVGPSGGGKTTLLRTLAGLetadsgtFLLDGSPFDPTSSKQQEQVVGVVfqdfQL 86
Cdd:cd03227 3 VLGRFPSYFVPNDVTF--GEGSLTIITGPNGSGKSTILDAIGLA-------LGGAQSATRRRSGVKAGCIVAAV----SA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 87 FPHLSVMdnitigprlvlkqdketytskanhlaklldieellnnfpyQLSGGQKQRLAIARAMA---MNPKVL-AYDEPT 162
Cdd:cd03227 70 ELIFTRL----------------------------------------QLSGGEKELSALALILAlasLKPRPLyILDEID 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 510806666 163 SALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIgDKVLKVEP 209
Cdd:cd03227 110 RGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELA-DKLIHIKK 155
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-196 |
3.32e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 53.53 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETADSGTFL-LDGSPFDPTSSKQQEQVvgvvfqdfqlfphlsvmdnitigprlvlk 105
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLI----------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 106 qdketytskanhlaklldieeLLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQV------ASLILE 179
Cdd:smart00382 53 ---------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLllleelRLLLLL 111
|
170
....*....|....*..
gi 510806666 180 LKADGVTQIVVTHDLDF 196
Cdd:smart00382 112 KSEKNLTVILTTNDEKD 128
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
13-194 |
3.83e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 13 SKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGS-PFDPtsskQQEQVVGVvfqdfqlfphlS 91
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSiAYVP----QQAWIMNA-----------T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 92 VMDNItigprLVLKQDKETYTSKANHLAKL-LDIEELLNNFPYQ-------LSGGQKQRLAIARAMAMNPKVLAYDEPTS 163
Cdd:PTZ00243 737 VRGNI-----LFFDEEDAARLADAVRVSQLeADLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190
....*....|....*....|....*....|.
gi 510806666 164 ALDPALRQQVASLILELKADGVTQIVVTHDL 194
Cdd:PTZ00243 812 ALDAHVGERVVEECFLGALAGKTRVLATHQV 842
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-194 |
8.06e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 17 INNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSP-FDPTSSKQQEQVVGVvfqdfqlfphlsvmDN 95
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAaLIAISSGLNGQLTGI--------------EN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 96 ITIgPRLVLKQDKETYTSKANHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVAS 175
Cdd:PRK13545 106 IEL-KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
|
170
....*....|....*....
gi 510806666 176 LILELKADGVTQIVVTHDL 194
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSL 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-208 |
2.46e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.25 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGS-----PFDPTSSKQQEQ 75
Cdd:PRK10636 1 MIVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlawVNQETPALPQPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 76 VVGVVFQDF---QLFPHLSVMDNITIGPRLVLKQDKE------TYTSKANHLAKLLDI-EELLNNFPYQLSGGQKQRLAI 145
Cdd:PRK10636 81 LEYVIDGDReyrQLEAQLHDANERNDGHAIATIHGKLdaidawTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 510806666 146 ARAMAMNPKVLAYDEPTSALDPAlrqqvASLILE--LKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK10636 161 AQALICRSDLLLLDEPTNHLDLD-----AVIWLEkwLKSYQGTLILISHDRDFLDPIVDKIIHIE 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-195 |
2.75e-08 |
|
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: 52.55 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSF--GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADsGTFLLDGSPFDPTSSKQQEQVVGV 79
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPhlsvmdnitiGPrlvLKQDKETYTSKANH----LAKLLDIEELLNNFP-----------YQLSGGQKQRLA 144
Cdd:cd03289 82 IPQKVFIFS----------GT---FRKNLDPYGKWSDEeiwkVAEEVGLKSVIEQFPgqldfvlvdggCVLSHGHKQLMC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 510806666 145 IARAMAMNPKVLAYDEPTSALDPaLRQQVASLILELKADGVTQIVVTHDLD 195
Cdd:cd03289 149 LARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIE 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-195 |
4.66e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 4 LKNVNKSFGSKKVInnLDLV----IPDGQIlAIVGPSGGGKTTLLRTLAGLETADSG-TFLLDGSPfdptsskqqeqvVG 78
Cdd:PRK11819 9 MNRVSKVVPPKKQI--LKDIslsfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPGIK------------VG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQDFQLFPHLSVMDNITIG-PRLVLKQDK--ETYTSKANHLA---KLLD----IEELLNNF----------------- 131
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVEEGvAEVKAALDRfnEIYAAYAEPDAdfdALAAeqgeLQEIIDAAdawdldsqleiamdalr 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 510806666 132 --PY-----QLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPalrQQVASLILELKADGVTQIVVTHD---LD 195
Cdd:PRK11819 154 cpPWdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPGTVVAVTHDryfLD 224
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-193 |
2.47e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 50.24 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 12 GSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLdgSPFDPTSSKQQEQVVGVvfqDFQLFPHLS 91
Cdd:PLN03073 520 GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR--SAKVRMAVFSQHHVDGL---DLSSNPLLY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 92 VMDNITIGPRLVLKQdketytskanHLAKLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDpalRQ 171
Cdd:PLN03073 595 MMRCFPGVPEQKLRA----------HLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD---LD 661
|
170 180
....*....|....*....|....
gi 510806666 172 QVASLI--LELKADGVtqIVVTHD 193
Cdd:PLN03073 662 AVEALIqgLVLFQGGV--LMVSHD 683
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-177 |
5.44e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 5.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFgSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdpTSSKQQEQVVGVV 80
Cdd:PRK13541 1 MLSLHQLQFNI-EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNC----NINNIAKPYCTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 81 FQDFQLFPHLSVMDNitigprlvLKQDKETYTS-----KANHLAKLLDieeLLNNFPYQLSGGQKQRLAIARAMAMNPKV 155
Cdd:PRK13541 76 GHNLGLKLEMTVFEN--------LKFWSEIYNSaetlyAAIHYFKLHD---LLDEKCYSLSSGMQKIVAIARLIACQSDL 144
|
170 180
....*....|....*....|..
gi 510806666 156 LAYDEPTSALDPALRQQVASLI 177
Cdd:PRK13541 145 WLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-193 |
5.59e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 1 MIELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTF-LLDGSPFDPTSSKQQEqvvgV 79
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGYFAQHQLE----F 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 80 VFQDFQLFPHLSvmdniTIGPRLVLKQDKETYTSKANHLAKLLDIEEllnnfpyQLSGGQKQRLAIARAMAMNPKVLAYD 159
Cdd:PRK10636 388 LRADESPLQHLA-----RLAPQELEQKLRDYLGGFGFQGDKVTEETR-------RFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190
....*....|....*....|....*....|....
gi 510806666 160 EPTSALDPALRQQVASLILELkaDGVTqIVVTHD 193
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALIDF--EGAL-VVVSHD 486
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
2-194 |
6.26e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 6.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVnKSFGSKKVInnlDLvipDGQILAIVGPSGGGKTTLLRTLagletadsgTFLLDGSPFdpTSSKQQEQV----- 76
Cdd:COG0419 5 LRLENF-RSYRDTETI---DF---DDGLNLIVGPNGAGKSTILEAI---------RYALYGKAR--SRSKLRSDLinvgs 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 77 ----VGVVFQ-------------DFQLFPHLS------VMDNITIGPRL-----VLKQDKETYTSKANHLAKLLDIE-EL 127
Cdd:COG0419 67 eeasVELEFEhggkryrierrqgEFAEFLEAKpserkeALKRLLGLEIYeelkeRLKELEEALESALEELAELQKLKqEI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 510806666 128 LNNF-----PYQLSGGQKQRLAIARAMAMnpkVLayDepTSALDPALRQQVASLILELKadgvtqiVVTHDL 194
Cdd:COG0419 147 LAQLsgldpIETLSGGERLRLALADLLSL---IL--D--FGSLDEERLERLLDALEELA-------IITHVI 204
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-196 |
8.12e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 2 IELKNVNKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAgletadsgTFLLDGSPFDPTSSKQQEQVVG--- 78
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA--------MHAIDGIPKNCQILHVEQEVVGddt 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 79 VVFQ--------------------------DFQLFPHLSVMDNIT------IGPRL--VLKQ----DKETYTSKANH-LA 119
Cdd:PLN03073 250 TALQcvlntdiertqlleeeaqlvaqqrelEFETETGKGKGANKDgvdkdaVSQRLeeIYKRleliDAYTAEARAASiLA 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 120 KLLDIEELLNNFPYQLSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPAlrqqvASLILE--LKADGVTQIVVTHDLDF 196
Cdd:PLN03073 330 GLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLH-----AVLWLEtyLLKWPKTFIVVSHAREF 403
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-195 |
1.41e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 16 VINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSPFDPTSSKQQEQVVGVVFQDFQLFphlSVMDN 95
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLF---SGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 96 ITIGPrlvLKQDKETYTSKANHLAKLLDIeelLNNFPYQL-----------SGGQKQRLAIARAMAMNPKVLAYDEPTSA 164
Cdd:PLN03232 1328 FNIDP---FSEHNDADLWEALERAHIKDV---IDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190
....*....|....*....|....*....|.
gi 510806666 165 LDPALRQQVASLILElKADGVTQIVVTHDLD 195
Cdd:PLN03232 1402 VDVRTDSLIQRTIRE-EFKSCTMLVIAHRLN 1431
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-208 |
1.73e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 47.12 E-value: 1.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 5 KNVNKSFGSkkvINNLDLVIPDGQILAIVGPSGGGKTTLLRTLAGLETADSGTFLLDGSpfdptsskqqeqvVGVVFQDF 84
Cdd:PRK13546 31 KHKNKTFFA---LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVIAISA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 85 QLFPHLSVMDNITIGPRLVLKQDKETytskANHLAKLLDIEELlNNFPYQ----LSGGQKQRLAIARAMAMNPKVLAYDE 160
Cdd:PRK13546 95 GLSGQLTGIENIEFKMLCMGFKRKEI----KAMTPKIIEFSEL-GEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 161 PTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVLKVE 208
Cdd:PRK13546 170 ALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIE 217
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
132-208 |
9.13e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 9.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 132 PYQLSGGQKQ------RLAIARAMA--------MNPKVLayDEPTSALDPALRQQVASLILELKADGVTQI-VVTHDldf 196
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAegiegdapLPPLIL--DEPTVFLDSGHVSQLVDLVESMRRLGVEQIvVVSHD--- 853
|
90
....*....|....
gi 510806666 197 AEEIG--DKVLKVE 208
Cdd:PRK02224 854 DELVGaaDDLVRVE 867
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-195 |
1.62e-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: 44.17 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 19 NLDLVIPDGQILAIVGPSGGGKTTLlrtlagletadsgtflldgsPFDPTSSKQQEQVVGVVFQDF-QLFPHLSV--MDN 95
Cdd:cd03270 13 NVDVDIPRNKLVVITGVSGSGKSSL--------------------AFDTIYAEGQRRYVESLSAYArQFLGQMDKpdVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 96 IT-IGPRLVLKQDKETYTSKA----------------------NHLAKLLDI--EEL-LNNFPYQLSGGQKQRLAIARAM 149
Cdd:cd03270 73 IEgLSPAIAIDQKTTSRNPRStvgtvteiydylrllfarvgirERLGFLVDVglGYLtLSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 510806666 150 AMNPKVLAY--DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLD 195
Cdd:cd03270 153 GSGLTGVLYvlDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDED 200
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
3-209 |
5.56e-05 |
|
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: 42.64 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 3 ELKNVNkSFGSKKVINNLDLviPDGQILAIVGPSGGGKTTLLrtlagletaDSGTFLLDGSpfdpTSSKQQEQVVGVVFQ 82
Cdd:cd03279 7 ELKNFG-PFREEQVIDFTGL--DNNGLFLICGPTGAGKSTIL---------DAITYALYGK----TPRYGRQENLRSVFA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 83 DFQLFphLSVMDNITIGPRL-----VLKQDKETYTSKAnhlakLL---DIEELLNNFPYQLSGGQKQRLAIARAMAMNpK 154
Cdd:cd03279 71 PGEDT--AEVSFTFQLGGKKyrverSRGLDYDQFTRIV-----LLpqgEFDRFLARPVSTLSGGETFLASLSLALALS-E 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 155 VLAY-----------DEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIgDKVLKVEP 209
Cdd:cd03279 143 VLQNrggarlealfiDEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERI-PQRLEVIK 207
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
134-191 |
7.03e-05 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 42.25 E-value: 7.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806666 134 QLSGGQKQRLAIARAMAMN-----PKVLaYDEPTSALDPALRQQVASLILELkADGvTQIVVT 191
Cdd:cd03272 158 QLSGGQKSLVALALIFAIQkcdpaPFYL-FDEIDAALDAQYRTAVANMIKEL-SDG-AQFITT 217
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
136-201 |
8.53e-05 |
|
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: 42.73 E-value: 8.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 510806666 136 SGGQKQ------RLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQ-----IVVTHDLDFAEEIG 201
Cdd:TIGR00606 1201 SAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSRSQQrnfqlLVITHDEDFVELLG 1277
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
135-205 |
3.46e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 40.87 E-value: 3.46e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510806666 135 LSGGQKQRLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAEEIGDKVL 205
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIL 462
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-191 |
8.82e-04 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 39.12 E-value: 8.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 14 KKVINNLDLVIPDGQILAIVGPSGGGKTTLlrTLAGLETAD--SGTFLLDGSPFDPTSSKQQEQVVGVVFQD-------- 83
Cdd:cd03288 34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSL--SLAFFRMVDifDGKIVIDGIDISKLPLHTLRSRLSIILQDpilfsgsi 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 84 -FQLFPHLSVMDNiTIGPRLVLKQDKETYTSKANHLAKLldIEELLNNFpyqlSGGQKQRLAIARAMAMNPKVLAYDEPT 162
Cdd:cd03288 112 rFNLDPECKCTDD-RLWEALEIAQLKNMVKSLPGGLDAV--VTEGGENF----SVGQRQLFCLARAFVRKSSILIMDEAT 184
|
170 180
....*....|....*....|....*....
gi 510806666 163 SALDPALRQQVASLILELKADgvtQIVVT 191
Cdd:cd03288 185 ASIDMATENILQKVVMTAFAD---RTVVT 210
|
|
| ABC_MSH6_euk |
cd03286 |
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA ... |
8-48 |
1.75e-03 |
|
ATP-binding cassette domain of eukaryotic MutS6 homolog; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family possess C-terminal domain with a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213253 [Multi-domain] Cd Length: 218 Bit Score: 38.18 E-value: 1.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 510806666 8 NKSFGSKKVINNLDLVIPDGQILAIVGPSGGGKTTLLRTLA 48
Cdd:cd03286 11 NASTASSFVPNDVDLGATSPRILVLTGPNMGGKSTLLRTVC 51
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
27-59 |
1.84e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 38.69 E-value: 1.84e-03
10 20 30
....*....|....*....|....*....|...
gi 510806666 27 GQILAIVGPSGGGKTTLLRTLAGLETADSGTFL 59
Cdd:COG3899 311 GELVLVSGEAGIGKSRLVRELARRARARGGRVL 343
|
|
| ABC_MutS_homologs |
cd03243 |
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair ... |
9-48 |
2.10e-03 |
|
ATP-binding cassette domain of MutS homologs; The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213210 [Multi-domain] Cd Length: 202 Bit Score: 37.61 E-value: 2.10e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 510806666 9 KSFGSKKVINNlDLVIPDGQILAIVGPSGGGKTTLLRTLA 48
Cdd:cd03243 12 ALTKGETFVPN-DINLGSGRLLLITGPNMGGKSTYLRSIG 50
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
132-194 |
2.72e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.75 E-value: 2.72e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 132 PYQLSGGQKQ---RLAIARAMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDL 194
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSP 299
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1-44 |
2.79e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.07 E-value: 2.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 510806666 1 MIELKNVNKsfgskkviNNL---DLVIPDGQILAIVGPSGGGKTTLL 44
Cdd:TIGR00630 613 FLTLKGARE--------NNLkniTVSIPLGLFTCITGVSGSGKSTLI 651
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-209 |
4.52e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 133 YQLSGGQKQRLAIAR---AMAMNPKVLAYDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLDFAeEIGDKVLKVEP 209
Cdd:PRK00635 808 SSLSGGEIQRLKLAYellAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVV-KVADYVLELGP 886
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
20-192 |
5.21e-03 |
|
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 36.46 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 20 LDLVIPDG-QILAIVGPSGGGKTTLLRTLaGLET--ADSGTFLldgsPFDPTSSkqqeqvvgvvfqdfqlfphLSVMDNI 96
Cdd:cd03280 20 LDIQLGENkRVLVITGPNAGGKTVTLKTL-GLLTlmAQSGLPI----PAAEGSS-------------------LPVFENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510806666 97 --TIGPRLVLKQDKETYTSkanHLAKLLDIeellnnfpyqLSGGQKQRLAIaramamnpkvlaYDEPTSALDPALRQQVA 174
Cdd:cd03280 76 faDIGDEQSIEQSLSTFSS---HMKNIARI----------LQHADPDSLVL------------LDELGSGTDPVEGAALA 130
|
170
....*....|....*....
gi 510806666 175 SLILE-LKADGVTQIVVTH 192
Cdd:cd03280 131 IAILEeLLERGALVIATTH 149
|
|
| SpoIIIAA |
COG3854 |
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ... |
20-48 |
5.57e-03 |
|
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443063 Cd Length: 309 Bit Score: 37.05 E-value: 5.57e-03
10 20 30
....*....|....*....|....*....|.
gi 510806666 20 LDLVIPDGQILA--IVGPSGGGKTTLLRTLA 48
Cdd:COG3854 131 LPYIISGGRIYNtlIISPPGCGKTTLLRDIA 161
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
26-72 |
5.72e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 35.78 E-value: 5.72e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 510806666 26 DGQILAIVGPSGGGKTTLLRTL-AGLETADSGTFLLDgsPFDPTSSKQ 72
Cdd:pfam13401 4 GAGILVLTGESGTGKTTLLRRLlEQLPEVRDSVVFVD--LPSGTSPKD 49
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
135-202 |
5.77e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.50 E-value: 5.77e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 510806666 135 LSGGQKQRLAIARAMAMNPKVLAY--DEPTSALDPALRQQVASLILELKADGVTQIVVTHD---LDFAEEIGD 202
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGITYilDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIID 549
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
30-87 |
6.70e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 36.42 E-value: 6.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 510806666 30 LAIVGPSGGGKTTLLRTLA-------GLETADSGTFLLDgspFDPTSSKQQ----EQVVGVVFQDFQLF 87
Cdd:cd04170 2 IALVGHSGSGKTTLAEALLyatgaidRLGRVEDGNTVSD---YDPEEKKRKmsieTSVAPLEWNGHKIN 67
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
29-48 |
7.20e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 36.36 E-value: 7.20e-03
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
135-195 |
9.46e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 36.05 E-value: 9.46e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510806666 135 LSGGQKQRLAIARAMAMNPK-----VLayDEPTSALDPALRQQVASLILELKADGVTQIVVTHDLD 195
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRSTgktlyIL--DEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD 233
|
|
| |
